Heterogeneous Electron-Transfer Dynamics through Dipole-Bridge Groups.

PubMed

Nieto-Pescador, Jesus; Abraham, Baxter; Li, Jingjing; Batarseh, Alberto; Bartynski, Robert A; Galoppini, Elena; Gundlach, Lars

2016-01-14

Heterogeneous electron transfer (HET) between photoexcited molecules and colloidal TiO 2 has been investigated for a set of Zn-porphyrin chromophores attached to the semiconductor via linkers that allow to change level alignment by 200 meV by reorientation of the dipole moment. These unique dye molecules have been studied by femtosecond transient absorption spectroscopy in solution and adsorbed on the TiO 2 colloidal film in vacuum. In solution energy transfer from the excited chromophore to the dipole group has been identified as a slow relaxation pathway competing with S 2 -S 1 internal conversion. On the film heterogeneous electron transfer occurred in 80 fs, much faster compared to all intramolecular pathways. Despite a difference of 200 meV in level alignment of the excited state with respect to the semiconductor conduction band, identical electron transfer times were measured for different linkers. The measurements are compared to a quantum-mechanical model that accounts for electronic-vibronic coupling and finite band width for the acceptor states. We conclude that HET occurs into a distribution of transition states that differs from regular surface states or bridge mediated states.

Quantum Electron Tunneling in Respiratory Complex I1

PubMed Central

Hayashi, Tomoyuki; Stuchebrukhov, Alexei A.

2014-01-01

We have simulated the atomistic details of electronic wiring of all Fe/S clusters in complex I, a key enzyme in the respiratory electron transport chain. The tunneling current theory of many-electron systems is applied to the broken-symmetry (BS) states of the protein at the ZINDO level. One-electron tunneling approximation is found to hold in electron tunneling between the anti-ferromagnetic binuclear and tetranuclear Fe/S clusters with moderate induced polarization of the core electrons. Calculated tunneling energy is about 3 eV higher than Fermi level in the band gap of the protein, which supports that the mechanism of electron transfer is quantum mechanical tunneling, as in the rest of electron transport chain. Resulting electron tunneling pathways consist of up to three key contributing protein residues between neighboring Fe/S clusters. A distinct signature of the wave properties of electrons is observed as quantum interferences when multiple tunneling pathways exist. In N6a-N6b, electron tunnels along different pathways depending on the involved BS states, suggesting possible fluctuations of the tunneling pathways driven by the local protein environment. The calculated distance dependence of the electron transfer rates with internal water molecules included are in good agreement with a reported phenomenological relation. PMID:21495666

Water-mediated electron transfer between protein redox centers.

PubMed

Migliore, Agostino; Corni, Stefano; Felice, Rosa Di; Molinari, Elisa

2007-04-12

Recent experimental and theoretical investigations show that water molecules between or near redox partners can significantly affect their electron-transfer (ET) properties. Here we study the effects of intervening water molecules on the electron self-exchange reaction of azurin (Az), by performing a conformational sampling on the water medium and by using a newly developed ab initio method to calculate transfer integrals between molecular redox sites. We show that the insertion of water molecules at the interface between the copper active sites of Az dimers slightly increases the overall ET rate, while some favorable water conformations can considerably enhance the ET kinetics. These features are traced back to the interplay of two competing factors: the electrostatic interaction between the water and protein subsystems (mainly opposing the ET process for the water arrangements drawn from MD simulations) and the effectiveness of water in mediating ET coupling pathways. Such an interplay provides a physical basis for the found absence of correlation between the electronic couplings derived through ab initio electronic structure calculations and the related quantities obtained through the Empirical Pathways (EP) method. In fact, the latter does not account for electrostatic effects on the transfer integrals. Thus, we conclude that the water-mediated electron tunneling is not controlled by the geometry of a single physical pathway. We discuss the results in terms of the interplay between different ET pathways controlled by the conformational changes of one of the water molecules via its electrostatic influence. Finally, we examine the dynamical effects of the interfacial water and check the validity of the Condon approximation.

Transforming exoelectrogens for biotechnology using synthetic biology.

PubMed

TerAvest, Michaela A; Ajo-Franklin, Caroline M

2016-04-01

Extracellular electron transfer pathways allow certain bacteria to transfer energy between intracellular chemical energy stores and extracellular solids through redox reactions. Microorganisms containing these pathways, exoelectrogens, are a critical part of microbial electrochemical technologies that aim to impact applications in bioenergy, biosensing, and biocomputing. However, there are not yet any examples of economically viable microbial electrochemical technologies due to the limitations of naturally occurring exoelectrogens. Here we first briefly summarize recent discoveries in understanding extracellular electron transfer pathways, then review in-depth the creation of customized and novel exoelectrogens for biotechnological applications. We analyze engineering efforts to increase current production in native exoelectrogens, which reveals that modulating certain processes within extracellular electron transfer are more effective than others. We also review efforts to create new exoelectrogens and highlight common challenges in this work. Lastly, we summarize work utilizing engineered exoelectrogens for biotechnological applications and the key obstacles to their future development. Fueled by the development of genetic tools, these approaches will continue to expand and genetically modified organisms will continue to improve the outlook for microbial electrochemical technologies. © 2015 Wiley Periodicals, Inc.

PATHWAYS - ELECTRON TUNNELING PATHWAYS IN PROTEINS

NASA Technical Reports Server (NTRS)

Beratan, D. N.

1994-01-01

The key to understanding the mechanisms of many important biological processes such as photosynthesis and respiration is a better understanding of the electron transfer processes which take place between metal atoms (and other groups) fixed within large protein molecules. Research is currently focused on the rate of electron transfer and the factors that influence it, such as protein composition and the distance between metal atoms. Current models explain the swift transfer of electrons over considerable distances by postulating bridge-mediated tunneling, or physical tunneling pathways, made up of interacting bonds in the medium around and between donor and acceptor sites. The program PATHWAYS is designed to predict the route along which electrons travel in the transfer processes. The basic strategy of PATHWAYS is to begin by recording each possible path element on a connectivity list, including in each entry which two atoms are connected and what contribution the connection would make to the overall rate if it were included in a pathway. The list begins with the bonded molecular structure (including the backbone sequence and side chain connectivity), and then adds probable hydrogen bond links and through-space contacts. Once this list is completed, the program runs a tree search from the donor to the acceptor site to find the dominant pathways. The speed and efficiency of the computer search offers an improvement over manual techniques. PATHWAYS is written in FORTRAN 77 for execution on DEC VAX series computers running VMS. The program inputs data from four data sets and one structure file. The software was written to input BIOGRAF (old format) structure files based on x-ray crystal structures and outputs ASCII files listing the best pathways and BIOGRAF vector files containing the paths. Relatively minor changes could be made in the input format statements for compatibility with other graphics software. The executable and source code are included with the distribution. The main memory requirement for execution is 2.6 Mb. This program is available in DEC VAX BACKUP format on a 9-track 1600 BPI magnetic tape (standard distribution) or on a TK50 tape cartridge. PATHWAYS was developed in 1988. PATHWAYS is a copyrighted work with all copyright vested in NASA. DEC, VAX, VMS, and TK50 are trademarks of Digital Equipment Corporation. BIOGRAF is a trademark of Molecular Simulations, Inc., Sunnyvale, CA.

Electron Bifurcation: Thermodynamics and Kinetics of Two-Electron Brokering in Biological Redox Chemistry.

PubMed

Zhang, Peng; Yuly, Jonathon L; Lubner, Carolyn E; Mulder, David W; King, Paul W; Peters, John W; Beratan, David N

2017-09-19

How can proteins drive two electrons from a redox active donor onto two acceptors at very different potentials and distances? And how can this transaction be conducted without dissipating very much energy or violating the laws of thermodynamics? Nature appears to have addressed these challenges by coupling thermodynamically uphill and downhill electron transfer reactions, using two-electron donor cofactors that have very different potentials for the removal of the first and second electron. Although electron bifurcation is carried out with near perfection from the standpoint of energy conservation and electron delivery yields, it is a biological energy transduction paradigm that has only come into focus recently. This Account provides an exegesis of the biophysical principles that underpin electron bifurcation. Remarkably, bifurcating electron transfer (ET) proteins typically send one electron uphill and one electron downhill by similar energies, such that the overall reaction is spontaneous, but not profligate. Electron bifurcation in the NADH-dependent reduced ferredoxin: NADP + oxidoreductase I (Nfn) is explored in detail here. Recent experimental progress in understanding the structure and function of Nfn allows us to dissect its workings in the framework of modern ET theory. The first electron that leaves the two-electron donor flavin (L-FAD) executes a positive free energy "uphill" reaction, and the departure of this electron switches on a second thermodynamically spontaneous ET reaction from the flavin along a second pathway that moves electrons in the opposite direction and at a very different potential. The singly reduced ET products formed from the bifurcating flavin are more than two nanometers distant from each other. In Nfn, the second electron to leave the flavin is much more reducing than the first: the potentials are said to be "crossed." The eventually reduced cofactors, NADH and ferredoxin in the case of Nfn, perform crucial downstream redox processes of their own. We dissect the thermodynamics and kinetics of electron bifurcation in Nfn and find that the key features of electron bifurcation are (1) spatially separated transfer pathways that diverge from a two-electron donor, (2) one thermodynamically uphill and one downhill redox pathway, with a large negative shift in the donor's reduction potential after departure of the first electron, and (3) electron tunneling and activation factors that enable bifurcation, producing a 1:1 partitioning of electrons onto the two pathways. Electron bifurcation is found in the CO 2 reducing pathways of methanogenic archaea, in the hydrogen pathways of hydrogenases, in the nitrogen fixing pathway of Fix, and in the mitochondrial charge transfer chain of complex III, cytochrome bc 1 . While crossed potentials may offer the biological advantage of producing tightly regulated high energy reactive species, neither kinetic nor thermodynamic considerations mandate crossed potentials to generate successful electron bifurcation. Taken together, the theoretical framework established here, focusing on the underpinning electron tunneling barriers and activation free energies, explains the logic of electron bifurcation that enables energy conversion and conservation in Nfn, points toward bioinspired schemes to execute multielectron redox chemistry, and establishes a roadmap for examining novel electron bifurcation networks in nature.

Water Molecules Gating a Photoinduced One-Electron Two-Protons Transfer in a Tyrosine/Histidine (Tyr/His) Model of Photosystem II.

PubMed

Chararalambidis, Georgios; Das, Shyamal; Trapali, Adelais; Quaranta, Annamaria; Orio, Maylis; Halime, Zakaria; Fertey, Pierre; Guillot, Régis; Coutsolelos, Athanassios; Leibl, Winfried; Aukauloo, Ally; Sircoglou, Marie

2018-05-22

We investigate a biomimetic model of a Tyr Z /His 190 pair, a hydrogen-bonded phenol/imidazole covalently attached to a porphyrin sensitizer. Laser flash photolysis in the presence of an external electron acceptor reveals the need for water molecules to unlock the light-induced oxidation of the phenol through an intramolecular pathway. Kinetics monitoring encompasses two fast phases with distinct spectral properties. The first phase is related to a one-electron transfer from the phenol to the porphyrin radical cation coupled with a domino two-proton transfer leading to the ejection of a proton from the imidazole-phenol pair. The second phase concerns conveying the released proton to the porphyrin N 4 coordinating cavity. Our study provides an unprecedented example of a light-induced electron-transfer process in a Tyr Z /His 190 model of photosystem II, evidencing the movement of both the phenol and imidazole protons along an isoenergetic pathway. © 2018 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.

Constraint-Based Modeling of Carbon Fixation and the Energetics of Electron Transfer in Geobacter metallireducens

DOE Office of Scientific and Technical Information (OSTI.GOV)

Feist, AM; Nagarajan, H; Rotaru, AE

2014-04-24

Geobacter species are of great interest for environmental and biotechnology applications as they can carry out direct electron transfer to insoluble metals or other microorganisms and have the ability to assimilate inorganic carbon. Here, we report on the capability and key enabling metabolic machinery of Geobacter metallireducens GS-15 to carry out CO2 fixation and direct electron transfer to iron. An updated metabolic reconstruction was generated, growth screens on targeted conditions of interest were performed, and constraint-based analysis was utilized to characterize and evaluate critical pathways and reactions in G. metallireducens. The novel capability of G. metallireducens to grow autotrophically withmore » formate and Fe(III) was predicted and subsequently validated in vivo. Additionally, the energetic cost of transferring electrons to an external electron acceptor was determined through analysis of growth experiments carried out using three different electron acceptors (Fe(III), nitrate, and fumarate) by systematically isolating and examining different parts of the electron transport chain. The updated reconstruction will serve as a knowledgebase for understanding and engineering Geobacter and similar species. Author Summary The ability of microorganisms to exchange electrons directly with their environment has large implications for our knowledge of industrial and environmental processes. For decades, it has been known that microbes can use electrodes as electron acceptors in microbial fuel cell settings. Geobacter metallireducens has been one of the model organisms for characterizing microbe-electrode interactions as well as environmental processes such as bioremediation. Here, we significantly expand the knowledge of metabolism and energetics of this model organism by employing constraint-based metabolic modeling. Through this analysis, we build the metabolic pathways necessary for carbon fixation, a desirable property for industrial chemical production. We further discover a novel growth condition which enables the characterization of autotrophic (i.e., carbon-fixing) metabolism in Geobacter. Importantly, our systems-level modeling approach helped elucidate the key metabolic pathways and the energetic cost associated with extracellular electron transfer. This model can be applied to characterize and engineer the metabolism and electron transfer capabilities of Geobacter for biotechnological applications.« less

Internal electron transfer between hemes and Cu(II) bound at cysteine beta93 promotes methemoglobin reduction by carbon monoxide.

PubMed

Bonaventura, C; Godette, G; Tesh, S; Holm, D E; Bonaventura, J; Crumbliss, A L; Pearce, L L; Peterson, J

1999-02-26

Previous studies showed that CO/H2O oxidation provides electrons to drive the reduction of oxidized hemoglobin (metHb). We report here that Cu(II) addition accelerates the rate of metHb beta chain reduction by CO by a factor of about 1000. A mechanism whereby electron transfer occurs via an internal pathway coupling CO/H2O oxidation to Fe(III) and Cu(II) reduction is suggested by the observation that the copper-induced rate enhancement is inhibited by blocking Cys-beta93 with N-ethylmaleimide. Furthermore, this internal electron-transfer pathway is more readily established at low Cu(II) concentrations in Hb Deer Lodge (beta2His --> Arg) and other species lacking His-beta2 than in Hb A0. This difference is consistent with preferential binding of Cu(II) in Hb A0 to a high affinity site involving His-beta2, which is ineffective in promoting electron exchange between Cu(II) and the beta heme iron. Effective electron transfer is thus affected by Hb type but is not governed by the R left arrow over right arrow T conformational equilibrium. The beta hemes in Cu(II)-metHb are reduced under CO at rates close to those observed for cytochrome c oxidase, where heme and copper are present together in the oxygen-binding site and where internal electron transfer also occurs.

Bridge-mediated hopping or superexchange electron-transfer processes in bis(triarylamine) systems

NASA Astrophysics Data System (ADS)

Lambert, Christoph; Nöll, Gilbert; Schelter, Jürgen

2002-09-01

Hopping and superexchange are generally considered to be alternative electron-transfer mechanisms in molecular systems. In this work we used mixed-valence radical cations as model systems for the investigation of electron-transfer pathways. We show that substituents attached to a conjugated bridge connecting two triarylamine redox centres have a marked influence on the near-infrared absorption spectra of the corresponding cations. Spectral analysis, followed by evaluation of the electron-transfer parameters using the Generalized Mulliken-Hush theory and simulation of the potential energy surfaces, indicate that hopping and superexchange are not alternatives, but are both present in the radical cation with a dimethoxybenzene bridge. We found that the type of electron-transfer mechanism depends on the bridge-reorganization energy as well as on the bridge-state energy. Because superexchange and hopping follow different distance laws, our findings have implications for the design of new molecular and polymeric electron-transfer materials.

The electron transfer flavoprotein: ubiquinone oxidoreductases.

PubMed

Watmough, Nicholas J; Frerman, Frank E

2010-12-01

Electron transfer flavoprotein: ubiqionone oxidoreductase (ETF-QO) is a component of the mitochondrial respiratory chain that together with electron transfer flavoprotein (ETF) forms a short pathway that transfers electrons from 11 different mitochondrial flavoprotein dehydrogenases to the ubiquinone pool. The X-ray structure of the pig liver enzyme has been solved in the presence and absence of a bound ubiquinone. This structure reveals ETF-QO to be a monotopic membrane protein with the cofactors, FAD and a [4Fe-4S](+1+2) cluster, organised to suggests that it is the flavin that serves as the immediate reductant of ubiquinone. ETF-QO is very highly conserved in evolution and the recombinant enzyme from the bacterium Rhodobacter sphaeroides has allowed the mutational analysis of a number of residues that the structure suggested are involved in modulating the reduction potential of the cofactors. These experiments, together with the spectroscopic measurement of the distances between the cofactors in solution have confirmed the intramolecular pathway of electron transfer from ETF to ubiquinone. This approach can be extended as the R. sphaeroides ETF-QO provides a template for investigating the mechanistic consequences of single amino acid substitutions of conserved residues that are associated with a mild and late onset variant of the metabolic disease multiple acyl-CoA dehydrogenase deficiency (MADD). Copyright © 2010 Elsevier B.V. All rights reserved.

The Involvement of Hydrogen-producing and ATP-dependent NADPH-consuming Pathways in Setting the Redox Poise in the Chloroplast of Chlamydomonas reinhardtii in Anoxia

PubMed Central

Clowez, Sophie; Godaux, Damien; Cardol, Pierre; Wollman, Francis-André; Rappaport, Fabrice

2015-01-01

Photosynthetic microalgae are exposed to changing environmental conditions. In particular, microbes found in ponds or soils often face hypoxia or even anoxia, and this severely impacts their physiology. Chlamydomonas reinhardtii is one among such photosynthetic microorganisms recognized for its unusual wealth of fermentative pathways and the extensive remodeling of its metabolism upon the switch to anaerobic conditions. As regards the photosynthetic electron transfer, this remodeling encompasses a strong limitation of the electron flow downstream of photosystem I. Here, we further characterize the origin of this limitation. We show that it stems from the strong reducing pressure that builds up upon the onset of anoxia, and this pressure can be relieved either by the light-induced synthesis of ATP, which promotes the consumption of reducing equivalents, or by the progressive activation of the hydrogenase pathway, which provides an electron transfer pathway alternative to the CO2 fixation cycle. PMID:25691575

Structural aspects of denitrifying enzymes.

PubMed

Moura, I; Moura, J J

2001-04-01

The reduction of nitrate to nitrogen gas via nitrite, nitric oxide and nitrous oxide is the metabolic pathway usually known as denitrification, a key step in the nitrogen cycle. As observed for other elemental cycles, a battery of enzymes are utilized, namely the reductases for nitrate, nitrite, nitric oxide and nitrous oxide, as well as multiple electron donors that interact with these enzymes, in order to carry out the stepwise reactions that involve key intermediates. Because of the importance of this pathway (of parallel importance to the nitrogen-fixation pathway), efforts are underway to understand the structures of the participating enzymes and to uncover mechanistic aspects. Three-dimensional structures have been solved for the majority of these enzymes in the past few years, revealing the architecture of the active metal sites as well as global structural aspects, and possible mechanistic aspects. In addition, the recognition of specific electron-transfer partners raises important questions regarding specific electron-transfer pathways, partner recognition and control of metabolism.

Osm1 facilitates the transfer of electrons from Erv1 to fumarate in the redox-regulated import pathway in the mitochondrial intermembrane space

PubMed Central

Neal, Sonya E.; Dabir, Deepa V.; Wijaya, Juwina; Boon, Cennyana; Koehler, Carla M.

2017-01-01

Prokaryotes have aerobic and anaerobic electron acceptors for oxidative folding of periplasmic proteins. The mitochondrial intermembrane space has an analogous pathway with the oxidoreductase Mia40 and sulfhydryl oxidase Erv1, termed the mitochondrial intermembrane space assembly (MIA) pathway. The aerobic electron acceptors include oxygen and cytochrome c, but an acceptor that can function under anaerobic conditions has not been identified. Here we show that the fumarate reductase Osm1, which facilitates electron transfer from fumarate to succinate, fills this gap as a new electron acceptor. In addition to microsomes, Osm1 localizes to the mitochondrial intermembrane space and assembles with Erv1 in a complex. In reconstitution studies with reduced Tim13, Mia40, and Erv1, the addition of Osm1 and fumarate completes the disulfide exchange pathway that results in Tim13 oxidation. From in vitro import assays, mitochondria lacking Osm1 display decreased import of MIA substrates, Cmc1 and Tim10. Comparative reconstitution assays support that the Osm1/fumarate couple accepts electrons with similar efficiency to cytochrome c and that the cell has strategies to coordinate expression of the terminal electron acceptors. Thus Osm1/fumarate is a new electron acceptor couple in the mitochondrial intermembrane space that seems to function in both aerobic and anaerobic conditions. PMID:28814504

Antioxidative mechanisms in chlorogenic acid.

PubMed

Tošović, Jelena; Marković, Svetlana; Dimitrić Marković, Jasmina M; Mojović, Miloš; Milenković, Dejan

2017-12-15

Although chlorogenic acid (5CQA) is an important ingredient of various foods and beverages, mechanisms of its antioxidative action have not been fully clarified. Besides electron spin resonance experiment, this study includes thermodynamic and mechanistic investigations of the hydrogen atom transfer (HAT), radical adduct formation (RAF), sequential proton loss electron transfer (SPLET), and single electron transfer - proton transfer (SET-PT) mechanisms of 5CQA in benzene, ethanol, and water solutions. The calculations were performed using the M06-2X/6-311++G(d,p) level of theory and CPCM solvation model. It was found that SET-PT is not a plausible antioxidative mechanism of 5CQA. RAF pathways are faster, but HAT yields thermodynamically more stable radical products, indicating that in acidic and neutral media 5CQA can take either HAT or RAF pathways. In basic environment (e.g. at physiological pH) SPLET is the likely antioxidative mechanism of 5CQA with extremely high rate. Copyright © 2017 Elsevier Ltd. All rights reserved.

Possible Dynamically Gated Conductance along Heme Wires in Bacterial Multiheme Cytochromes

DOE Office of Scientific and Technical Information (OSTI.GOV)

Smith, Dayle MA; Rosso, Kevin M.

2014-07-24

The staggered cross decaheme configuration of electron transfer co-factors in the outer-membrane cytochrome MtrF may serve as a prototype for conformationally-gated multi-heme electron transport. Derived from the bacterium Shewanella oneidensis, the staggered cross configuration reveals intersecting c-type octaheme and tetraheme “wires” containing thermodynamic “hills” and “valleys”, suggesting that the protein structure may include a dynamical mechanism for conductance and pathway switching depending on enzymatic functional need. Recent molecular simulations have established the pair-wise electronic couplings, redox potentials, and reorganization energies to predict the maximum conductance along the various heme wire pathways by sequential hopping of a single electron (PNAS (2014)more » 11,611-616). Here, we expand this information with classical molecular and statistical mechanics calculations of large-amplitude protein dynamics in MtrF, to address its potential to modulate pathway conductance, including assessment of the effect of the total charge state. Explicit solvent molecular dynamics simulations of fully oxidized and fully reduced MtrF employing ten independent 50-ns simulations at 300 K and 1 atm showed that reduced MtrF is more expanded and explores more conformational space than oxidized MtrF, and that heme reduction leads to increased heme solvent exposure. The slowest mode of collective decaheme motion is 90% similar between the oxidized and reduced states, and consists primarily of inter-heme separation with minor rotational contributions. The frequency of this motion is 1.7×107 s 1 for fully-oxidized and fully-reduced MtrF, respectively, slower than the downhill electron transfer rates between stacked heme pairs at the octaheme termini and faster than the electron transfer rates between parallel hemes in the tetraheme chain. This implies that MtrF uses slow conformational fluctuations to modulate electron flow along the octaheme pathway, apparently for the purpose of increasing the residence time of electrons on lowest potential hemes 4 and 9. This apparent gating mechanism should increase the success rate of electron transfer from MtrF to low potential environmental acceptors via these two solvent-exposed hemes.« less

Leveraging Electron Transfer Dissociation for Site Selective Radical Generation: Applications for Peptide Epimer Analysis

NASA Astrophysics Data System (ADS)

Lyon, Yana A.; Beran, Gregory; Julian, Ryan R.

2017-07-01

Traditional electron-transfer dissociation (ETD) experiments operate through a complex combination of hydrogen abundant and hydrogen deficient fragmentation pathways, yielding c and z ions, side-chain losses, and disulfide bond scission. Herein, a novel dissociation pathway is reported, yielding homolytic cleavage of carbon-iodine bonds via electronic excitation. This observation is very similar to photodissociation experiments where homolytic cleavage of carbon-iodine bonds has been utilized previously, but ETD activation can be performed without addition of a laser to the mass spectrometer. Both loss of iodine and loss of hydrogen iodide are observed, with the abundance of the latter product being greatly enhanced for some peptides after additional collisional activation. These observations suggest a novel ETD fragmentation pathway involving temporary storage of the electron in a charge-reduced arginine side chain. Subsequent collisional activation of the peptide radical produced by loss of HI yields spectra dominated by radical-directed dissociation, which can be usefully employed for identification of peptide isomers, including epimers.

Alternative Pathway of Metronidazole Activation in Trichomonas vaginalis Hydrogenosomes

PubMed Central

Hrdý, Ivan; Cammack, Richard; Stopka, Pavel; Kulda, Jaroslav; Tachezy, Jan

2005-01-01

Metronidazole and related 5-nitroimidazoles are the only available drugs in the treatment of human urogenital trichomoniasis caused by the protozoan parasite Trichomonas vaginalis. The drugs are activated to cytotoxic anion radicals by their reduction within the hydrogenosomes. It has been established that electrons required for metronidazole activation are released from pyruvate by the activity of pyruvate:ferredoxin oxidoreductase and transferred to the drug by a low-redox-potential carrier, ferredoxin. Here we describe a novel pathway involved in the drug activation within the hydrogenosome. The source of electrons is malate, another major hydrogenosomal substrate, which is oxidatively decarboxylated to pyruvate and CO2 by NAD-dependent malic enzyme. The electrons released during this reaction are transferred from NADH to ferredoxin by NADH dehydrogenase homologous to the catalytic module of mitochondrial complex I, which uses ferredoxin as electron acceptor. Trichomonads acquire high-level metronidazole resistance only after both pyruvate- and malate-dependent pathways of metronidazole activation are eliminated from the hydrogenosomes. PMID:16304169

Cytochromes and iron sulfur proteins in sulfur metabolism of phototrophic bacteria

NASA Technical Reports Server (NTRS)

Fischer, U.

1985-01-01

Dissimilatory sulfur metabolism in phototrophic sulfur bacteria provides the bacteria with electrons for photosynthetic electron transport chain and, with energy. Assimilatory sulfate reduction is necessary for the biosynthesis of sulfur-containing cell components. Sulfide, thiosulfate, and elemental sulfur are the sulfur compounds most commonly used by phototrophic bacteria as electron donors for anoxygenic photosynthesis. Cytochromes or other electron transfer proteins, like high-potential-iron-sulfur protein (HIPIP) function as electron acceptors or donors for most enzymatic steps during the oxidation pathways of sulfide or thiosulfate. Yet, heme- or siroheme-containing proteins themselves undergo enzymatic activities in sulfur metabolism. Sirohemes comprise a porphyrin-like prosthetic group of sulfate reductase. eenzymatic reactions involve electron transfer. Electron donors or acceptors are necessary for each reaction. Cytochromes and iron sulfur problems, are able to transfer electrons.

High Throughput Engineering to Revitalize a Vestigial Electron Transfer Pathway in Bacterial Photosynthetic Reaction Centers*

PubMed Central

Faries, Kaitlyn M.; Kressel, Lucas L.; Wander, Marc J.; Holten, Dewey; Laible, Philip D.; Kirmaier, Christine; Hanson, Deborah K.

2012-01-01

Photosynthetic reaction centers convert light energy into chemical energy in a series of transmembrane electron transfer reactions, each with near 100% yield. The structures of reaction centers reveal two symmetry-related branches of cofactors (denoted A and B) that are functionally asymmetric; purple bacterial reaction centers use the A pathway exclusively. Previously, site-specific mutagenesis has yielded reaction centers capable of transmembrane charge separation solely via the B branch cofactors, but the best overall electron transfer yields are still low. In an attempt to better realize the architectural and energetic factors that underlie the directionality and yields of electron transfer, sites within the protein-cofactor complex were targeted in a directed molecular evolution strategy that implements streamlined mutagenesis and high throughput spectroscopic screening. The polycistronic approach enables efficient construction and expression of a large number of variants of a heteroligomeric complex that has two intimately regulated subunits with high sequence similarity, common features of many prokaryotic and eukaryotic transmembrane protein assemblies. The strategy has succeeded in the discovery of several mutant reaction centers with increased efficiency of the B pathway; they carry multiple substitutions that have not been explored or linked using traditional approaches. This work expands our understanding of the structure-function relationships that dictate the efficiency of biological energy-conversion reactions, concepts that will aid the design of bio-inspired assemblies capable of both efficient charge separation and charge stabilization. PMID:22247556

A modeling approach to direct interspecies electron transfer process in anaerobic transformation of ethanol to methane.

PubMed

Liu, Yiwen; Zhang, Yaobin; Zhao, Zhiqiang; Ngo, Huu Hao; Guo, Wenshan; Zhou, Junliang; Peng, Lai; Ni, Bing-Jie

2017-01-01

Recent studies have shown that direct interspecies electron transfer (DIET) plays an important part in contributing to methane production from anaerobic digestion. However, so far anaerobic digestion models that have been proposed only consider two pathways for methane production, namely, acetoclastic methanogenesis and hydrogenotrophic methanogenesis, via indirect interspecies hydrogen transfer, which lacks an effective way for incorporating DIET into this paradigm. In this work, a new mathematical model is specifically developed to describe DIET process in anaerobic digestion through introducing extracellular electron transfer as a new pathway for methane production, taking anaerobic transformation of ethanol to methane as an example. The developed model was able to successfully predict experimental data on methane dynamics under different experimental conditions, supporting the validity of the developed model. Modeling predictions clearly demonstrated that DIET plays an important role in contributing to overall methane production (up to 33 %) and conductive material (i.e., carbon cloth) addition would significantly promote DIET through increasing ethanol conversion rate and methane production rate. The model developed in this work will potentially enhance our current understanding on syntrophic metabolism via DIET.

Gene Transfers Shaped the Evolution of De Novo NAD+ Biosynthesis in Eukaryotes

PubMed Central

Ternes, Chad M.; Schönknecht, Gerald

2014-01-01

NAD+ is an essential molecule for life, present in each living cell. It can function as an electron carrier or cofactor in redox biochemistry and energetics, and serves as substrate to generate the secondary messenger cyclic ADP ribose and nicotinic acid adenine dinucleotide phosphate. Although de novo NAD+ biosynthesis is essential, different metabolic pathways exist in different eukaryotic clades. The kynurenine pathway starting with tryptophan was most likely present in the last common ancestor of all eukaryotes, and is active in fungi and animals. The aspartate pathway, detected in most photosynthetic eukaryotes, was probably acquired from the cyanobacterial endosymbiont that gave rise to chloroplasts. An evolutionary analysis of enzymes catalyzing de novo NAD+ biosynthesis resulted in evolutionary trees incongruent with established organismal phylogeny, indicating numerous gene transfers. Endosymbiotic gene transfers probably introduced the aspartate pathway into eukaryotes and may have distributed it among different photosynthetic clades. In addition, several horizontal gene transfers substituted eukaryotic genes with bacterial orthologs. Although horizontal gene transfer is accepted as a key mechanism in prokaryotic evolution, it is supposed to be rare in eukaryotic evolution. The essential metabolic pathway of de novo NAD+ biosynthesis in eukaryotes was shaped by numerous gene transfers. PMID:25169983

Synergies between Unsaturated Zn/Cu Doping Sites in Carbon Dots Provide New Pathways for Photocatalytic Oxidation

DOE PAGES

Wu, Wenting; Zhang, Qinggang; Wang, Ruiqin; ...

2017-12-07

Unsaturated metal species (UMS) confined in nanomaterials play important roles for electron transfer in a wide range of catalytic reactions. However, the limited fabrication methods of UMS restrict their wider catalytic applications. Here in this paper, we report on the synergy of unsaturated Zn and Cu dopants confined in carbon dots (ZnCu-CDs) to produce enhanced electron transfer and photooxidation processes in the doped CDs. The Zn/Cu species chelate with the carbon matrix mainly through Cu-O(N)-Zn-O(N)-Cu complexes. Within this structure, Cu 2+ acts as a mild oxidizer that facilely increases the unsaturated Zn content and also precisely tunes the unsaturated Znmore » valence state to Zn d+, where d is between 1 and 2, instead of Zn. With the help of UMS, electron-transfer pathways are produced, enhancing both the electron donating (7.0 times) and-accepting (5.3 times) abilities relative to conventional CDs. Because of these synergistic effects, the photocatalytic efficiency of CDs in photooxidation reactions is shown to improve more than 5-fold.« less

Enhanced Ionization of Embedded Clusters by Electron-Transfer-Mediated Decay in Helium Nanodroplets.

PubMed

LaForge, A C; Stumpf, V; Gokhberg, K; von Vangerow, J; Stienkemeier, F; Kryzhevoi, N V; O'Keeffe, P; Ciavardini, A; Krishnan, S R; Coreno, M; Prince, K C; Richter, R; Moshammer, R; Pfeifer, T; Cederbaum, L S; Mudrich, M

2016-05-20

We report the observation of electron-transfer-mediated decay (ETMD) involving magnesium (Mg) clusters embedded in helium (He) nanodroplets. ETMD is initiated by the ionization of He followed by removal of two electrons from the Mg clusters of which one is transferred to the He ion while the other electron is emitted into the continuum. The process is shown to be the dominant ionization mechanism for embedded clusters for photon energies above the ionization potential of He. For Mg clusters larger than five atoms we observe stable doubly ionized clusters. Thus, ETMD provides an efficient pathway to the formation of doubly ionized cold species in doped nanodroplets.

Elucidating the role of methyl viologen as a scavenger of photoactivated electrons from photosystem I under aerobic and anaerobic conditions.

PubMed

Bennett, Tyler; Niroomand, Hanieh; Pamu, Ravi; Ivanov, Ilia; Mukherjee, Dibyendu; Khomami, Bamin

2016-03-28

We present detailed electrochemical investigations into the role of dissolved O2 in electrolyte solutions in scavenging photoactivated electrons from a uniform photosystem I (PS I) monolayer assembled on alkanethiolate SAM (self-assembled monolayer)/Au surfaces while using methyl viologen (MV(2+)) as the redox mediator. To this end, we report results for direct measurements of light induced photocurrent from uniform monolayer assemblies of PS I on C9 alkanethiolate SAM/Au surfaces. These measurements, apart from demonstrating the ability of dissolved O2 in the electrolyte medium to act as an electron scavenger, also reveal its essential role in driving the solution-phase methyl viologen to initiate light-induced directional electron transfer from an electron donor surface (Au) via surface assembled PS I trimers. Specifically, our systematic electrochemical measurements have revealed that the dissolved O2 in aqueous electrolyte solutions form a complex intermediate species with MV that plays the essential role in mediating redox pathways for unidirectional electron transfer processes. This critical insight into the redox-mediated electron transfer pathways allows for rational design of electron scavengers through systematic tuning of mediator combinations that promote such intermediate formation. Our current findings facilitate the incorporation of PS I-based bio-hybrid constructs as photo-anodes in future photoelectrochemical cells and bio-electronic devices.

Role of the photosynthetic electron transfer chain in electrogenic activity of cyanobacteria.

PubMed

Pisciotta, John M; Zou, Yongjin; Baskakov, Ilia V

2011-07-01

Certain anaerobic bacteria, termed electrogens, produce an electric current when electrons from oxidized organic molecules are deposited to extracellular metal oxide acceptors. In these heterotrophic "metal breathers", the respiratory electron transport chain (R-ETC) works in concert with membrane-bound cytochrome oxidases to transfer electrons to the extracellular acceptors. The diversity of bacteria able to generate an electric current appears more widespread than previously thought, and aerobic phototrophs, including cyanobacteria, possess electrogenic activity. However, unlike heterotrophs, cyanobacteria electrogenic activity is light dependent, which suggests that a novel pathway could exist. To elucidate the electrogenic mechanism of cyanobacteria, the current studies used site-specific inhibitors to target components of the photosynthetic electron transport chain (P-ETC) and cytochrome oxidases. Here, we show that (1) P-ETC and, particularly, water photolysed by photosystem II (PSII) is the source of electrons discharged to the environment by illuminated cyanobacteria, and (2) water-derived electrons are transmitted from PSII to extracellular electron acceptors via plastoquinone and cytochrome bd quinol oxidase. Two cyanobacterial genera (Lyngbya and Nostoc) displayed very similar electrogenic responses when treated with P-ETC site-specific inhibitors, suggesting a conserved electrogenic pathway. We propose that in cyanobacteria, electrogenic activity may represent a form of overflow metabolism to protect cells under high-intensity light. This study offers insight into electron transfer between phototrophic microorganisms and the environment and expands our knowledge into biologically based mechanisms for harnessing solar energy.

Unusual redox behavior in the photoinduced electron-transfer reactions of amino ketones

DOE Office of Scientific and Technical Information (OSTI.GOV)

Bergmark, W.R.; Whitten, D.G.; DeWan, C.

1992-11-04

Irradiation of a wet benzene solution of 1,2-diphenyl-2-piperidino-1-ethanome and 9,10-dicyanoanthracene leads to the formation of benzil and deoxybenzoin. We have interpreted these products as arising from deprotonation leading to net oxidation coupled with reductive elimination. The latter pathway is noteworthy in that we show reductive elimination of an electron donor can be a chief consequence of photochemical single electron transfer (SET) quenching. 22 refs., 3 figs., 1 tab.

Communication: Charge transfer dominates over proton transfer in the reaction of nitric acid with gas-phase hydrated electrons

NASA Astrophysics Data System (ADS)

Lengyel, Jozef; Med, Jakub; Slavíček, Petr; Beyer, Martin K.

2017-09-01

The reaction of HNO3 with hydrated electrons (H2O)n- (n = 35-65) in the gas phase was studied using Fourier transform ion cyclotron resonance (FT-ICR) mass spectrometry and ab initio molecular dynamics simulations. Kinetic analysis of the experimental data shows that OH-(H2O)m is formed primarily via a reaction of the hydrated electron with HNO3 inside the cluster, while proton transfer is not observed and NO3-(H2O)m is just a secondary product. The reaction enthalpy was determined using nanocalorimetry, revealing a quite exothermic charge transfer with -241 ± 69 kJ mol-1. Ab initio molecular dynamics simulations indicate that proton transfer is an allowed reaction pathway, but the overall thermochemistry favors charge transfer.

The Alternative complex III: properties and possible mechanisms for electron transfer and energy conservation.

PubMed

Refojo, Patrícia N; Teixeira, Miguel; Pereira, Manuela M

2012-10-01

Alternative complexes III (ACIII) are recently identified membrane-bound enzymes that replace functionally the cytochrome bc(1/)b(6)f complexes. In general, ACIII are composed of four transmembrane proteins and three peripheral subunits that contain iron-sulfur centers and C-type hemes. ACIII are built by a combination of modules present in different enzyme families, namely the complex iron-sulfur molybdenum containing enzymes. In this article a historical perspective on the investigation of ACIII is presented, followed by an overview of the present knowledge on these enzymes. Electron transfer pathways within the protein are discussed taking into account possible different locations (cytoplasmatic or periplasmatic) of the iron-sulfur containing protein and their contribution to energy conservation. In this way several hypotheses for energy conservation modes are raised including linear and bifurcating electron transfer pathways. This article is part of a Special Issue entitled: 17th European Bioenergetics Conference (EBEC 2012). Copyright © 2012 Elsevier B.V. All rights reserved.

Metagenomic insight into methanogenic reactors promoting direct interspecies electron transfer via granular activated carbon.

PubMed

Park, Jeong-Hoon; Park, Jong-Hun; Je Seong, Hoon; Sul, Woo Jun; Jin, Kang-Hyun; Park, Hee-Deung

2018-07-01

To provide insight into direct interspecies electron transfer via granular activated carbon (GAC), the effect of GAC supplementation on anaerobic digestion was evaluated. Compared to control samples, the GAC supplementation increased the total amount of methane production and its production rate by 31% and 72%, respectively. 16S rDNA sequencing analysis revealed a shift in the archaeal community composition; the Methanosarcina proportion decreased 17%, while the Methanosaeta proportion increased 5.6%. Metagenomic analyses based on shotgun sequencing demonstrated that the abundance of pilA and omcS genes belonging to Geobacter species decreased 69.4% and 29.4%, respectively. Furthermore, the analyses suggested a carbon dioxide reduction pathway rather than an acetate decarboxylation pathway for methane formation. Taken together, these results suggest that GAC improved methane production performance by shifting the microbial community and altering functional genes associated with direct interspecies electron transfer via conductive materials. Copyright © 2018 Elsevier Ltd. All rights reserved.

Metagenomic insights into the ecology and physiology of microbes in bioelectrochemical systems.

PubMed

Kouzuma, Atsushi; Ishii, Shun'ichi; Watanabe, Kazuya

2018-05-01

In bioelectrochemical systems (BESs), electrons are transferred between electrochemically active microbes (EAMs) and conductive materials, such as electrodes, via extracellular electron transfer (EET) pathways, and electrons thus transferred stimulate intracellular catabolic reactions. Catabolic and EET pathways have extensively been studied for several model EAMs, such as Shewanella oneidensis MR-1 and Geobacter sulfurreducens PCA, whereas it is also important to understand the ecophysiology of EAMs in naturally occurring microbiomes, such as those in anode biofilms in microbial fuel cells treating wastewater. Recent studies have exploited metagenomics and metatranscriptomics (meta-omics) approaches to characterize EAMs in BES-associated microbiomes. Here we review recent BES studies that used meta-omics approaches and show that these studies have discovered unexpected features of EAMs and deepened our understanding of functions and behaviors of microbes in BESs. It is desired that more studies will employ meta-omics approaches for advancing our knowledge on microbes in BESs. Copyright © 2018 Elsevier Ltd. All rights reserved.

Interference of interchromophoric energy-transfer pathways in π-conjugated macrocycles

DOE PAGES

Alfonso Hernandez, Laura; Nelson, Tammie Renee; Gelin, Maxim F.; ...

2016-11-10

The interchromophoric energy-transfer pathways between weakly coupled units in a π-conjugated phenylene–ethynylene macrocycle and its half-ring analogue have been investigated using the nonadiabatic excited-state molecular dynamics approach. To track the flow of electronic transition density between macrocycle units, we formulate a transition density flux analysis adapted from the statistical minimum flow method previously developed to investigate vibrational energy flow. Following photoexcitation, transition density is primarily delocalized on two chromophore units and the system undergoes ultrafast energy transfer, creating a localized excited state on a single unit. In the macrocycle, distinct chromophore units donate transition density to a single acceptor unitmore » but do not interchange transition density among each other. We find that energy transfer in the macrocycle is slower than in the corresponding half ring because of the presence of multiple interfering energy-transfer pathways. Finally, simulation results are validated by modeling the fluorescence anisotropy decay.« less

Insights into dissociative electron transfer in esterified shikonin semiquinones by in situ ESR/UV-Vis spectroelectrochemistry.

PubMed

Armendáriz-Vidales, G; Frontana, C

2015-11-21

In this work, electrogenerated anion and dianion species from shikonin and its ester derivative isovalerylshikonin were characterized by means of ESR/UV-Vis spectroelectrochemistry. Analysis of the spectra supported the proposal that stepwise dissociative electron transfer (DET) takes place during the second reduction process of the esterified compound. Quantum chemical calculations were performed for validating the occurrence of this mechanistic pathway and for obtaining thermodynamic information on the electron transfer process; ΔG(cleavage)(0) was estimated to be -0.45 eV, considering that the two possible products of the overall reaction scheme are both a quinone and carboxylate anions.

Role of pendant proton relays and proton-coupled electron transfer on the hydrogen evolution reaction by nickel hangman porphyrins

DOE PAGES

Bediako, D. Kwabena; Solis, Brian H.; Dogutan, Dilek K.; ...

2014-10-08

Here, the hangman motif provides mechanistic insights into the role of pendant proton relays in governing proton-coupled electron transfer (PCET) involved in the hydrogen evolution reaction (HER). We now show improved HER activity of Ni compared with Co hangman porphyrins. Cyclic voltammogram data and simulations, together with computational studies using density functional theory, implicate a shift in electrokinetic zone between Co and Ni hangman porphyrins due to a change in the PCET mechanism. Unlike the Co hangman porphyrin, the Ni hangman porphyrin does not require reduction to the formally metal(0) species before protonation by weak acids in acetonitrile. We concludemore » that protonation likely occurs at the Ni(I) state followed by reduction, in a stepwise proton transfer–electron transfer pathway. Spectroelectrochemical and computational studies reveal that upon reduction of the Ni(II) compound, the first electron is transferred to a metal-based orbital, whereas the second electron is transferred to a molecular orbital on the porphyrin ring.« less

Role of pendant proton relays and proton-coupled electron transfer on the hydrogen evolution reaction by nickel hangman porphyrins

PubMed Central

Bediako, D. Kwabena; Solis, Brian H.; Dogutan, Dilek K.; Roubelakis, Manolis M.; Maher, Andrew G.; Lee, Chang Hoon; Chambers, Matthew B.; Hammes-Schiffer, Sharon; Nocera, Daniel G.

2014-01-01

The hangman motif provides mechanistic insights into the role of pendant proton relays in governing proton-coupled electron transfer (PCET) involved in the hydrogen evolution reaction (HER). We now show improved HER activity of Ni compared with Co hangman porphyrins. Cyclic voltammogram data and simulations, together with computational studies using density functional theory, implicate a shift in electrokinetic zone between Co and Ni hangman porphyrins due to a change in the PCET mechanism. Unlike the Co hangman porphyrin, the Ni hangman porphyrin does not require reduction to the formally metal(0) species before protonation by weak acids in acetonitrile. We conclude that protonation likely occurs at the Ni(I) state followed by reduction, in a stepwise proton transfer–electron transfer pathway. Spectroelectrochemical and computational studies reveal that upon reduction of the Ni(II) compound, the first electron is transferred to a metal-based orbital, whereas the second electron is transferred to a molecular orbital on the porphyrin ring. PMID:25298534

What Hinders Electron Transfer Dissociation (ETD) of DNA Cations?

NASA Astrophysics Data System (ADS)

Hari, Yvonne; Leumann, Christian J.; Schürch, Stefan

2017-12-01

Radical activation methods, such as electron transfer dissociation (ETD), produce structural information complementary to collision-induced dissociation. Herein, electron transfer dissociation of 3-fold protonated DNA hexamers was studied to gain insight into the fragmentation mechanism. The fragmentation patterns of a large set of DNA hexamers confirm cytosine as the primary target of electron transfer. The reported data reveal backbone cleavage by internal electron transfer from the nucleobase to the phosphate linker leading either to a•/ w or d/ z• ion pairs. This reaction pathway contrasts with previous findings on the dissociation processes after electron capture by DNA cations, suggesting multiple, parallel dissociation channels. However, all these channels merely result in partial fragmentation of the precursor ion because the charge-reduced DNA radical cations are quite stable. Two hypotheses are put forward to explain the low dissociation yield of DNA radical cations: it is either attributed to non-covalent interactions between complementary fragments or to the stabilization of the unpaired electron in stacked nucleobases. MS3 experiments suggest that the charge-reduced species is the intact oligonucleotide. Moreover, introducing abasic sites significantly increases the dissociation yield of DNA cations. Consequently, the stabilization of the unpaired electron by π-π-stacking provides an appropriate rationale for the high intensity of DNA radical cations after electron transfer. [Figure not available: see fulltext.

Surface Proton Transfer Promotes Four-Electron Oxygen Reduction on Gold Nanocrystal Surfaces in Alkaline Solution

DOE Office of Scientific and Technical Information (OSTI.GOV)

Lu, Fang; Zhang, Yu; Liu, Shizhong

Four-electron oxygen reduction reaction (4e-ORR), as a key pathway in energy conversion, is preferred over the two-electron reduction pathway that falls short in dissociating dioxygen molecules. Gold (Au) surfaces exhibit high sensitivity of the ORR pathway to its atomic structures. The long-standing puzzle remains unsolved why the Au surfaces with {100} sub-facets were exceptionally capable to catalyze the 4e-ORR in alkaline solution, though limited within a narrow potential window. Herein we report the discovery of a dominant 4e-ORR over the whole potential range on {310} surface of Au nanocrystal shaped as truncated ditetragonal prism (TDP). In contrast, ORR pathways onmore » single-crystalline facets of shaped nanoparticles, including {111} on nano-octahedra and {100} on nano-cubes, are similar to their single-crystal counterparts. Combining our experimental results with density functional theory calculations, we elucidate the key role of surface proton transfers from co-adsorbed H 2O molecules in activating the facet- and potential-dependent 4e ORR on Au in alkaline solutions. These results elucidate how surface atomic structures determine the reaction pathways via bond scission and formation among weakly adsorbed water and reaction intermediates. The new insight helps in developing facet-specific nanocatalysts for various reactions.« less

Surface Proton Transfer Promotes Four-Electron Oxygen Reduction on Gold Nanocrystal Surfaces in Alkaline Solution

DOE PAGES

Lu, Fang; Zhang, Yu; Liu, Shizhong; ...

2017-05-11

Four-electron oxygen reduction reaction (4e-ORR), as a key pathway in energy conversion, is preferred over the two-electron reduction pathway that falls short in dissociating dioxygen molecules. Gold (Au) surfaces exhibit high sensitivity of the ORR pathway to its atomic structures. The long-standing puzzle remains unsolved why the Au surfaces with {100} sub-facets were exceptionally capable to catalyze the 4e-ORR in alkaline solution, though limited within a narrow potential window. Herein we report the discovery of a dominant 4e-ORR over the whole potential range on {310} surface of Au nanocrystal shaped as truncated ditetragonal prism (TDP). In contrast, ORR pathways onmore » single-crystalline facets of shaped nanoparticles, including {111} on nano-octahedra and {100} on nano-cubes, are similar to their single-crystal counterparts. Combining our experimental results with density functional theory calculations, we elucidate the key role of surface proton transfers from co-adsorbed H 2O molecules in activating the facet- and potential-dependent 4e ORR on Au in alkaline solutions. These results elucidate how surface atomic structures determine the reaction pathways via bond scission and formation among weakly adsorbed water and reaction intermediates. The new insight helps in developing facet-specific nanocatalysts for various reactions.« less

The influence of alternative pathways of respiration that utilize branched-chain amino acids following water shortage in Arabidopsis.

PubMed

Pires, Marcel V; Pereira Júnior, Adilson A; Medeiros, David B; Daloso, Danilo M; Pham, Phuong Anh; Barros, Kallyne A; Engqvist, Martin K M; Florian, Alexandra; Krahnert, Ina; Maurino, Veronica G; Araújo, Wagner L; Fernie, Alisdair R

2016-06-01

During dark-induced senescence isovaleryl-CoA dehydrogenase (IVDH) and D-2-hydroxyglutarate dehydrogenase (D-2HGDH) act as alternate electron donors to the ubiquinol pool via the electron-transfer flavoprotein/electron-transfer flavoprotein:ubiquinone oxidoreductase (ETF/ETFQO) pathway. However, the role of this pathway in response to other stresses still remains unclear. Here, we demonstrated that this alternative pathway is associated with tolerance to drought in Arabidopsis. In comparison with wild type (WT) and lines overexpressing D-2GHDH, loss-of-function etfqo-1, d2hgdh-2 and ivdh-1 mutants displayed compromised respiration rates and were more sensitive to drought. Our results demonstrated that an operational ETF/ETFQO pathway is associated with plants' ability to withstand drought and to recover growth once water becomes replete. Drought-induced metabolic reprogramming resulted in an increase in tricarboxylic acid (TCA) cycle intermediates and total amino acid levels, as well as decreases in protein, starch and nitrate contents. The enhanced levels of the branched-chain amino acids in loss-of-function mutants appear to be related to their increased utilization as substrates for the TCA cycle under water stress. Our results thus show that mitochondrial metabolism is highly active during drought stress responses and provide support for a role of alternative respiratory pathways within this response. © 2015 John Wiley & Sons Ltd.

Suicide Inhibition of Cytochrome P450 Enzymes by Cyclopropylamines via a Ring-opening Mechanism: Proton-Coupled Electron Transfer Makes a Difference

NASA Astrophysics Data System (ADS)

Zhang, Xiaoqian; Li, Xiao-Xi; Liu, Yufang; Wang, Yong

2017-01-01

N-benzyl-N-cyclopropylamine (BCA) has been attracting great interests for decades for its partial suicide inactivation role to cytochrome P450 (P450) via a ring-opening mechanism besides acting as a role of normal substrates. Understanding the mechanism of such partial inactivation is vital to the clinical drug design. Thus, density functional theoretical (DFT) calculations were carried out on such P450-catalyzed reactions, not only on the metabolic pathway, but on the ring-opening inactivation one. Our theoretical results demonstrated that, in the metabolic pathway, besides the normal carbinolamine, an unexpected enamine was formed via the dual hydrogen abstraction (DHA) process, in which the competition between rotation of the H-abstracted substrate radical and the rotation of hydroxyl group of the protonated Cpd II moiety plays a significant role in product branch; In the inactivation pathway, the well-noted single electron transfer (SET) mechanism-involved process was invalidated for its high energy barrier, a proton-coupled electron transfer (PCET(ET)) mechanism plays a role. Our results are consistent with other related theoretical works on heteroatom-hydrogen (X-H, X = O, N) activation and revealed new features. The revealed mechanisms will play a positive role in relative drug design.

Analysis of the complex formation, interaction and electron transfer pathway between the "open" conformation of NADPH-cytochrome P450 reductase and aromatase.

PubMed

Dai, Yuejie; Zhen, Jing; Zhang, Xiuli; Zhong, Yonghui; Liu, Shaodan; Sun, Ziyue; Guo, Yue; Wu, Qingli

2015-09-01

The complex structure of human aromatase (CYP19) and the open form of ΔTGEE mutant NADPH-cytochrome P450 reductase (mCPR) was constructed using template-based protein alignment method. Dynamic simulation of formed complex was performed on NAMD 2.9, in which CHARMm all 27_prot_lipid_na force field and an explicit TIP3P water solvent model were applied. The result showed mCPR in its open conformation could steadily combine with aromatase from the proximal face. Data analysis indicates hydrogen bonds and four salt bridges on the binding surface enhance the interaction between the two protein molecules. Amino acid, Lys108 plays a key role in aromatase activity through the formation of a salt bridge with Asp147 and two hydrogen bonds with Asp147 and Gln150 in mCPR. The optimal pathway for the first electron transfer from CPR to aromatase was revealed and calculated using HARLEM software. The rates for solvent mediated and non-solvent mediated electron transfer from FMNH2 to heme were determined as 1.04×10(6)s(-)(1) and 4.86×10(5)s(-)(1) respectively, which indicates the solvent water can facilitate the electron transfer from FMNH2 to heme. This study presents a novel strategy for the study of the protein-protein interactions based on the template-based protein alignment, which may help new aromtase development targeting the electron transfer between mCPR and aromatase. Copyright © 2015 Elsevier Inc. All rights reserved.

Consecutive Fragmentation Mechanisms of Protonated Ferulic Acid Probed by Infrared Multiple Photon Dissociation Spectroscopy and Electronic Structure Calculations

NASA Astrophysics Data System (ADS)

Martens, Sabrina M.; Marta, Rick A.; Martens, Jonathan K.; McMahon, Terry B.

2012-10-01

Protonated ferulic acid and its principle fragment ion have been characterized using infrared multiple photon dissociation spectroscopy and electronic structure calculations at the B3LYP/6-311 + G(d,p) level of theory. Due to its extensively conjugated structure, protonated ferulic acid is observed to yield three stable fragment ions in IRMPD experiments. It is proposed that two parallel fragmentation pathways of protonated ferulic acid are being observed. The first pathway involves proton transfer, resulting in the loss of water and subsequently carbon monoxide, producing fragment ions m/z 177 and 149, respectively. Optimization of m/z 177 yields a species containing an acylium group, which is supported by a diagnostic peak in the IRMPD spectrum at 2168 cm-1. The second pathway involves an alternate proton transfer leading to loss of methanol and rearrangement to a five-membered ring.

The Use of Chemical Probes for the Characterization of the Predominant Abiotic Reductants in Anaerobic Sediments

EPA Science Inventory

Identifying the predominant chemical reductants and pathways for electron transfer in anaerobic systems is paramount to the development of environmental fate models that incorporate pathways for abiotic reductive transformations. Currently, such models do not exist. In this chapt...

Mechanisms and Rates of U(VI) Reduction by Fe(II) in Homogeneous Aqueous Solution and the Role of U(V) Disproportionation

DOE Office of Scientific and Technical Information (OSTI.GOV)

Collins, Richard N.; Rosso, Kevin M.

Molecular-level pathways in the aqueous redox transformation of uranium by iron remain unclear, despite the importance of this knowledge for predicting uranium transport and distribution in natural and engineered environments. As the relative importance of homogeneous versus heterogeneous pathways is difficult to probe experimentally, here we apply computational molecular simulation to isolate rates of key one electron transfer reactions in the homogeneous pathway. By comparison to experimental observations the role of the heterogeneous pathway also becomes clear. Density functional theory (DFT) and Marcus theory calculations for all primary monomeric species at pH values ≤7 show for UO22+ and its hydrolysismore » species UO2OH+ and UO2(OH)20 that reduction by Fe2+ is thermodynamically favorable, though kinetically limited for UO22+. An inner-sphere encounter complex between UO2OH+ and Fe2+ was the most stable for the first hydrolysis species and displayed an electron transfer rate constant ket = 4.3 × 103 s-1. Three stable inner- and outer-sphere encounter complexes between UO2(OH)20 and Fe2+ were found, with electron transfer rate constants ranging from ket = 7.6 × 102 to 7.2 × 104 s-1. Homogeneous reduction of these U(VI) hydrolysis species to U(V) is, therefore, predicted to be facile. In contrast, homogeneous reduction of UO2+ by Fe2+ was found to be thermodynamically unfavorable, suggesting the possible importance of U(V)-U(V) disproportionation as a route to U(IV). Calculations on homogeneous disproportionation, however, while yielding a stable outer-sphere U(V)-U(V) encounter complex, indicate that this electron transfer reaction is not feasible at circumneutral pH. Protonation of both axial O atoms of acceptor U(V) (i.e., by H3O+) was found to be a prerequisite to stabilize U(IV), consistent with the experimental observation that the rate of this reaction is inversely correlated with pH. Thus, despite prevailing notions that U(V) is rapidly eliminated by homogeneous disproportionation, this pathway is irrelevant at environmental conditions.« less

Osm1 facilitates the transfer of electrons from Erv1 to fumarate in the redox-regulated import pathway in the mitochondrial intermembrane space.

PubMed

Neal, Sonya E; Dabir, Deepa V; Wijaya, Juwina; Boon, Cennyana; Koehler, Carla M

2017-10-15

Prokaryotes have aerobic and anaerobic electron acceptors for oxidative folding of periplasmic proteins. The mitochondrial intermembrane space has an analogous pathway with the oxidoreductase Mia40 and sulfhydryl oxidase Erv1, termed the mitochondrial intermembrane space assembly (MIA) pathway. The aerobic electron acceptors include oxygen and cytochrome c , but an acceptor that can function under anaerobic conditions has not been identified. Here we show that the fumarate reductase Osm1, which facilitates electron transfer from fumarate to succinate, fills this gap as a new electron acceptor. In addition to microsomes, Osm1 localizes to the mitochondrial intermembrane space and assembles with Erv1 in a complex. In reconstitution studies with reduced Tim13, Mia40, and Erv1, the addition of Osm1 and fumarate completes the disulfide exchange pathway that results in Tim13 oxidation. From in vitro import assays, mitochondria lacking Osm1 display decreased import of MIA substrates, Cmc1 and Tim10. Comparative reconstitution assays support that the Osm1/fumarate couple accepts electrons with similar efficiency to cytochrome c and that the cell has strategies to coordinate expression of the terminal electron acceptors. Thus Osm1/fumarate is a new electron acceptor couple in the mitochondrial intermembrane space that seems to function in both aerobic and anaerobic conditions. © 2017 Neal et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0).

Photosynthetic Membranes of Synechocystis or Plants Convert Sunlight to Photocurrent through Different Pathways due to Different Architectures.

PubMed

Pinhassi, Roy I; Kallmann, Dan; Saper, Gadiel; Larom, Shirley; Linkov, Artyom; Boulouis, Alix; Schöttler, Mark-Aurel; Bock, Ralph; Rothschild, Avner; Adir, Noam; Schuster, Gadi

2015-01-01

Thylakoid membranes contain the redox active complexes catalyzing the light-dependent reactions of photosynthesis in cyanobacteria, algae and plants. Crude thylakoid membranes or purified photosystems from different organisms have previously been utilized for generation of electrical power and/or fuels. Here we investigate the electron transferability from thylakoid preparations from plants or the cyanobacterium Synechocystis. We show that upon illumination, crude Synechocystis thylakoids can reduce cytochrome c. In addition, this crude preparation can transfer electrons to a graphite electrode, producing an unmediated photocurrent of 15 μA/cm2. Photocurrent could be obtained in the presence of the PSII inhibitor DCMU, indicating that the source of electrons is QA, the primary Photosystem II acceptor. In contrast, thylakoids purified from plants could not reduce cyt c, nor produced a photocurrent in the photocell in the presence of DCMU. The production of significant photocurrent (100 μA/cm2) from plant thylakoids required the addition of the soluble electron mediator DCBQ. Furthermore, we demonstrate that use of crude thylakoids from the D1-K238E mutant in Synechocystis resulted in improved electron transferability, increasing the direct photocurrent to 35 μA/cm2. Applying the analogous mutation to tobacco plants did not achieve an equivalent effect. While electron abstraction from crude thylakoids of cyanobacteria or plants is feasible, we conclude that the site of the abstraction of the electrons from the thylakoids, the architecture of the thylakoid preparations influence the site of the electron abstraction, as well as the transfer pathway to the electrode. This dictates the use of different strategies for production of sustainable electrical current from photosynthetic thylakoid membranes of cyanobacteria or higher plants.

Distal [FeS]-Cluster Coordination in [NiFe]-Hydrogenase Facilitates Intermolecular Electron Transfer

PubMed Central

Petrenko, Alexander; Stein, Matthias

2017-01-01

Biohydrogen is a versatile energy carrier for the generation of electric energy from renewable sources. Hydrogenases can be used in enzymatic fuel cells to oxidize dihydrogen. The rate of electron transfer (ET) at the anodic side between the [NiFe]-hydrogenase enzyme distal iron–sulfur cluster and the electrode surface can be described by the Marcus equation. All parameters for the Marcus equation are accessible from Density Functional Theory (DFT) calculations. The distal cubane FeS-cluster has a three-cysteine and one-histidine coordination [Fe4S4](His)(Cys)3 first ligation sphere. The reorganization energy (inner- and outer-sphere) is almost unchanged upon a histidine-to-cysteine substitution. Differences in rates of electron transfer between the wild-type enzyme and an all-cysteine mutant can be rationalized by a diminished electronic coupling between the donor and acceptor molecules in the [Fe4S4](Cys)4 case. The fast and efficient electron transfer from the distal iron–sulfur cluster is realized by a fine-tuned protein environment, which facilitates the flow of electrons. This study enables the design and control of electron transfer rates and pathways by protein engineering. PMID:28067774

Commonalities and differences in plants deficient in autophagy and alternative pathways of respiration on response to extended darkness.

PubMed

Barros, Jessica A S; Cavalcanti, João Henrique F; Medeiros, David B; Nunes-Nesi, Adriano; Avin-Wittenberg, Tamar; Fernie, Alisdair R; Araújo, Wagner L

2017-11-02

Autophagy is a highly conserved cellular mechanism in eukaryotes allowing the degradation of cell constituents. It is of crucial significance in both cellular homeostasis and nutrient recycling. During energy limited conditions plant cells can metabolize alternative respiratory substrates, such as amino acids, providing electrons to the mitochondrial metabolism via the tricarboxylic acid (TCA) cycle or electron transfer flavoprotein/ electron transfer flavoprotein ubiquinone oxidoreductase (ETF/ETFQO) system. Our recent study reveals the importance of autophagy in the supply of amino acids to provide energy through alternative pathways of respiration during carbon starvation. This fact apart, autophagy seems to have more generalized effects related not only to amino acid catabolism but also to metabolism in general. By further comparing the metabolic data obtained with atg mutants with those of mutants involved in the alternative pathways of respiration, we observed clear differences between these mutants, pointing out additional effects of the autophagy deficiency on metabolism of Arabidopsis leaves. Collectively, our data point to an interdependence between mitochondrial metabolism and autophagy and suggest an exquisite regulation of primary metabolism under low energetic conditions.

Enhancing Bidirectional Electron Transfer of Shewanella oneidensis by a Synthetic Flavin Pathway.

PubMed

Yang, Yun; Ding, Yuanzhao; Hu, Yidan; Cao, Bin; Rice, Scott A; Kjelleberg, Staffan; Song, Hao

2015-07-17

Flavins regulate the rate and direction of extracellular electron transfer (EET) in Shewanella oneidensis. However, low concentration of endogenously secreted flavins by the wild-type S. oneidensis MR-1 limits its EET efficiency in bioelectrochemical systems (BES). Herein, a synthetic flavin biosynthesis pathway from Bacillus subtilis was heterologously expressed in S. oneidensis MR-1, resulting in ∼25.7 times' increase in secreted flavin concentration. This synthetic flavin module enabled enhanced bidirectional EET rate of MR-1, in which its maximum power output in microbial fuel cells increased ∼13.2 times (from 16.4 to 233.0 mW/m(2)), and the inward current increased ∼15.5 times (from 15.5 to 255.3 μA/cm(2)).

Chemoselective reduction and oxidation of ketones in water through control of the electron transfer pathway

PubMed Central

Kim, Sun Min; Yoo, Ho Sung; Hosono, Hideo; Yang, Jung Woon; Kim, Sung Wng

2015-01-01

The selective synthesis of different products from the same starting materials in water, which is the most abundant solvent in nature, is a crucial issue as it maximizes the utilization of materials. Realizing such reactions for ketones is of considerable importance because numerous organic functionalities can be obtained via nucleophilic addition reactions. Herein, we report chemoselective reduction and oxidation reactions of 1,2-diketones in water, which initiates anionic electron transfer from the inorganic electride [Ca24Al28O64]4+·4e−, through controlling the pathway of the electrons to substrates. The generation of different radical species for transient intermediates was the key process required to control the reaction selectivity, which was achieved by reacting the anionic electrons with either diketones or O2, leading to the formation of ketyl dianion and superoxide radicals in the reduction and oxidation reactions, respectively. This methodology that utilizes electrides may provide an alternative to the pulse radiolysis of water in synthetic chemistry. PMID:26020413

Constraint-based modeling of carbon fixation and the energetics of electron transfer in Geobacter metallireducens.

PubMed

Feist, Adam M; Nagarajan, Harish; Rotaru, Amelia-Elena; Tremblay, Pier-Luc; Zhang, Tian; Nevin, Kelly P; Lovley, Derek R; Zengler, Karsten

2014-04-01

Geobacter species are of great interest for environmental and biotechnology applications as they can carry out direct electron transfer to insoluble metals or other microorganisms and have the ability to assimilate inorganic carbon. Here, we report on the capability and key enabling metabolic machinery of Geobacter metallireducens GS-15 to carry out CO2 fixation and direct electron transfer to iron. An updated metabolic reconstruction was generated, growth screens on targeted conditions of interest were performed, and constraint-based analysis was utilized to characterize and evaluate critical pathways and reactions in G. metallireducens. The novel capability of G. metallireducens to grow autotrophically with formate and Fe(III) was predicted and subsequently validated in vivo. Additionally, the energetic cost of transferring electrons to an external electron acceptor was determined through analysis of growth experiments carried out using three different electron acceptors (Fe(III), nitrate, and fumarate) by systematically isolating and examining different parts of the electron transport chain. The updated reconstruction will serve as a knowledgebase for understanding and engineering Geobacter and similar species.

Dioxygen in Polyoxometalate Mediated Reactions.

PubMed

Weinstock, Ira A; Schreiber, Roy E; Neumann, Ronny

2018-03-14

In this review article, we consider the use of molecular oxygen in reactions mediated by polyoxometalates. Polyoxometalates are anionic metal oxide clusters of a variety of structures that are soluble in liquid phases and therefore amenable to homogeneous catalytic transformations. Often, they are active for electron transfer oxidations of a myriad of substrates and upon reduction can be reoxidized by molecular oxygen. For example, the phosphovanadomolybdate, H 5 PV 2 Mo 10 O 40 , can oxidize Pd(0) thereby enabling aerobic reactions catalyzed by Pd and H 5 PV 2 Mo 10 O 40 . In a similar vein, polyoxometalates can stabilize metal nanoparticles, leading to additional transformations. Furthermore, electron transfer oxidation of other substrates such as halides and sulfur-containing compounds is possible. More uniquely, H 5 PV 2 Mo 10 O 40 and its analogues can mediate electron transfer-oxygen transfer reactions where oxygen atoms are transferred from the polyoxometalate to the substrate. This unique property has enabled correspondingly unique transformations involving carbon-carbon, carbon-hydrogen, and carbon-metal bond activation. The pathway for the reoxidation of vanadomolybdates with O 2 appears to be an inner-sphere reaction, but the oxidation of one-electron reduced polyoxotungstates has been shown through intensive research to be an outer-sphere reaction. Beyond electron transfer and electron transfer-oxygen transfer aerobic transformations, there a few examples of apparent dioxygenase activity where both oxygen atoms are donated to a substrate.

Photoemission into water adsorbed on metals: Probing dissociative electron transfer using theory

NASA Astrophysics Data System (ADS)

Zhang, Yu; Whitten, J. L.

The photoinduced dissociation of water adsorbed on a silver nanoparticle is explored using theory to probe reaction pathways that produce hydrogen. Ab initio configuration theory is used to describe the systems. A formulation that allows excited electronic states embedded in a near continuum of lower energy states to be calculated accurately is described. Electron attachment of a photoemitted electron to adsorbed water can lead to the formation of H2 at a very low energy barrier with oxygen remaining on the Ag surface. A large energy barrier to form H2 plus adsorbed O is found for the ground state. The excited state has a much smaller barrier to OH stretch; however, to dissociate, the system must cross over from the excited state to the ground state potential energy surface. The cross over point is near the transition state for a ground state process. A characteristic feature of the excited state potential curve is an increase in energy in the early stages of OH stretch as the charge transfer state evolves from a state with considerable Rydberg character to one that has a typical OH antibonding molecular orbital. Another pathway releases a H atom leaving OH on the surface. Effects due to doping of a Ag nanoparticle with a K electron donor atom are compared with those caused by a Fermi level shift due to an applied potential. Results are also reported for electron transfer to a solvated lithium ion, Li(H2O) 6+, near the surface of a silver particle. A steering mechanism is found that involves the interaction of a hydridic hydrogen formed after electron transfer with an acidic hydrogen of a second solvated water molecule.

Cytochrome bc1 complexes of microorganisms.

PubMed Central

Trumpower, B L

1990-01-01

The cytochrome bc1 complex is the most widely occurring electron transfer complex capable of energy transduction. Cytochrome bc1 complexes are found in the plasma membranes of phylogenetically diverse photosynthetic and respiring bacteria, and in the inner mitochondrial membrane of all eucaryotic cells. In all of these species the bc1 complex transfers electrons from a low-potential quinol to a higher-potential c-type cytochrome and links this electron transfer to proton translocation. Most bacteria also possess alternative pathways of quinol oxidation capable of circumventing the bc1 complex, but these pathways generally lack the energy-transducing, protontranslocating activity of the bc1 complex. All cytochrome bc1 complexes contain three electron transfer proteins which contain four redox prosthetic groups. These are cytochrome b, which contains two b heme groups that differ in their optical and thermodynamic properties; cytochrome c1, which contains a covalently bound c-type heme; and a 2Fe-2S iron-sulfur protein. The mechanism which links proton translocation to electron transfer through these proteins is the proton motive Q cycle, and this mechanism appears to be universal to all bc1 complexes. Experimentation is currently focused on understanding selected structure-function relationships prerequisite for these redox proteins to participate in the Q-cycle mechanism. The cytochrome bc1 complexes of mitochondria differ from those of bacteria, in that the former contain six to eight supernumerary polypeptides, in addition to the three redox proteins common to bacteria and mitochondria. These extra polypeptides are encoded in the nucleus and do not contain redox prosthetic groups. The functions of the supernumerary polypeptides of the mitochondrial bc1 complexes are generally not known and are being actively explored by genetically manipulating these proteins in Saccharomyces cerevisiae. Images PMID:2163487

Genome-scale stoichiometry analysis to elucidate the innate capability of the cyanobacterium Synechocystis for electricity generation.

PubMed

Mao, Longfei; Verwoerd, Wynand S

2013-10-01

Synechocystis sp. PCC 6803 has been considered as a promising biocatalyst for electricity generation in recent microbial fuel cell research. However, the innate maximum current production potential and underlying metabolic pathways supporting the high current output are still unknown. This is mainly due to the fact that the high-current production cell phenotype results from the interaction among hundreds of reactions in the metabolism and it is impossible for reductionist methods to characterize the pathway selection in such a metabolic state. In this study, we employed computational metabolic techniques, flux balance analysis, and flux variability analysis, to exploit the maximum current outputs of Synechocystis sp. PCC 6803, in five electron transfer cases, namely, ferredoxin- and plastoquinol-dependent electron transfers under photoautotrophic cultivation, and NADH-dependent mediated electron transfer under photoautotrophic, heterotrophic, and mixotrophic conditions. In these five modes, the maximum current outputs were computed as 0.198, 0.7918, 0.198, 0.4652, and 0.4424 A gDW⁻¹, respectively. Comparison of the five operational modes suggests that plastoquinol-/c-type cytochrome-targeted electricity generation had an advantage of liberating the highest current output achievable for Synechocystis sp. PCC 6803. On the other hand, the analysis indicates that the currency metabolite, NADH-, dependent electricity generation can rely on a number of reactions from different pathways, and is thus more robust against environmental perturbations.

Observation of correlated electronic decay in expanding clusters triggered by near-infrared fields

PubMed Central

Schütte, B.; Arbeiter, M.; Fennel, T.; Jabbari, G.; Kuleff, A.I.; Vrakking, M.J.J.; Rouzée, A.

2015-01-01

When an excited atom is embedded into an environment, novel relaxation pathways can emerge that are absent for isolated atoms. A well-known example is interatomic Coulombic decay, where an excited atom relaxes by transferring its excess energy to another atom in the environment, leading to its ionization. Such processes have been observed in clusters ionized by extreme-ultraviolet and X-ray lasers. Here, we report on a correlated electronic decay process that occurs following nanoplasma formation and Rydberg atom generation in the ionization of clusters by intense, non-resonant infrared laser fields. Relaxation of the Rydberg states and transfer of the available electronic energy to adjacent electrons in Rydberg states or quasifree electrons in the expanding nanoplasma leaves a distinct signature in the electron kinetic energy spectrum. These so far unobserved electron-correlation-driven energy transfer processes may play a significant role in the response of any nano-scale system to intense laser light. PMID:26469997

From Cholesterogenesis to Steroidogenesis: Role of Riboflavin and Flavoenzymes in the Biosynthesis of Vitamin D12

PubMed Central

Pinto, John T.; Cooper, Arthur J. L.

2014-01-01

Flavin-dependent monooxygenases and oxidoreductases are located at critical branch points in the biosynthesis and metabolism of cholesterol and vitamin D. These flavoproteins function as obligatory intermediates that accept 2 electrons from NAD(P)H with subsequent 1-electron transfers to a variety of cytochrome P450 (CYP) heme proteins within the mitochondria matrix (type I) and the (microsomal) endoplasmic reticulum (type II). The mode of electron transfer in these systems differs slightly in the number and form of the flavin prosthetic moiety. In the type I mitochondrial system, FAD-adrenodoxin reductase interfaces with adrenodoxin before electron transfer to CYP heme proteins. In the microsomal type II system, a diflavin (FAD/FMN)-dependent cytochrome P450 oxidoreductase [NAD(P)H-cytochrome P450 reductase (CPR)] donates electrons to a multitude of heme oxygenases. Both flavoenzyme complexes exhibit a commonality of function with all CYP enzymes and are crucial for maintaining a balance of cholesterol and vitamin D metabolites. Deficits in riboflavin availability, imbalances in the intracellular ratio of FAD to FMN, and mutations that affect flavin binding domains and/or interactions with client proteins result in marked structural alterations within the skeletal and central nervous systems similar to those of disorders (inborn errors) in the biosynthetic pathways that lead to cholesterol, steroid hormones, and vitamin D and their metabolites. Studies of riboflavin deficiency during embryonic development demonstrate congenital malformations similar to those associated with genetic alterations of the flavoenzymes in these pathways. Overall, a deeper understanding of the role of riboflavin in these pathways may prove essential to targeted therapeutic designs aimed at cholesterol and vitamin D metabolism. PMID:24618756

Electrochemically enhanced microbial CO conversion to volatile fatty acids using neutral red as an electron mediator.

PubMed

Im, Chae Ho; Kim, Changman; Song, Young Eun; Oh, Sang-Eun; Jeon, Byong-Hun; Kim, Jung Rae

2018-01-01

Conversion of C1 gas feedstock, including carbon monoxide (CO), into useful platform chemicals has attracted considerable interest in industrial biotechnology. Nevertheless, the low conversion yield and/or growth rate of CO-utilizing microbes make it difficult to develop a C1 gas biorefinery process. The Wood-Ljungdahl pathway which utilize CO is a pathway suffered from insufficient electron supply, in which the conversion can be increased further when an additional electron source like carbohydrate or hydrogen is provided. In this study, electrode-based electron transference using a bioelectrochemical system (BES) was examined to compensate for the insufficient reducing equivalent and increase the production of volatile fatty acids. The BES including neutral red (BES-NR), which facilitated electron transfer between bacteria and electrode, was compared with BES without neutral red and open circuit control. The coulombic efficiency based on the current input to the system and the electrons recovered into VFAs, was significantly higher in BES-NR than the control. These results suggest that the carbon electrode provides a platform to regulate the redox balance for improving the bioconversion of CO, and amending the conventional C1 gas fermentation. Copyright © 2017 Elsevier Ltd. All rights reserved.

Photoinduced electron transfer (PET) versus excimer formation in supramolecular p/n-heterojunctions of perylene bisimide dyes and implications for organic photovoltaics.

PubMed

Nowak-Król, Agnieszka; Fimmel, Benjamin; Son, Minjung; Kim, Dongho; Würthner, Frank

2015-01-01

Foldamer systems comprised of two perylene bisimide (PBI) dyes attached to the conjugated backbones of 1,2-bis(phenylethynyl)benzene and phenylethynyl-bis(phenylene)indane, respectively, were synthesized and investigated with regard to their solvent-dependent properties. UV/Vis absorption and steady-state fluorescence spectra show that both foldamers exist predominantly in a folded H-aggregated state consisting of π-π-stacked PBIs in THF and in more random conformations with weaker excitonic coupling between the PBIs in chloroform. Time-resolved fluorescence spectroscopy and transient absorption spectroscopy reveal entirely different relaxation pathways for the photoexcited molecules in the given solvents, i.e. photoinduced electron transfer leading to charge separated states for the open conformations (in chloroform) and relaxation into excimer states with red-shifted emission for the stacked conformations (in THF). Supported by redox data from cyclic voltammetry and Rehm-Weller analysis we could relate the processes occurring in these solution-phase model systems to the elementary processes in organic solar cells. Accordingly, only if relaxation pathways such as excimer formation are strictly avoided in molecular semiconductor materials, excitons may diffuse over larger distances to the heterojunction interface and produce photocurrent via the formation of electron/hole pairs by photoinduced electron transfer.

Role of the HoxZ subunit in the electron transfer pathway of the membrane-bound [NiFe]-hydrogenase from Ralstonia eutropha immobilized on electrodes.

PubMed

Sezer, Murat; Frielingsdorf, Stefan; Millo, Diego; Heidary, Nina; Utesch, Tillman; Mroginski, Maria-Andrea; Friedrich, Bärbel; Hildebrandt, Peter; Zebger, Ingo; Weidinger, Inez M

2011-09-01

The role of the diheme cytochrome b (HoxZ) subunit in the electron transfer pathway of the membrane-bound [NiFe]-hydrogenase (MBH) heterotrimer from Ralstonia eutropha H16 has been investigated. The MBH in its native heterotrimeric state was immobilized on electrodes and subjected to spectroscopic and electrochemical analysis. Surface enhanced resonance Raman spectroscopy was used to monitor the redox and coordination state of the HoxZ heme cofactors while concomitant protein film voltammetric measurements gave insights into the catalytic response of the enzyme on the electrode. The entire MBH heterotrimer as well as its isolated HoxZ subunit were immobilized on silver electrodes coated with self-assembled monolayers of ω-functionalized alkylthiols, displaying the preservation of the native heme pocket structure and an electrical communication between HoxZ and the electrode. For the immobilized MBH heterotrimer, catalytic reduction of the HoxZ heme cofactors was observed upon H(2) addition. The catalytic currents of MBH with and without the HoxZ subunit were measured and compared with the heterogeneous electron transfer rates of the isolated HoxZ. On the basis of the spectroscopic and electrochemical results, we conclude that the HoxZ subunit under these artificial conditions is not primarily involved in the electron transfer to the electrode but plays a crucial role in stabilizing the enzyme on the electrode. © 2011 American Chemical Society

On the nature of organic and inorganic centers that bifurcate electrons, coupling exergonic and endergonic oxidation-reduction reactions.

PubMed

Peters, John W; Beratan, David N; Schut, Gerrit J; Adams, Michael W W

2018-04-19

Bifurcating electrons to couple endergonic and exergonic electron-transfer reactions has been shown to have a key role in energy conserving redox enzymes. Bifurcating enzymes require a redox center that is capable of directing electron transport along two spatially separate pathways. Research into the nature of electron bifurcating sites indicates that one of the keys is the formation of a low potential oxidation state to satisfy the energetics required of the endergonic half reaction, indicating that any redox center (organic or inorganic) that can exist in multiple oxidation states with sufficiently separated redox potentials should be capable of electron bifurcation. In this Feature Article, we explore a paradigm for bifurcating electrons down independent high and low potential pathways, and describe redox cofactors that have been demonstrated or implicated in driving this unique biochemistry.

Reaction pathways of producing and losing particles in atmospheric pressure methane nanosecond pulsed needle-plane discharge plasma

NASA Astrophysics Data System (ADS)

Zhao, Yuefeng; Wang, Chao; Li, Li; Wang, Lijuan; Pan, Jie

2018-03-01

In this work, a two-dimensional fluid model is built up to numerically investigate the reaction pathways of producing and losing particles in atmospheric pressure methane nanosecond pulsed needle-plane discharge plasma. The calculation results indicate that the electron collisions with CH4 are the key pathways to produce the neutral particles CH2 and CH as well as the charged particles e and CH3+. CH3, H2, H, C2H2, and C2H4 primarily result from the reactions between the neutral particles and CH4. The charge transfer reactions are the significant pathways to produce CH4+, C2H2+, and C2H4+. As to the neutral species CH and H and the charged species CH3+, the reactions between themselves and CH4 contribute to substantial losses of these particles. The ways responsible for losing CH3, H2, C2H2, and C2H4 are CH3 + H → CH4, H2 + CH → CH2 + H, CH4+ + C2H2 → C2H2+ + CH4, and CH4+ + C2H4 → C2H4+ + CH4, respectively. Both electrons and C2H4+ are consumed by the dissociative electron-ion recombination reactions. The essential reaction pathways of losing CH4+ and C2H2+ are the charge transfer reactions.

Electron Transfer Mechanisms of DNA Repair by Photolyase

NASA Astrophysics Data System (ADS)

Zhong, Dongping

2015-04-01

Photolyase is a flavin photoenzyme that repairs two DNA base damage products induced by ultraviolet (UV) light: cyclobutane pyrimidine dimers and 6-4 photoproducts. With femtosecond spectroscopy and site-directed mutagenesis, investigators have recently made significant advances in our understanding of UV-damaged DNA repair, and the entire enzymatic dynamics can now be mapped out in real time. For dimer repair, six elementary steps have been characterized, including three electron transfer reactions and two bond-breaking processes, and their reaction times have been determined. A unique electron-tunneling pathway was identified, and the critical residues in modulating the repair function at the active site were determined. The dynamic synergy between the elementary reactions for maintaining high repair efficiency was elucidated, and the biological nature of the flavin active state was uncovered. For 6-4 photoproduct repair, a proton-coupled electron transfer repair mechanism has been revealed. The elucidation of electron transfer mechanisms and two repair photocycles is significant and provides a molecular basis for future practical applications, such as in rational drug design for curing skin cancer.

Nanopore Electrochemistry: A Nexus for Molecular Control of Electron Transfer Reactions

PubMed Central

2018-01-01

Pore-based structures occur widely in living organisms. Ion channels embedded in cell membranes, for example, provide pathways, where electron and proton transfer are coupled to the exchange of vital molecules. Learning from mother nature, a recent surge in activity has focused on artificial nanopore architectures to effect electrochemical transformations not accessible in larger structures. Here, we highlight these exciting advances. Starting with a brief overview of nanopore electrodes, including the early history and development of nanopore sensing based on nanopore-confined electrochemistry, we address the core concepts and special characteristics of nanopores in electron transfer. We describe nanopore-based electrochemical sensing and processing, discuss performance limits and challenges, and conclude with an outlook for next-generation nanopore electrode sensing platforms and the opportunities they present. PMID:29392173

Cucumber possesses a single terminal alternative oxidase gene that is upregulated by cold stress and in the mosaic (MSC) mitochondrial mutants

USDA-ARS?s Scientific Manuscript database

In plants alternative oxidase (AOX) is an important nuclear-encoded enzyme active in the mitochondrial electron-transport chain, transferring electrons from ubiquinol to alternative oxidase instead of the cytochrome pathway to yield ubiquinone and water. AOX protects against unexpected inhibition of...

Mechanically Controlled Electron Transfer in a Single-Polypeptide Transistor

NASA Astrophysics Data System (ADS)

Sheu, Sheh-Yi; Yang, Dah-Yen

2017-01-01

Proteins are of interest in nano-bio electronic devices due to their versatile structures, exquisite functionality and specificity. However, quantum transport measurements produce conflicting results due to technical limitations whereby it is difficult to precisely determine molecular orientation, the nature of the moieties, the presence of the surroundings and the temperature; in such circumstances a better understanding of the protein electron transfer (ET) pathway and the mechanism remains a considerable challenge. Here, we report an approach to mechanically drive polypeptide flip-flop motion to achieve a logic gate with ON and OFF states during protein ET. We have calculated the transmission spectra of the peptide-based molecular junctions and observed the hallmarks of electrical current and conductance. The results indicate that peptide ET follows an NC asymmetric process and depends on the amino acid chirality and α-helical handedness. Electron transmission decreases as the number of water molecules increases, and the ET efficiency and its pathway depend on the type of water-bridged H-bonds. Our results provide a rational mechanism for peptide ET and new perspectives on polypeptides as potential candidates in logic nano devices.

Differential Electrochemical Conductance Imaging at the Nanoscale.

PubMed

López-Martínez, Montserrat; Artés, Juan Manuel; Sarasso, Veronica; Carminati, Marco; Díez-Pérez, Ismael; Sanz, Fausto; Gorostiza, Pau

2017-09-01

Electron transfer in proteins is essential in crucial biological processes. Although the fundamental aspects of biological electron transfer are well characterized, currently there are no experimental tools to determine the atomic-scale electronic pathways in redox proteins, and thus to fully understand their outstanding efficiency and environmental adaptability. This knowledge is also required to design and optimize biomolecular electronic devices. In order to measure the local conductance of an electrode surface immersed in an electrolyte, this study builds upon the current-potential spectroscopic capacity of electrochemical scanning tunneling microscopy, by adding an alternating current modulation technique. With this setup, spatially resolved, differential electrochemical conductance images under bipotentiostatic control are recorded. Differential electrochemical conductance imaging allows visualizing the reversible oxidation of an iron electrode in borate buffer and individual azurin proteins immobilized on atomically flat gold surfaces. In particular, this method reveals submolecular regions with high conductance within the protein. The direct observation of nanoscale conduction pathways in redox proteins and complexes enables important advances in biochemistry and bionanotechnology. © 2017 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

Electron transfer of Pseudomonas aeruginosa CP1 in electrochemical reduction of nitric oxide.

PubMed

Zhou, Shaofeng; Huang, Shaobin; He, Jiaxin; Li, Han; Zhang, Yongqing

2016-10-01

This study reports catalytic electro-chemical reduction of nitric oxide (NO) enhanced by Pseudomonas aeruginosa strain CP1. The current generated in the presence of bacteria was 4.36times that in the absence of the bacteria. The strain was able to catalyze electro-chemical reduction of NO via indirect electron transfer with an electrode, revealed by a series of cyclic voltammetry experiments. Soluble electron shuttles secreted into solution by live bacteria were responsible for the catalytic effects. The enhancement of NO reduction was also confirmed by detection of nitrous oxide; the level of this intermediate was 46.4% higher in the presence of bacteria than in controls, illustrated that the electron transfer pathway did not directly reduce nitric oxide to N2. The findings of this study may offer a new model for bioelectrochemical research in the field of NO removal by biocatalysts. Copyright © 2016 Elsevier Ltd. All rights reserved.

Model-based confirmation of alternative substrates of mitochondrial electron transport chain.

PubMed

Kleessen, Sabrina; Araújo, Wagner L; Fernie, Alisdair R; Nikoloski, Zoran

2012-03-30

Discrimination of metabolic models based on high throughput metabolomics data, reflecting various internal and external perturbations, is essential for identifying the components that contribute to the emerging behavior of metabolic processes. Here, we investigate 12 different models of the mitochondrial electron transport chain (ETC) in Arabidopsis thaliana during dark-induced senescence in order to elucidate the alternative substrates to this metabolic pathway. Our findings demonstrate that the coupling of the proposed computational approach, based on dynamic flux balance analysis, with time-resolved metabolomics data results in model-based confirmations of the hypotheses that, during dark-induced senescence in Arabidopsis, (i) under conditions where the main substrate for the ETC are not fully available, isovaleryl-CoA dehydrogenase and 2-hydroxyglutarate dehydrogenase are able to donate electrons to the ETC, (ii) phytanoyl-CoA does not act even as an indirect substrate of the electron transfer flavoprotein/electron-transfer flavoprotein:ubiquinone oxidoreductase complex, and (iii) the mitochondrial γ-aminobutyric acid transporter has functional significance in maintaining mitochondrial metabolism. Our study provides a basic framework for future in silico studies of alternative pathways in mitochondrial metabolism under extended darkness whereby the role of its components can be computationally discriminated based on available molecular profile data.

Electron Transfer Pathways Facilitating U(VI) Reduction by Fe(II) on Al- vs Fe-Oxides

DOE Office of Scientific and Technical Information (OSTI.GOV)

Taylor, S. D.; Becker, U.; Rosso, K. M.

This study continues mechanistic development of heterogeneous electron transfer (ET) pathways at mineral surfaces in aquatic environments that enable the reduction U(VI) by surface-associated Fe(II). Using computational molecular simulation within the framework of Marcus Theory, our findings highlight the importance of the configurations and interaction of the electron donor and acceptor species with the substrate, with respect to influencing its electronic structure and thereby the ability of semiconducting minerals to facilitate ET. U(VI) reduction by surface-associated Fe(II) (adsorbed or structurally incorporated into the lattice) on an insulating, corundum (001) surface (α-Al2O3) occurs when proximal inner-sphere (IS) surface complexes are formed,more » such that ET occurs through a combination of direct exchange (i.e., Fe d- and U f-orbitals overlap through space) and superexchange via intervening surface oxygen atoms. U(VI) reduction by coadsorbed Fe(II) on the isostructural semiconducting hematite (α-Fe2O3) basal surface requires either their direct electronic interaction (e.g., IS complexation) or mediation of this interaction indirectly through the surface via an intrasurface pathway. Conceptually possible longer-range ET by charge-hopping through surface Fe atoms was investigated to determine whether this indirect pathway is competitive with direct ET. The calculations show that energy barriers are large for this conduction-based pathway; interfacial ET into the hematite surface is endothermic (+80.1 kJ/mol) and comprises the rate-limiting step (10–6 s–1). The presence of the IS adsorbates appears to weaken the electronic coupling between underlying Fe ions within the surface, resulting in slower intra-surface ET (10–5 s–1) than expected in the bulk basal plane. Our findings lay out first insights into donor-acceptor communication via a charge-hopping pathway through the surface for heterogeneous reduction of U(VI) by Fe(II) and help provide a basis for experimental interrogation of this important process at mineral-water interfaces.« less

Trapped in imidazole: how to accumulate multiple photoelectrons on a black-absorbing ruthenium complex.

PubMed

Zedler, Linda; Kupfer, Stephan; de Moraes, Inês Rabelo; Wächtler, Maria; Beckert, Rainer; Schmitt, Michael; Popp, Jürgen; Rau, Sven; Dietzek, Benjamin

2014-03-24

Ruthenium dyes incorporating a 4H-imidazole chromophore as a ligand exhibit a spectrally broad absorption in the UV/Vis region. Furthermore, they show the ability to store two electrons within the 4H-imidazole ligand. These features render them promising molecular systems, for example, as inter- or intramolecular electron relays. To optimize the structures with respect to their electron-storage capability, it is crucial to understand the impact of structural changes accompanying photoinduced charge transfer in the electronic intermediates of multistep electron-transfer processes. The photophysical properties of these (reactive) intermediates might impact the function of the molecular systems quite substantially. However, the spectroscopic study of short-lived intermediates in stepwise multielectron-transfer processes is experimentally challenging. To this end, this contribution reports on the electrochemical generation of anions identical to intermediate structures and their spectroscopic characterization by in situ resonance Raman and UV/Vis spectroelectrochemistry and computational methods. Thereby, an efficient two-electron pathway to the 4H-imidazole electron-accepting ligand is identified. © 2014 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

CO2 Reduction Catalyzed by Nitrogenase: Pathways to Formate, Carbon Monoxide, and Methane.

PubMed

Khadka, Nimesh; Dean, Dennis R; Smith, Dayle; Hoffman, Brian M; Raugei, Simone; Seefeldt, Lance C

2016-09-06

The reduction of N2 to NH3 by Mo-dependent nitrogenase at its active-site metal cluster FeMo-cofactor utilizes reductive elimination of Fe-bound hydrides with obligatory loss of H2 to activate the enzyme for binding/reduction of N2. Earlier work showed that wild-type nitrogenase and a nitrogenase with amino acid substitutions in the MoFe protein near FeMo-cofactor can catalytically reduce CO2 by two or eight electrons/protons to carbon monoxide (CO) and methane (CH4) at low rates. Here, it is demonstrated that nitrogenase preferentially reduces CO2 by two electrons/protons to formate (HCOO(-)) at rates >10 times higher than rates of CO2 reduction to CO and CH4. Quantum mechanical calculations on the doubly reduced FeMo-cofactor with a Fe-bound hydride and S-bound proton (E2(2H) state) favor a direct reaction of CO2 with the hydride ("direct hydride transfer" reaction pathway), with facile hydride transfer to CO2 yielding formate. In contrast, a significant barrier is observed for reaction of Fe-bound CO2 with the hydride ("associative" reaction pathway), which leads to CO and CH4. Remarkably, in the direct hydride transfer pathway, the Fe-H behaves as a hydridic hydrogen, whereas in the associative pathway it acts as a protic hydrogen. MoFe proteins with amino acid substitutions near FeMo-cofactor (α-70(Val→Ala), α-195(His→Gln)) are found to significantly alter the distribution of products between formate and CO/CH4.

Bacterial decolorization of textile dyes is an extracellular process requiring a multicomponent electron transfer pathway

PubMed Central

Brigé, Ann; Motte, Bart; Borloo, Jimmy; Buysschaert, Géraldine; Devreese, Bart; Van Beeumen, Jozef J.

2008-01-01

Summary Many studies have reported microorganisms as efficient biocatalysts for colour removal of dye‐containing industrial wastewaters. We present the first comprehensive study to identify all molecular components involved in decolorization by bacterial cells. Mutants from the model organism Shewanella oneidensis MR‐1, generated by random transposon and targeted insertional mutagenesis, were screened for defects in decolorization of an oxazine and diazo dye. We demonstrate that decolorization is an extracellular reduction process requiring a multicomponent electron transfer pathway that consists of cytoplasmic membrane, periplasmic and outer membrane components. The presence of melanin, a redox‐active molecule excreted by S. oneidensis, was shown to enhance the dye reduction rates. Menaquinones and the cytochrome CymA are the crucial cytoplasmic membrane components of the pathway, which then branches off via a network of periplasmic cytochromes to three outer membrane cytochromes. The key proteins of this network are MtrA and OmcB in the periplasm and outer membrane respectively. A model of the complete dye reduction pathway is proposed in which the dye molecules are reduced by the outer membrane cytochromes either directly or indirectly via melanin. PMID:21261820

Lower growth temperature increases alternative pathway capacity and alternative oxidase protein in tobacco.

PubMed

Vanlerberghe, G C; McIntosh, L

1992-09-01

Suspension cells of NT1 tobacco (Nicotiana tabacum L. cv bright yellow) have been used to study the effect of growth temperature on the CN-resistant, salicylhydroxamic acid-sensitive alternative pathway of respiration. Mitochondria isolated from cells maintained at 30 degrees C had a low capacity to oxidize succinate via the alternative pathway, whereas mitochondria isolated from cells 24 h after transfer to 18 degrees C displayed, on average, a 5-fold increase in this capacity (from 7 to 32 nanoatoms oxygen per milligram protein per minute). This represented an increase in alternative pathway capacity from 18 to 45% of the total capacity of electron transport. This increased capacity was lost upon transfer of cells back to 30 degrees C. A monoclonal antibody to the terminal oxidase of the alternative pathway (the alternative oxidase) from Sauromatum guttatum (T.E. Elthon, R.L. Nickels, L. McIntosh [1989] Plant Physiology 89: 1311-1317) recognized a 35-kilodalton mitochondrial protein in tobacco. There was an excellent correlation between the capacity of the alternative path in isolated tobacco mitochondria and the levels of this 35-kilodalton alternative oxidase protein. Cycloheximide could inhibit both the increased level of the 35-kilodalton alternative oxidase protein and the increased alternative pathway capacity normally seen upon transfer to 18 degrees C. We conclude that transfer of tobacco cells to the lower temperature increases the capacity of the alternative pathway due, at least in part, to de novo synthesis of the 35-kilodalton alternative oxidase protein.

Promotion of atomic hydrogen recombination as an alternative to electron trapping for the role of metals in the photocatalytic production of H2

PubMed Central

Joo, Ji Bong; Dillon, Robert; Lee, Ilkeun; Yin, Yadong; Bardeen, Christopher J.; Zaera, Francisco

2014-01-01

The production of hydrogen from water with semiconductor photocatalysts can be promoted by adding small amounts of metals to their surfaces. The resulting enhancement in photocatalytic activity is commonly attributed to a fast transfer of the excited electrons generated by photon absorption from the semiconductor to the metal, a step that prevents deexcitation back to the ground electronic state. Here we provide experimental evidence that suggests an alternative pathway that does not involve electron transfer to the metal but requires it to act as a catalyst for the recombination of the hydrogen atoms made via the reduction of protons on the surface of the semiconductor instead. PMID:24843154

Promotion of atomic hydrogen recombination as an alternative to electron trapping for the role of metals in the photocatalytic production of H2.

PubMed

Joo, Ji Bong; Dillon, Robert; Lee, Ilkeun; Yin, Yadong; Bardeen, Christopher J; Zaera, Francisco

2014-06-03

The production of hydrogen from water with semiconductor photocatalysts can be promoted by adding small amounts of metals to their surfaces. The resulting enhancement in photocatalytic activity is commonly attributed to a fast transfer of the excited electrons generated by photon absorption from the semiconductor to the metal, a step that prevents deexcitation back to the ground electronic state. Here we provide experimental evidence that suggests an alternative pathway that does not involve electron transfer to the metal but requires it to act as a catalyst for the recombination of the hydrogen atoms made via the reduction of protons on the surface of the semiconductor instead.

Monitoring long-range electron transfer pathways in proteins by stimulated attosecond broadband X-ray Raman spectroscopy

DOE PAGES

Zhang, Yu; Biggs, Jason D.; Govind, Niranjan; ...

2014-10-09

In this study, long-range electron transfer (ET) plays a key role in many biological energy conversion and synthesis processes. We show that nonlinear spectroscopy with attosecond X-ray pulses provides a real time movie of the evolving oxidation states and electron densities around atoms, and can probe these processes with high spatial and temporal resolution. This is demonstrated in a simulation study of the stimulated X-ray Raman (SXRS) signals in Re-modified azurin, which had long served as a benchmark for long-range ET in proteins. Nonlinear SXRS signals are sensitive to the local electronic structure and should offer a novel window formore » long-range ET.« less

An Fe-S cluster in the conserved Cys-rich region in the catalytic subunit of FAD-dependent dehydrogenase complexes.

PubMed

Shiota, Masaki; Yamazaki, Tomohiko; Yoshimatsu, Keiichi; Kojima, Katsuhiro; Tsugawa, Wakako; Ferri, Stefano; Sode, Koji

2016-12-01

Several bacterial flavin adenine dinucleotide (FAD)-harboring dehydrogenase complexes comprise three distinct subunits: a catalytic subunit with FAD, a cytochrome c subunit containing three hemes, and a small subunit. Owing to the cytochrome c subunit, these dehydrogenase complexes have the potential to transfer electrons directly to an electrode. Despite various electrochemical applications and engineering studies of FAD-dependent dehydrogenase complexes, the intra/inter-molecular electron transfer pathway has not yet been revealed. In this study, we focused on the conserved Cys-rich region in the catalytic subunits using the catalytic subunit of FAD dependent glucose dehydrogenase complex (FADGDH) as a model, and site-directed mutagenesis and electron paramagnetic resonance (EPR) were performed. By co-expressing a hitch-hiker protein (γ-subunit) and a catalytic subunit (α-subunit), FADGDH γα complexes were prepared, and the properties of the catalytic subunit of both wild type and mutant FADGDHs were investigated. Substitution of the conserved Cys residues with Ser resulted in the loss of dye-mediated glucose dehydrogenase activity. ICP-AEM and EPR analyses of the wild-type FADGDH catalytic subunit revealed the presence of a 3Fe-4S-type iron-sulfur cluster, whereas none of the Ser-substituted mutants showed the EPR spectrum characteristic for this cluster. The results suggested that three Cys residues in the Cys-rich region constitute an iron-sulfur cluster that may play an important role in the electron transfer from FAD (intra-molecular) to the multi-heme cytochrome c subunit (inter-molecular) electron transfer pathway. These features appear to be conserved in the other three-subunit dehydrogenases having an FAD cofactor. Copyright © 2016 Elsevier B.V. All rights reserved.

Theoretical investigation of the electron transfer dynamics and photodegradation pathways in a hydrogen-evolving ruthenium-palladium photocatalyst.

PubMed

Staniszewska, Magdalena; Kupfer, Stephan; Guthmuller, Julien

2018-05-16

Time-dependent density functional theory calculations combined with the Marcus theory of electron transfer (ET) were applied on the molecular photocatalyst [(tbbpy)2Ru(tpphz)PdCl2]2+ in order to elucidate the light-induced relaxation pathways populated upon excitation in the longer wavelength range of its absorption spectrum. The computational results show that after the initial excitation, metal (Ru) to ligand (tpphz) charge transfer (MLCT) triplet states are energetically accessible, but that an ET toward the catalytic center (PdCl2) from these states is a slow process, with estimated time constants above 1 ns. Instead, the calculations predict that low-lying Pd-centered states are efficiently populated - associated to an energy transfer toward the catalytic center. Thus, it is postulated that these states lead to the dissociation of a Cl- and are consequently responsible for the experimentally observed degradation of the catalytic center. Following dissociation, it is shown that the ET rates from the MLCT states to the charge separated states are significantly increased (i.e. 10^5-10^6 times larger). This demonstrates that alteration of the catalytic center generates efficient charge separation. © 2018 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

Balancing cellular redox metabolism in microbial electrosynthesis and electro fermentation - A chance for metabolic engineering.

PubMed

Kracke, Frauke; Lai, Bin; Yu, Shiqin; Krömer, Jens O

2018-01-01

More and more microbes are discovered that are capable of extracellular electron transfer, a process in which they use external electrodes as electron donors or acceptors for metabolic reactions. This feature can be used to overcome cellular redox limitations and thus optimizing microbial production. The technologies, termed microbial electrosynthesis and electro-fermentation, have the potential to open novel bio-electro production platforms from sustainable energy and carbon sources. However, the performance of reported systems is currently limited by low electron transport rates between microbes and electrodes and our limited ability for targeted engineering of these systems due to remaining knowledge gaps about the underlying fundamental processes. Metabolic engineering offers many opportunities to optimize these processes, for instance by genetic engineering of pathways for electron transfer on the one hand and target product synthesis on the other hand. With this review, we summarize the status quo of knowledge and engineering attempts around chemical production in bio-electrochemical systems from a microbe perspective. Challenges associated with the introduction or enhancement of extracellular electron transfer capabilities into production hosts versus the engineering of target compound synthesis pathways in natural exoelectrogens are discussed. Recent advances of the research community in both directions are examined critically. Further, systems biology approaches, for instance using metabolic modelling, are examined for their potential to provide insight into fundamental processes and to identify targets for metabolic engineering. Copyright © 2017 International Metabolic Engineering Society. Published by Elsevier Inc. All rights reserved.

Mapping cellular Fe-S cluster uptake and exchange reactions - divergent pathways for iron-sulfur cluster delivery to human ferredoxins.

PubMed

Fidai, Insiya; Wachnowsky, Christine; Cowan, J A

2016-12-07

Ferredoxins are protein mediators of biological electron-transfer reactions and typically contain either [2Fe-2S] or [4Fe-4S] clusters. Two ferredoxin homologues have been identified in the human genome, Fdx1 and Fdx2, that share 43% identity and 69% similarity in protein sequence and both bind [2Fe-2S] clusters. Despite the high similarity, the two ferredoxins play very specific roles in distinct physiological pathways and cannot replace each other in function. Both eukaryotic and prokaryotic ferredoxins and homologues have been reported to receive their Fe-S cluster from scaffold/delivery proteins such as IscU, Isa, glutaredoxins, and Nfu. However, the preferred and physiologically relevant pathway for receiving the [2Fe-2S] cluster by ferredoxins is subject to speculation and is not clearly identified. In this work, we report on in vitro UV-visible (UV-vis) circular dichroism studies of [2Fe-2S] cluster transfer to the ferredoxins from a variety of partners. The results reveal rapid and quantitative transfer to both ferredoxins from several donor proteins (IscU, Isa1, Grx2, and Grx3). Transfer from Isa1 to Fdx2 was also observed to be faster than that of IscU to Fdx2, suggesting that Fdx2 could receive its cluster from Isa1 instead of IscU. Several other transfer combinations were also investigated and the results suggest a complex, but kinetically detailed map for cellular cluster trafficking. This is the first step toward building a network map for all of the possible iron-sulfur cluster transfer pathways in the mitochondria and cytosol, providing insights on the most likely cellular pathways and possible redundancies in these pathways.

Bidirectional Photoinduced Electron Transfer in Ruthenium(II)-Tris-bipyridyl-Modified PpcA, a Multi-heme c -Type Cytochrome from Geobacter sulfurreducens

DOE Office of Scientific and Technical Information (OSTI.GOV)

Kokhan, Oleksandr; Ponomarenko, Nina S.; Pokkuluri, P. Raj

PpcA, a tri-heme cytochrome c7 from Geobacter sulfurreducens was investigated as a model for photosensitizer-initiated electron transfer within a multi-heme "molecular wire" protein architecture. E. coli expression of PpcA was found to be tolerant of cysteine site-directed mutagenesis, demonstrated by the successful expression of natively folded proteins bearing cysteine mutations at a series of sites selected to vary characteristically with respect to the three -CXXCH- heme binding domains. A preliminary survey of 5 selected mutants found that the introduced cysteines can be readily covalently linked to a Ru(II)-(2,2'-bpy)2(4-bromomethyl-4’-methyl-2,2'-bpy) photosensitizer (where bpy = bipyridine), and that the linked constructs support bothmore » photo-oxidative and photo-reductive quenching of the photosensitizer excited-state, depending upon the initial heme redox state. For photo-oxidative electron transfer, apparent heme reduction risetimes were found to vary from 7 x 10-12 s to 5 x 10-8 s, depending upon the site of photosensitizer linking. The excited-state electron transfers are about 103-fold faster than any previously reported photosensitizer-redox protein covalently linked construct. Preliminary conformational analysis using molecular dynamics simulations shows that rates for electron transfer track both the distance and pathways for electron transfer. Two mutants with the fastest charge transfer rates, A23C and K29C, showed a significant role of specific paths for electron transfer. While K29C labeled mutant was expected to have approximately 0.8Å greater donor-acceptor distance, it showed 20-fold faster charge separation rate. Clear evidence for inter-heme electron transfer within the multi-heme protein is not detected within the lifetimes of the charge separated states. These results demonstrate an opportunity to develop multi-heme c-cytochromes for investigation of electron transfer in protein "molecular wires" and to serve as frameworks for metalloprotein designs that support multiple electron transfer redox chemistry.« less

First principles studies of electron tunneling in proteins

PubMed Central

Hayashi, Tomoyuki; Stuchebrukhov, Alexei A.

2014-01-01

A first principles study of electronic tunneling along the chain of seven Fe/S clusters in respiratory complex I, a key enzyme in the respiratory electron transport chain, is described. The broken-symmetry states of the Fe/S metal clusters calculated at both DFT and semi-empirical ZINDO levels were utilized to examine both the extremely weak electronic couplings between Fe/S clusters and the tunneling pathways, which provide a detailed atomistic-level description of the charge transfer process in the protein. One-electron tunneling approximation was found to hold within a reasonable accuracy, with only a moderate induced polarization of the core electrons. The method is demonstrated to be able to calculate accurately the coupling matrix elements as small as 10−4 cm−1. A distinct signature of the wave properties of electrons is observed as quantum interferences of multiple tunneling pathways. PMID:25383312

Transfer of the cytochrome P450-dependent dhurrin pathway from Sorghum bicolor into Nicotiana tabacum chloroplasts for light-driven synthesis

PubMed Central

Gnanasekaran, Thiyagarajan; Karcher, Daniel; Nielsen, Agnieszka Zygadlo; Martens, Helle Juel; Ruf, Stephanie; Kroop, Xenia; Olsen, Carl Erik; Motawie, Mohammed Saddik; Pribil, Mathias; Møller, Birger Lindberg; Bock, Ralph; Jensen, Poul Erik

2016-01-01

Plant chloroplasts are light-driven cell factories that have great potential to act as a chassis for metabolic engineering applications. Using plant chloroplasts, we demonstrate how photosynthetic reducing power can drive a metabolic pathway to synthesise a bio-active natural product. For this purpose, we stably engineered the dhurrin pathway from Sorghum bicolor into the chloroplasts of Nicotiana tabacum (tobacco). Dhurrin is a cyanogenic glucoside and its synthesis from the amino acid tyrosine is catalysed by two membrane-bound cytochrome P450 enzymes (CYP79A1 and CYP71E1) and a soluble glucosyltransferase (UGT85B1), and is dependent on electron transfer from a P450 oxidoreductase. The entire pathway was introduced into the chloroplast by integrating CYP79A1, CYP71E1, and UGT85B1 into a neutral site of the N. tabacum chloroplast genome. The two P450s and the UGT85B1 were functional when expressed in the chloroplasts and converted endogenous tyrosine into dhurrin using electrons derived directly from the photosynthetic electron transport chain, without the need for the presence of an NADPH-dependent P450 oxidoreductase. The dhurrin produced in the engineered plants amounted to 0.1–0.2% of leaf dry weight compared to 6% in sorghum. The results obtained pave the way for plant P450s involved in the synthesis of economically important compounds to be engineered into the thylakoid membrane of chloroplasts, and demonstrate that their full catalytic cycle can be driven directly by photosynthesis-derived electrons. PMID:26969746

Probing and Exploiting the Interplay between Nuclear and Electronic Motion in Charge Transfer Processes.

PubMed

Delor, Milan; Sazanovich, Igor V; Towrie, Michael; Weinstein, Julia A

2015-04-21

The Born-Oppenheimer approximation refers to the assumption that the nuclear and electronic wave functions describing a molecular system evolve and can be determined independently. It is now well-known that this approximation often breaks down and that nuclear-electronic (vibronic) coupling contributes greatly to the ultrafast photophysics and photochemistry observed in many systems ranging from simple molecules to biological organisms. In order to probe vibronic coupling in a time-dependent manner, one must use spectroscopic tools capable of correlating the motions of electrons and nuclei on an ultrafast time scale. Recent developments in nonlinear multidimensional electronic and vibrational spectroscopies allow monitoring both electronic and structural factors with unprecedented time and spatial resolution. In this Account, we present recent studies from our group that make use of different variants of frequency-domain transient two-dimensional infrared (T-2DIR) spectroscopy, a pulse sequence combining electronic and vibrational excitations in the form of a UV-visible pump, a narrowband (12 cm(-1)) IR pump, and a broadband (400 cm(-1)) IR probe. In the first example, T-2DIR is used to directly compare vibrational dynamics in the ground and relaxed electronic excited states of Re(Cl)(CO)3(4,4'-diethylester-2,2'-bipyridine) and Ru(4,4'-diethylester-2,2'-bipyridine)2(NCS)2, prototypical charge transfer complexes used in photocatalytic CO2 reduction and electron injection in dye-sensitized solar cells. The experiments show that intramolecular vibrational redistribution (IVR) and vibrational energy transfer (VET) are up to an order of magnitude faster in the triplet charge transfer excited state than in the ground state. These results show the influence of electronic arrangement on vibrational coupling patterns, with direct implications for vibronic coupling mechanisms in charge transfer excited states. In the second example, we show unambiguously that electronic and vibrational movement are coupled in a donor-bridge-acceptor complex based on a Pt(II) trans-acetylide design motif. Time-resolved IR (TRIR) spectroscopy reveals that the rate of electron transfer (ET) is highly dependent on the amount of excess energy localized on the bridge following electronic excitation. Using an adaptation of T-2DIR, we are able to selectively perturb bridge-localized vibrational modes during charge separation, resulting in the donor-acceptor charge separation pathway being completely switched off, with all excess energy redirected toward the formation of a long-lived intraligand triplet state. A series of control experiments reveal that this effect is mode specific: it is only when the high-frequency bridging C≡C stretching mode is pumped that radical changes in photoproduct yields are observed. These experiments therefore suggest that one may perturb electronic movement by stimulating structural motion along the reaction coordinate using IR light. These studies add to a growing body of evidence suggesting that controlling the pathways and efficiency of charge transfer may be achieved through synthetic and perturbative approaches aiming to modulate vibronic coupling. Achieving such control would represent a breakthrough for charge transfer-based applications such as solar energy conversion and molecular electronics.

Timing of electron and proton transfer in the ba(3) cytochrome c oxidase from Thermus thermophilus.

PubMed

von Ballmoos, Christoph; Lachmann, Peter; Gennis, Robert B; Ädelroth, Pia; Brzezinski, Peter

2012-06-05

Heme-copper oxidases are membrane-bound proteins that catalyze the reduction of O(2) to H(2)O, a highly exergonic reaction. Part of the free energy of this reaction is used for pumping of protons across the membrane. The ba(3) oxidase from Thermus thermophilus presumably uses a single proton pathway for the transfer of substrate protons used during O(2) reduction as well as for the transfer of the protons that are pumped across the membrane. The pumping stoichiometry (0.5 H(+)/electron) is lower than that of most other (mitochondrial-like) oxidases characterized to date (1 H(+)/electron). We studied the pH dependence and deuterium isotope effect of the kinetics of electron and proton transfer reactions in the ba(3) oxidase. The results from these studies suggest that the movement of protons to the catalytic site and movement to a site located some distance from the catalytic site [proposed to be a "proton-loading site" (PLS) for pumped protons] are separated in time, which allows individual investigation of these reactions. A scenario in which the uptake and release of a pumped proton occurs upon every second transfer of an electron to the catalytic site would explain the decreased proton pumping stoichiometry compared to that of mitochondrial-like oxidases.

Photocurrent generation by direct electron transfer using photosynthetic reaction centres

NASA Astrophysics Data System (ADS)

Mahmoudzadeh, A.; Saer, R.; Jun, D.; Mirvakili, S. M.; Takshi, A.; Iranpour, B.; Ouellet, E.; Lagally, E. T.; Madden, J. D. W.; Beatty, J. T.

2011-09-01

Photosynthetic reaction centres (RCs) convert light into separated charges with nearly perfect quantum efficiency, and have been used to generate photocurrent. Previous work has shown that electron tunnelling rates between redox centres in proteins depend exponentially on the tunnelling distance. In this work the RC from Rhodobacter sphaeroides was genetically modified with the aim of achieving the shortest tunnelling distances yet demonstrated between the RC's electron-accepting P site and underlying graphite and gold electrodes, and between the electron donor Q site and graphite electrodes. Opposite charges are carried to counter electrodes using mobile mediators, as in dye-sensitised solar cells. Native RCs are bound to graphite surfaces through N-(1-pyrene)iodoacetamide. Although the linker's length is only 4 Å, the electron transfer pathway between the Q electron donor site on the RC and the electrode surface is still too large for current to be significant. A mutant version with the electron acceptor P side close to the graphite surface produced currents of 15 nA cm-2 upon illumination. Direct binding of RCs to a gold surface is shown, resulting in currents of 5 nA cm-2. In both cases the current was unaffected by mediator concentration but increased with illumination, suggesting that direct electron transfer was achieved. The engineering of an RC to achieve direct electron transfer will help with long term efforts to demonstrate RC-based photovoltaic devices.

Multichannel modeling and two-photon coherent transfer paths in NaK

NASA Astrophysics Data System (ADS)

Schulze, T. A.; Temelkov, I. I.; Gempel, M. W.; Hartmann, T.; Knöckel, H.; Ospelkaus, S.; Tiemann, E.

2013-08-01

We explore possible pathways for the creation of ultracold polar NaK molecules in their absolute electronic and rovibrational ground state starting from ultracold Feshbach molecules. In particular, we present a multichannel analysis of the electronic ground and K(4p)+Na(3s) excited-state manifold of NaK, analyze the spin character of both the Feshbach molecular state and the electronically excited intermediate states and discuss possible coherent two-photon transfer paths from Feshbach molecules to rovibronic ground-state molecules. The theoretical study is complemented by the demonstration of stimulated Raman adiabatic passage from the X1Σ+(v=0) state to the a3Σ+ manifold on a molecular beam experiment.

DFT Study on Nitrite Reduction Mechanism in Copper-Containing Nitrite Reductase.

PubMed

Lintuluoto, Masami; Lintuluoto, Juha M

2016-01-12

Dissimilatory reduction of nitrite by copper-containing nitrite reductase (CuNiR) is an important step in the geobiochemical nitrogen cycle. The proposed mechanisms for the reduction of nitrite by CuNiRs include intramolecular electron and proton transfers, and these two events are understood to couple. Proton-coupled electron transfer is one of the key processes in enzyme reactions. We investigated the geometric structure of bound nitrite and the mechanism of nitrite reduction on CuNiR using density functional theory calculations. Also, the proton transfer pathway, the key residues, and their roles in the reaction mechanism were clarified in this study. In our results, the reduction of T2 Cu site promotes the proton transfer, and the hydrogen bond network around the binding site has an important role not only to stabilize the nitrite binding but also to promote the proton transfer to nitrite.

Study of Proton Transfer in E. Coli Photolyase

NASA Astrophysics Data System (ADS)

Zhang, Meng; Liu, Zheyun; Li, Jiang; Wang, Lijuan; Zhong, Dongping

2013-06-01

Photolyase is a flavoprotein which utilizes blue-light energy to repair UV-light damaged DNA. The catalytic cofactor of photolyase, flavin adenine dinucleotide (FAD), has five redox states. Conversions between these redox states involve intraprotein electron transfer and proton transfer, which play important role in protein function. Here we systematically studied proton transfer in E. coli photolyase in vitro by site-directed mutagenesis and steady-state UV-vis spectroscopy, and proposed the proton channel in photolyase. We found that in the mutant N378C/E363L, proton channel was completely eliminated when DNA substrate was bound to the protein. Proton is suggested to be transported from protein surface to FAD by two pathways: the proton relay pathway through E363 and surface water to N378 and then to FAD; and the proton diffusion pathway through the substrate binding pocket. In addition, reaction kinetics of conversions between the redox states was then solved and redox potentials of the redox states were determined. These results described a complete picture of FAD redox changes, which are fundamental to the functions of all flavoenzymes.

Chloroplast biogenesis 89: development of analytical tools for probing the biosynthetic topography of photosynthetic membranes by determination of resonance excitation energy transfer distances separating metabolic tetrapyrrole donors from chlorophyll a acceptors.

PubMed

Kopetz, Karen J; Kolossov, Vladimir L; Rebeiz, Constantin A

2004-06-15

The thorough understanding of photosynthetic membrane assembly requires a deeper knowledge of the coordination and regulation of the chlorophyll (Chl) and thylakoid apoprotein biosynthetic pathways. As a working hypothesis we have recently proposed three different Chl-thylakoid apoprotein biosynthesis models: a single-branched Chl biosynthetic pathway (SBP)-single location model, a SBP-multilocation model, and a multibranched Chl biosynthetic pathway (MBP)-sublocation model. The detection of resonance excitation energy transfer between tetrapyrrole precursors of Chl, and several Chl-protein complexes, has made it possible to test the validity of the proposed Chl-thylakoid apoprotein biosynthesis models by resonance excitation energy transfer determinations. In this work, resonance excitation energy transfer techniques that allow the determination of distances separating tetrapyrrole donors from Chl-protein acceptors in green plants by using readily available electronic spectroscopic instrumentation are developed. It is concluded that the calculated distances are compatible with the MBP-sublocation model and incompatible with the operation of the SBP-single location Chl-protein biosynthesis model.

Proton-coupled electron transfer and the role of water molecules in proton pumping by cytochrome c oxidase

PubMed Central

Sharma, Vivek; Enkavi, Giray; Vattulainen, Ilpo; Róg, Tomasz; Wikström, Mårten

2015-01-01

Molecular oxygen acts as the terminal electron sink in the respiratory chains of aerobic organisms. Cytochrome c oxidase in the inner membrane of mitochondria and the plasma membrane of bacteria catalyzes the reduction of oxygen to water, and couples the free energy of the reaction to proton pumping across the membrane. The proton-pumping activity contributes to the proton electrochemical gradient, which drives the synthesis of ATP. Based on kinetic experiments on the O–O bond splitting transition of the catalytic cycle (A → PR), it has been proposed that the electron transfer to the binuclear iron–copper center of O2 reduction initiates the proton pump mechanism. This key electron transfer event is coupled to an internal proton transfer from a conserved glutamic acid to the proton-loading site of the pump. However, the proton may instead be transferred to the binuclear center to complete the oxygen reduction chemistry, which would constitute a short-circuit. Based on atomistic molecular dynamics simulations of cytochrome c oxidase in an explicit membrane–solvent environment, complemented by related free-energy calculations, we propose that this short-circuit is effectively prevented by a redox-state–dependent organization of water molecules within the protein structure that gates the proton transfer pathway. PMID:25646428

DOE Office of Scientific and Technical Information (OSTI.GOV)

Alfonso Hernandez, Laura; Nelson, Tammie Renee; Gelin, Maxim F.

The interchromophoric energy-transfer pathways between weakly coupled units in a π-conjugated phenylene–ethynylene macrocycle and its half-ring analogue have been investigated using the nonadiabatic excited-state molecular dynamics approach. To track the flow of electronic transition density between macrocycle units, we formulate a transition density flux analysis adapted from the statistical minimum flow method previously developed to investigate vibrational energy flow. Following photoexcitation, transition density is primarily delocalized on two chromophore units and the system undergoes ultrafast energy transfer, creating a localized excited state on a single unit. In the macrocycle, distinct chromophore units donate transition density to a single acceptor unitmore » but do not interchange transition density among each other. We find that energy transfer in the macrocycle is slower than in the corresponding half ring because of the presence of multiple interfering energy-transfer pathways. Finally, simulation results are validated by modeling the fluorescence anisotropy decay.« less

Delayed Triplet-State Formation through Hybrid Charge Transfer Exciton at Copper Phthalocyanine/GaAs Heterojunction.

PubMed

Lim, Heeseon; Kwon, Hyuksang; Kim, Sang Kyu; Kim, Jeong Won

2017-10-05

Light absorption in organic molecules on an inorganic substrate and subsequent electron transfer to the substrate create so-called hybrid charge transfer exciton (HCTE). The relaxation process of the HCTE states largely determines charge separation efficiency or optoelectronic device performance. Here, the study on energy and time-dispersive behavior of photoelectrons at the hybrid interface of copper phthalocyanine (CuPc)/p-GaAs(001) upon light excitation of GaAs reveals a clear pathway for HCTE relaxation and delayed triplet-state formation. According to the ground-state energy level alignment at the interface, CuPc/p-GaAs(001) shows initially fast hole injection from GaAs to CuPc. Thus, the electrons in GaAs and holes in CuPc form an unusual HCTE state manifold. Subsequent electron transfer from GaAs to CuPc generates the formation of the triplet state in CuPc with a few picoseconds delay. Such two-step charge transfer causes delayed triplet-state formation without singlet excitation and subsequent intersystem crossing within the CuPc molecules.

Coenzyme Q biosynthesis and its role in the respiratory chain structure.

PubMed

Alcázar-Fabra, María; Navas, Plácido; Brea-Calvo, Gloria

2016-08-01

Coenzyme Q (CoQ) is a unique electron carrier in the mitochondrial respiratory chain, which is synthesized on-site by a nuclear encoded multiprotein complex. CoQ receives electrons from different redox pathways, mainly NADH and FADH2 from tricarboxylic acid pathway, dihydroorotate dehydrogenase, electron transfer flavoprotein dehydrogenase and glycerol-3-phosphate dehydrogenase that support key aspects of the metabolism. Here we explore some lines of evidence supporting the idea of the interaction of CoQ with the respiratory chain complexes, contributing to their superassembly, including respirasome, and its role in reactive oxygen species production in the mitochondrial inner membrane. We also review the current knowledge about the involvement of mitochondrial genome defects and electron transfer flavoprotein dehydrogenase mutations in the induction of secondary CoQ deficiency. This mechanism would imply specific interactions coupling CoQ itself or the CoQ-biosynthetic apparatus with the respiratory chain components. These interactions would regulate mitochondrial CoQ steady-state levels and function. This article is part of a Special Issue entitled 'EBEC 2016: 19th European Bioenergetics Conference, Riva del Garda, Italy, July 2-6, 2016', edited by Prof. Paolo Bernardi. Copyright © 2016 Elsevier B.V. All rights reserved.

Characterization of the periplasmic redox network that sustains the versatile anaerobic metabolism of Shewanella oneidensis MR-1

PubMed Central

Alves, Mónica N.; Neto, Sónia E.; Alves, Alexandra S.; Fonseca, Bruno M.; Carrêlo, Afonso; Pacheco, Isabel; Paquete, Catarina M.; Soares, Cláudio M.; Louro, Ricardo O.

2015-01-01

The versatile anaerobic metabolism of the Gram-negative bacterium Shewanella oneidensis MR-1 (SOMR-1) relies on a multitude of redox proteins found in its periplasm. Most are multiheme cytochromes that carry electrons to terminal reductases of insoluble electron acceptors located at the cell surface, or bona fide terminal reductases of soluble electron acceptors. In this study, the interaction network of several multiheme cytochromes was explored by a combination of NMR spectroscopy, activity assays followed by UV-visible spectroscopy and comparison of surface electrostatic potentials. From these data the small tetraheme cytochrome (STC) emerges as the main periplasmic redox shuttle in SOMR-1. It accepts electrons from CymA and distributes them to a number of terminal oxidoreductases involved in the respiration of various compounds. STC is also involved in the electron transfer pathway to reduce nitrite by interaction with the octaheme tetrathionate reductase (OTR), but not with cytochrome c nitrite reductase (ccNiR). In the main pathway leading the metal respiration STC pairs with flavocytochrome c (FccA), the other major periplasmic cytochrome, which provides redundancy in this important pathway. The data reveals that the two proteins compete for the binding site at the surface of MtrA, the decaheme cytochrome inserted on the periplasmic side of the MtrCAB–OmcA outer-membrane complex. However, this is not observed for the MtrA homologues. Indeed, neither STC nor FccA interact with MtrD, the best replacement for MtrA, and only STC is able to interact with the decaheme cytochrome DmsE of the outer-membrane complex DmsEFABGH. Overall, these results shown that STC plays a central role in the anaerobic respiratory metabolism of SOMR-1. Nonetheless, the trans-periplasmic electron transfer chain is functionally resilient as a consequence of redundancies that arise from the presence of alternative pathways that bypass/compete with STC. PMID:26175726

Conversion and origin of normal and abnormal temperature dependences of kinetic isotope effect in hydride transfer reactions.

PubMed

Zhu, Xiao-Qing; Li, Xiu-Tao; Han, Su-Hui; Mei, Lian-Rui

2012-05-18

The effects of substituents on the temperature dependences of kinetic isotope effect (KIE) for the reactions of the hydride transfer from the substituted 5-methyl-6-phenyl-5,6-dihydrophenanthridine (G-PDH) to thioxanthylium (TX(+)) in acetonitrile were examined, and the results show that the temperature dependences of KIE for the hydride transfer reactions can be converted by adjusting the nature of the substituents in the molecule of the hydride donor. In general, electron-withdrawing groups can make the KIE to have normal temperature dependence, but electron-donating groups can make the KIE to have abnormal temperature dependence. Thermodynamic analysis on the possible pathways of the hydride transfer from G-PDH to TX(+) in acetonitrile suggests that the transfers of the hydride anion in the reactions are all carried out by the concerted one-step mechanism whether the substituent is an electron-withdrawing group or an electron-donating group. But the examination of Hammett-type free energy analysis on the hydride transfer reactions supports that the concerted one-step hydride transfer is not due to an elementary chemical reaction. The experimental values of KIE at different temperatures for the hydride transfer reactions were modeled by using a kinetic equation formed according to a multistage mechanism of the hydride transfer including a returnable charge-transfer complex as the reaction intermediate; the real mechanism of the hydride transfer and the root that why the temperature dependences of KIE can be converted as the nature of the substituents are changed were discovered.

Lower Growth Temperature Increases Alternative Pathway Capacity and Alternative Oxidase Protein in Tobacco 1

PubMed Central

Vanlerberghe, Greg C.; McIntosh, Lee

1992-01-01

Suspension cells of NT1 tobacco (Nicotiana tabacum L. cv bright yellow) have been used to study the effect of growth temperature on the CN-resistant, salicylhydroxamic acid-sensitive alternative pathway of respiration. Mitochondria isolated from cells maintained at 30°C had a low capacity to oxidize succinate via the alternative pathway, whereas mitochondria isolated from cells 24 h after transfer to 18°C displayed, on average, a 5-fold increase in this capacity (from 7 to 32 nanoatoms oxygen per milligram protein per minute). This represented an increase in alternative pathway capacity from 18 to 45% of the total capacity of electron transport. This increased capacity was lost upon transfer of cells back to 30°C. A monoclonal antibody to the terminal oxidase of the alternative pathway (the alternative oxidase) from Sauromatum guttatum (T.E. Elthon, R.L. Nickels, L. McIntosh [1989] Plant Physiology 89: 1311-1317) recognized a 35-kilodalton mitochondrial protein in tobacco. There was an excellent correlation between the capacity of the alternative path in isolated tobacco mitochondria and the levels of this 35-kilodalton alternative oxidase protein. Cycloheximide could inhibit both the increased level of the 35-kilodalton alternative oxidase protein and the increased alternative pathway capacity normally seen upon transfer to 18°C. We conclude that transfer of tobacco cells to the lower temperature increases the capacity of the alternative pathway due, at least in part, to de novo synthesis of the 35-kilodalton alternative oxidase protein. Images Figure 3 Figure 4 PMID:16652932

Optical properties, excitation energy and primary charge transfer in photosystem II: theory meets experiment.

PubMed

Renger, Thomas; Schlodder, Eberhard

2011-01-01

In this review we discuss structure-function relationships of the core complex of photosystem II, as uncovered from analysis of optical spectra of the complex and its subunits. Based on descriptions of optical difference spectra including site directed mutagenesis we propose a revision of the multimer model of the symmetrically arranged reaction center pigments, described by an asymmetric exciton Hamiltonian. Evidence is provided for the location of the triplet state, the identity of the primary electron donor, the localization of the cation and the secondary electron transfer pathway in the reaction center. We also discuss the stationary and time-dependent optical properties of the CP43 and CP47 subunits and the excitation energy transfer and trapping-by-charge-transfer kinetics in the core complex. Copyright © 2011 Elsevier B.V. All rights reserved.

Model-based Confirmation of Alternative Substrates of Mitochondrial Electron Transport Chain

PubMed Central

Kleessen, Sabrina; Araújo, Wagner L.; Fernie, Alisdair R.; Nikoloski, Zoran

2012-01-01

Discrimination of metabolic models based on high throughput metabolomics data, reflecting various internal and external perturbations, is essential for identifying the components that contribute to the emerging behavior of metabolic processes. Here, we investigate 12 different models of the mitochondrial electron transport chain (ETC) in Arabidopsis thaliana during dark-induced senescence in order to elucidate the alternative substrates to this metabolic pathway. Our findings demonstrate that the coupling of the proposed computational approach, based on dynamic flux balance analysis, with time-resolved metabolomics data results in model-based confirmations of the hypotheses that, during dark-induced senescence in Arabidopsis, (i) under conditions where the main substrate for the ETC are not fully available, isovaleryl-CoA dehydrogenase and 2-hydroxyglutarate dehydrogenase are able to donate electrons to the ETC, (ii) phytanoyl-CoA does not act even as an indirect substrate of the electron transfer flavoprotein/electron-transfer flavoprotein:ubiquinone oxidoreductase complex, and (iii) the mitochondrial γ-aminobutyric acid transporter has functional significance in maintaining mitochondrial metabolism. Our study provides a basic framework for future in silico studies of alternative pathways in mitochondrial metabolism under extended darkness whereby the role of its components can be computationally discriminated based on available molecular profile data. PMID:22334689

Molecular Basis for Electron Flow Within Metal-and Electrode-Reducing Biofilms

DOE Office of Scientific and Technical Information (OSTI.GOV)

Bond, Daniel R.

2016-11-01

Electrochemical, spectral, genetic, and biochemical techniques were developed to reveal that a diverse suite of redox proteins and structural macromolecules outside the cell work together to move electrons long distances between Geobacter cells to metals and electrodes. In this project, we greatly expanded the known participants in the electron transfer pathway of Geobacter. For example, in addition to well-studied pili, polysaccharides contribute to anchoring, different cytochromes are required under different conditions, strategies change with redox potential, and the localization of these components can change depending on where cells are located in a biofilm. By inventing new electrodes compatible with real-timemore » spectral measurements, we were able to visualize the redox status of biofilms in action, leading to a hypothesis that long-distance electron transfer is ultimately limiting in these systems and redox potentials change within biofilms. The goals of this project were met, as we were able to 1) identify new elements crucial to the expression, assembly and function of the extracellular electron transfer phenotype 2) expand spectral and electrochemical techniques to define the mechanism and route of electron transfer through the matrix, and 3) combine this knowledge to build the next generation of genetic tools for study of this complex process.« less

DOE Office of Scientific and Technical Information (OSTI.GOV)

Wu, Wenting; Zhang, Qinggang; Wang, Ruiqin

Unsaturated metal species (UMS) confined in nanomaterials play important roles for electron transfer in a wide range of catalytic reactions. However, the limited fabrication methods of UMS restrict their wider catalytic applications. Here in this paper, we report on the synergy of unsaturated Zn and Cu dopants confined in carbon dots (ZnCu-CDs) to produce enhanced electron transfer and photooxidation processes in the doped CDs. The Zn/Cu species chelate with the carbon matrix mainly through Cu-O(N)-Zn-O(N)-Cu complexes. Within this structure, Cu 2+ acts as a mild oxidizer that facilely increases the unsaturated Zn content and also precisely tunes the unsaturated Znmore » valence state to Zn d+, where d is between 1 and 2, instead of Zn. With the help of UMS, electron-transfer pathways are produced, enhancing both the electron donating (7.0 times) and-accepting (5.3 times) abilities relative to conventional CDs. Because of these synergistic effects, the photocatalytic efficiency of CDs in photooxidation reactions is shown to improve more than 5-fold.« less

A bioinspired redox relay that mimics radical interactions of the Tyr-His pairs of photosystem II

NASA Astrophysics Data System (ADS)

Megiatto, Jackson D., Jr.; Méndez-Hernández, Dalvin D.; Tejeda-Ferrari, Marely E.; Teillout, Anne-Lucie; Llansola-Portolés, Manuel J.; Kodis, Gerdenis; Poluektov, Oleg G.; Rajh, Tijana; Mujica, Vladimiro; Groy, Thomas L.; Gust, Devens; Moore, Thomas A.; Moore, Ana L.

2014-05-01

In water-oxidizing photosynthetic organisms, light absorption generates a powerfully oxidizing chlorophyll complex (P680•+) in the photosystem II reaction centre. This is reduced via an electron transfer pathway from the manganese-containing water-oxidizing catalyst, which includes an electron transfer relay comprising a tyrosine (Tyr)-histidine (His) pair that features a hydrogen bond between a phenol group and an imidazole group. By rapidly reducing P680•+, the relay is thought to mitigate recombination reactions, thereby ensuring a high quantum yield of water oxidation. Here, we show that an artificial reaction centre that features a benzimidazole-phenol model of the Tyr-His pair mimics both the short-internal hydrogen bond in photosystem II and, using electron paramagnetic resonance spectroscopy, the thermal relaxation that accompanies proton-coupled electron transfer. Although this artificial system is much less complex than the natural one, theory suggests that it captures the essential features that are important in the function of the relay.

A review on the bioenergetics of anaerobic microbial metabolism close to the thermodynamic limits and its implications for digestion applications.

PubMed

Leng, Ling; Yang, Peixian; Singh, Shubham; Zhuang, Huichuan; Xu, Linji; Chen, Wen-Hsing; Dolfing, Jan; Li, Dong; Zhang, Yan; Zeng, Huiping; Chu, Wei; Lee, Po-Heng

2018-01-01

The exploration of the energetics of anaerobic digestion systems can reveal how microorganisms cooperate efficiently for cell growth and methane production, especially under low-substrate conditions. The establishment of a thermodynamically interdependent partnership, called anaerobic syntrophy, allows unfavorable reactions to proceed. Interspecies electron transfer and the concentrations of electron carriers are crucial for maintaining this mutualistic activity. This critical review summarizes the functional microorganisms and syntroph partners, particularly in the metabolic pathways and energy conservation of syntrophs. The kinetics and thermodynamics of propionate degradation to methane, reversibility of the acetate oxidation process, and estimation of microbial growth are summarized. The various routes of interspecies electron transfer, reverse electron transfer, and Poly-β-hydroxyalkanoate formation in the syntrophic community are also reviewed. Finally, promising and critical directions of future research are proposed. Fundamental insight in the activities and interactions involved in AD systems could serve as a guidance for engineered systems optimization and upgrade. Copyright © 2017 Elsevier Ltd. All rights reserved.

Redox potential as a master variable controlling pathways of metal reduction by Geobacter sulfurreducens

PubMed Central

Levar, Caleb E; Hoffman, Colleen L; Dunshee, Aubrey J; Toner, Brandy M; Bond, Daniel R

2017-01-01

Geobacter sulfurreducens uses at least two different pathways to transport electrons out of the inner membrane quinone pool before reducing acceptors beyond the outer membrane. When growing on electrodes poised at oxidizing potentials, the CbcL-dependent pathway operates at or below redox potentials of –0.10 V vs the standard hydrogen electrode, whereas the ImcH-dependent pathway operates only above this value. Here, we provide evidence that G. sulfurreducens also requires different electron transfer proteins for reduction of a wide range of Fe(III)- and Mn(IV)-(oxyhydr)oxides, and must transition from a high- to low-potential pathway during reduction of commonly studied soluble and insoluble metal electron acceptors. Freshly precipitated Fe(III)-(oxyhydr)oxides could not be reduced by mutants lacking the high-potential pathway. Aging these minerals by autoclaving did not change their powder X-ray diffraction pattern, but restored reduction by mutants lacking the high-potential pathway. Mutants lacking the low-potential, CbcL-dependent pathway had higher growth yields with both soluble and insoluble Fe(III). Together, these data suggest that the ImcH-dependent pathway exists to harvest additional energy when conditions permit, and CbcL switches on to allow respiration closer to thermodynamic equilibrium conditions. With evidence of multiple pathways within a single organism, the study of extracellular respiration should consider not only the crystal structure or solubility of a mineral electron acceptor, but rather the redox potential, as this variable determines the energetic reward affecting reduction rates, extents, and final microbial growth yields in the environment. PMID:28045456

Electron transfer to nitrogenase in different genomic and metabolic backgrounds.

PubMed

Poudel, Saroj; Colman, Daniel R; Fixen, Kathryn R; Ledbetter, Rhesa N; Zheng, Yanning; Pence, Natasha; Seefeldt, Lance C; Peters, John W; Harwood, Caroline S; Boyd, Eric S

2018-02-26

Nitrogenase catalyzes the reduction of dinitrogen (N 2 ) using low potential electrons from ferredoxin (Fd) or flavodoxin (Fld) through an ATP dependent process. Since its emergence in an anaerobic chemoautotroph, this oxygen (O 2 ) sensitive enzyme complex has evolved to operate in a variety of genomic and metabolic backgrounds including those of aerobes, anaerobes, chemotrophs, and phototrophs. However, whether pathways of electron delivery to nitrogenase are influenced by these different metabolic backgrounds is not well understood. Here, we report the distribution of homologs of Fds, Flds, and Fd/Fld-reducing enzymes in 359 genomes of putative N 2 fixers (diazotrophs). Six distinct lineages of nitrogenase were identified and their distributions largely corresponded to differences in the host cells' ability to integrate O 2 or light into energy metabolism. Predicted pathways of electron transfer to nitrogenase in aerobes, facultative anaerobes, and phototrophs varied from those in anaerobes at the level of Fds/Flds used to reduce nitrogenase, the enzymes that generate reduced Fds/Flds, and the putative substrates of these enzymes. Proteins that putatively reduce Fd with hydrogen or pyruvate were enriched in anaerobes, while those that reduce Fd with NADH/NADPH were enriched in aerobes, facultative anaerobes, and anoxygenic phototrophs. The energy metabolism of aerobic, facultatively anaerobic, and anoxygenic phototrophic diazotrophs often yields reduced NADH/NADPH that is not sufficiently reduced to drive N 2 reduction. At least two mechanisms have been acquired by these taxa to overcome this limitation and to generate electrons with potentials capable of reducing Fd. These include the bifurcation of electrons or the coupling of Fd reduction to reverse ion translocation. IMPORTANCE Nitrogen fixation supplies fixed nitrogen to cells from a variety of genomic and metabolic backgrounds including those of aerobes, facultative anaerobes, chemotrophs, and phototrophs. Here, using informatics approaches applied to genomic data, we show that pathways of electron transfer to nitrogenase in metabolically diverse diazotrophic taxa have diversified primarily in response to host cells' acquired ability to integrate O 2 or light into their energy metabolism. Acquisition of two key enzyme complexes enabled aerobic and facultatively anaerobic phototrophic taxa to generate electrons of sufficiently low potential to reduce nitrogenase: the bifurcation of electrons via the Fix complex or the coupling of Fd reduction to reverse ion translocation via the Rhodobacter nitrogen fixation (Rnf) complex. Copyright © 2018 American Society for Microbiology.

DOE Office of Scientific and Technical Information (OSTI.GOV)

Ledbetter, Rhesa N.; Garcia Costas, Amaya M.; Lubner, Carolyn E.

The biological reduction of dinitrogen (N 2) to ammonia (NH 3) by nitrogenase is an energetically demanding reaction that requires low-potential electrons and ATP; however, pathways used to deliver the electrons from central metabolism to the reductants of nitrogenase, ferredoxin or flavodoxin, remain unknown for many diazotrophic microbes. The FixABCX protein complex has been proposed to reduce flavodoxin or ferredoxin using NADH as the electron donor in a process known as electron bifurcation. Herein, the FixABCX complex from Azotobacter vinelandii was purified and demonstrated to catalyze an electron bifurcation reaction: oxidation of NADH (E m = -320 mV) coupled tomore » reduction of flavodoxin semiquinone (E m = -460 mV) and reduction of coenzyme Q (E m = 10 mV). Knocking out fix genes rendered ..delta..rnf A. vinelandii cells unable to fix dinitrogen, confirming that the FixABCX system provides another route for delivery of electrons to nitrogenase. Characterization of the purified FixABCX complex revealed the presence of flavin and iron-sulfur cofactors confirmed by native mass spectrometry, electron paramagnetic resonance spectroscopy, and transient absorption spectroscopy. Transient absorption spectroscopy further established the presence of a short-lived flavin semiquinone radical, suggesting that a thermodynamically unstable flavin semiquinone may participate as an intermediate in the transfer of an electron to flavodoxin. A structural model of FixABCX, generated using chemical cross-linking in conjunction with homology modeling, revealed plausible electron transfer pathways to both high- and low-potential acceptors. Altogether, this study informs a mechanism for electron bifurcation, offering insight into a unique method for delivery of low-potential electrons required for energy-intensive biochemical conversions.« less

Coherent control of the formation of cold heteronuclear molecules by photoassociation

NASA Astrophysics Data System (ADS)

de Lima, Emanuel F.

2017-01-01

We consider the formation of cold diatomic molecules in the electronic ground state by photoassociation of atoms of dissimilar species. A combination of two transition pathways from the free colliding pair of atoms to a bound vibrational level of the electronic molecular ground state is envisioned. The first pathway consists of a pump-dump scheme with two time-delayed laser pulses in the near-infrared frequency domain. The pump pulse drives the transition to a bound vibrational level of an excited electronic state, while the dump pulse transfers the population to a bound vibrational level of the electronic ground state. The second pathway takes advantage of the existing permanent dipole moment and employs a single pulse in the far-infrared domain to drive the transition from the unbound atoms directly to a bound vibrational level in the electronic ground state. We show that this scheme offers the possibility to coherently control the photoassociation yield by manipulating the relative phase and timing of the pulses. The photoassociation mechanism is illustrated for the formation of cold LiCs molecules.

Transfer of the cytochrome P450-dependent dhurrin pathway from Sorghum bicolor into Nicotiana tabacum chloroplasts for light-driven synthesis.

PubMed

Gnanasekaran, Thiyagarajan; Karcher, Daniel; Nielsen, Agnieszka Zygadlo; Martens, Helle Juel; Ruf, Stephanie; Kroop, Xenia; Olsen, Carl Erik; Motawie, Mohammed Saddik; Pribil, Mathias; Møller, Birger Lindberg; Bock, Ralph; Jensen, Poul Erik

2016-04-01

Plant chloroplasts are light-driven cell factories that have great potential to act as a chassis for metabolic engineering applications. Using plant chloroplasts, we demonstrate how photosynthetic reducing power can drive a metabolic pathway to synthesise a bio-active natural product. For this purpose, we stably engineered the dhurrin pathway from Sorghum bicolor into the chloroplasts of Nicotiana tabacum (tobacco). Dhurrin is a cyanogenic glucoside and its synthesis from the amino acid tyrosine is catalysed by two membrane-bound cytochrome P450 enzymes (CYP79A1 and CYP71E1) and a soluble glucosyltransferase (UGT85B1), and is dependent on electron transfer from a P450 oxidoreductase. The entire pathway was introduced into the chloroplast by integrating CYP79A1, CYP71E1, and UGT85B1 into a neutral site of the N. tabacum chloroplast genome. The two P450s and the UGT85B1 were functional when expressed in the chloroplasts and converted endogenous tyrosine into dhurrin using electrons derived directly from the photosynthetic electron transport chain, without the need for the presence of an NADPH-dependent P450 oxidoreductase. The dhurrin produced in the engineered plants amounted to 0.1-0.2% of leaf dry weight compared to 6% in sorghum. The results obtained pave the way for plant P450s involved in the synthesis of economically important compounds to be engineered into the thylakoid membrane of chloroplasts, and demonstrate that their full catalytic cycle can be driven directly by photosynthesis-derived electrons. © The Author 2016. Published by Oxford University Press on behalf of the Society for Experimental Biology.

Gene expression profiling of breast cancer cell lines treated with proton and electron radiations.

PubMed

Bravatà, Valentina; Minafra, Luigi; Cammarata, Francesco Paolo; Pisciotta, Pietro; Lamia, Debora; Marchese, Valentina; Manti, Lorenzo; Cirrone, Giuseppe Ap; Gilardi, Maria Carla; Cuttone, Giacomo; Forte, Giusi Irma; Russo, Giorgio

2018-06-11

Technological advances in radiation therapy are evolving with the use of hadrons, such as protons, indicated for tumors where conventional radiotherapy does not give significant advantages or for tumors located in sensitive regions, which need the maximum of dose-saving of the surrounding healthy tissues. The genomic response to conventional and non conventional Linear Energy Transfer exposure is a poor investigated topic and became an issue of radiobiological interest. The aim of this work was to analyze and compare molecular responses in term of gene expression profiles, induced by electron and proton irradiation in breast cancer cell lines. We studied the gene expression profiling differences by cDNA microarray activated in response to electron and proton irradiation with different Linear Energy Transfer values, among three breast cell lines (the tumorigenic MCF7 and MDA-MB-231 and the non tumorigenic MCF10A), exposed to the same sub-lethal dose of 9 Gy. Gene expression profiling pathway analyses showed the activation of different signaling and molecular networks in a cell line and radiation type-dependent manner. MCF10A and MDA-MB-231 cell lines were found to induce factors and pathways involved in the immunological process control. Here we describe in a detailed way the gene expression profiling and pathways activated after electron and proton irradiation in breast cancer cells. Summarizing, although specific pathways are activated in a radiation type-dependent manner, each cell line activates overall similar molecular networks in response to both these two types of ionizing radiation. Advances in knowledge: In the era of personalized medicine and breast cancer target-directed intervention, we trust that this study could drive radiation therapy towards personalized treatments, evaluating possible combined treatments, based on the molecular characterization.

Charge Separation and Triplet Exciton Formation Pathways in Small-Molecule Solar Cells as Studied by Time-Resolved EPR Spectroscopy

DOE PAGES

Thomson, Stuart A. J.; Niklas, Jens; Mardis, Kristy L.; ...

2017-09-13

Organic solar cells are a promising renewable energy technology, offering the advantages of mechanical flexibility and solution processability. An understanding of the electronic excited states and charge separation pathways in these systems is crucial if efficiencies are to be further improved. Here we use light induced electron paramagnetic resonance (LEPR) spectroscopy and density functional theory calculations (DFT) to study the electronic excited states, charge transfer (CT) dynamics and triplet exciton formation pathways in blends of the small molecule donors (DTS(FBTTh 2) 2, DTS(F2BTTh 2) 2, DTS(PTTh 2) 2, DTG(FBTTh 2) 2 and DTG(F2BTTh 2) 2) with the fullerene derivative PCmore » 61BM. Using high frequency EPR the g-tensor of the positive polaron on the donor molecules was determined. The experimental results are compared with DFT calculations which reveal that the spin density of the polaron is distributed over a dimer or trimer. Time-resolved EPR (TR-EPR) spectra attributed to singlet CT states were identified and the polarization patterns revealed similar charge separation dynamics in the four fluorobenzothiadiazole donors, while charge separation in the DTS(PTTh 2) 2 blend is slower. Using TR-EPR we also investigated the triplet exciton formation pathways in the blend. The polarization patterns reveal that the excitons originate from both intersystem crossing (ISC) and back electron transfer (BET) processes. The DTS(PTTh 2) 2 blend was found to contain substantially more triplet excitons formed by BET than the fluorobenzothiadiazole blends. As a result, the higher BET triplet exciton population in the DTS(PTTh 2) 2 blend is in accordance with the slower charge separation dynamics observed in this blend.« less

Charge Separation and Triplet Exciton Formation Pathways in Small Molecule Solar Cells as Studied by Time-resolved EPR Spectroscopy.

PubMed

Thomson, Stuart A J; Niklas, Jens; Mardis, Kristy L; Mallares, Christopher; Samuel, Ifor D W; Poluektov, Oleg G

2017-10-19

Organic solar cells are a promising renewable energy technology, offering the advantages of mechanical flexibility and solution processability. An understanding of the electronic excited states and charge separation pathways in these systems is crucial if efficiencies are to be further improved. Here we use light induced electron paramagnetic resonance (LEPR) spectroscopy and density functional theory calculations (DFT) to study the electronic excited states, charge transfer (CT) dynamics and triplet exciton formation pathways in blends of the small molecule donors (DTS(FBTTh 2 ) 2 , DTS(F 2 BTTh 2 ) 2 , DTS(PTTh 2 ) 2 , DTG(FBTTh 2 ) 2 and DTG(F 2 BTTh 2 ) 2 ) with the fullerene derivative PC 61 BM. Using high frequency EPR the g-tensor of the positive polaron on the donor molecules was determined. The experimental results are compared with DFT calculations which reveal that the spin density of the polaron is distributed over a dimer or trimer. Time-resolved EPR (TR-EPR) spectra attributed to singlet CT states were identified and the polarization patterns revealed similar charge separation dynamics in the four fluorobenzothiadiazole donors, while charge separation in the DTS(PTTh 2 ) 2 blend is slower. Using TR-EPR we also investigated the triplet exciton formation pathways in the blend. The polarization patterns reveal that the excitons originate from both intersystem crossing (ISC) and back electron transfer (BET) processes. The DTS(PTTh 2 ) 2 blend was found to contain substantially more triplet excitons formed by BET than the fluorobenzothiadiazole blends. The higher BET triplet exciton population in the DTS(PTTh 2 ) 2 blend is in accordance with the slower charge separation dynamics observed in this blend.

Charge Separation and Triplet Exciton Formation Pathways in Small-Molecule Solar Cells as Studied by Time-Resolved EPR Spectroscopy

DOE Office of Scientific and Technical Information (OSTI.GOV)

Thomson, Stuart A. J.; Niklas, Jens; Mardis, Kristy L.

Organic solar cells are a promising renewable energy technology, offering the advantages of mechanical flexibility and solution processability. An understanding of the electronic excited states and charge separation pathways in these systems is crucial if efficiencies are to be further improved. Here we use light induced electron paramagnetic resonance (LEPR) spectroscopy and density functional theory calculations (DFT) to study the electronic excited states, charge transfer (CT) dynamics and triplet exciton formation pathways in blends of the small molecule donors (DTS(FBTTh 2) 2, DTS(F2BTTh 2) 2, DTS(PTTh 2) 2, DTG(FBTTh 2) 2 and DTG(F2BTTh 2) 2) with the fullerene derivative PCmore » 61BM. Using high frequency EPR the g-tensor of the positive polaron on the donor molecules was determined. The experimental results are compared with DFT calculations which reveal that the spin density of the polaron is distributed over a dimer or trimer. Time-resolved EPR (TR-EPR) spectra attributed to singlet CT states were identified and the polarization patterns revealed similar charge separation dynamics in the four fluorobenzothiadiazole donors, while charge separation in the DTS(PTTh 2) 2 blend is slower. Using TR-EPR we also investigated the triplet exciton formation pathways in the blend. The polarization patterns reveal that the excitons originate from both intersystem crossing (ISC) and back electron transfer (BET) processes. The DTS(PTTh 2) 2 blend was found to contain substantially more triplet excitons formed by BET than the fluorobenzothiadiazole blends. As a result, the higher BET triplet exciton population in the DTS(PTTh 2) 2 blend is in accordance with the slower charge separation dynamics observed in this blend.« less

Time-Resolved Magnetic Field Effects Distinguish Loose Ion Pairs from Exciplexes

PubMed Central

2013-01-01

We describe the experimental investigation of time-resolved magnetic field effects in exciplex-forming organic donor–acceptor systems. In these systems, the photoexcited acceptor state is predominantly deactivated by bimolecular electron transfer reactions (yielding radical ion pairs) or by direct exciplex formation. The delayed fluorescence emitted by the exciplex is magnetosensitive if the reaction pathway involves loose radical ion pair states. This magnetic field effect results from the coherent interconversion between the electronic singlet and triplet radical ion pair states as described by the radical pair mechanism. By monitoring the changes in the exciplex luminescence intensity when applying external magnetic fields, details of the reaction mechanism can be elucidated. In this work we present results obtained with the fluorophore-quencher pair 9,10-dimethylanthracene/N,N-dimethylaniline (DMA) in solvents of systematically varied permittivity. A simple theoretical model is introduced that allows discriminating the initial state of quenching, viz., the loose ion pair and the exciplex, based on the time-resolved magnetic field effect. The approach is validated by applying it to the isotopologous fluorophore-quencher pairs pyrene/DMA and pyrene-d10/DMA. We detect that both the exciplex and the radical ion pair are formed during the initial quenching stage. Upon increasing the solvent polarity, the relative importance of the distant electron transfer quenching increases. However, even in comparably polar media, the exciplex pathway remains remarkably significant. We discuss our results in relation to recent findings on the involvement of exciplexes in photoinduced electron transfer reactions. PMID:24041160

The electron transfer system of syntrophically grown Desulfovibrio vulgaris

DOE Office of Scientific and Technical Information (OSTI.GOV)

Walker, C.B.; He, Z.; Yang, Z.K.

2009-05-01

Interspecies hydrogen transfer between organisms producing and consuming hydrogen promotes the decomposition of organic matter in most anoxic environments. Although syntrophic couplings between hydrogen producers and consumers are a major feature of the carbon cycle, mechanisms for energy recovery at the extremely low free energies of reactions typical of these anaerobic communities have not been established. In this study, comparative transcriptional analysis of a model sulfate-reducing microbe, Desulfovibrio vulgaris Hildenborough, suggested the use of alternative electron transfer systems dependent upon growth modality. During syntrophic growth on lactate with a hydrogenotrophic methanogen, D. vulgaris up-regulated numerous genes involved in electron transfermore » and energy generation when compared with sulfate-limited monocultures. In particular, genes coding for the putative membrane-bound Coo hydrogenase, two periplasmic hydrogenases (Hyd and Hyn) and the well-characterized high-molecular weight cytochrome (Hmc) were among the most highly expressed and up-regulated. Additionally, a predicted operon coding for genes involved in lactate transport and oxidation exhibited up-regulation, further suggesting an alternative pathway for electrons derived from lactate oxidation during syntrophic growth. Mutations in a subset of genes coding for Coo, Hmc, Hyd and Hyn impaired or severely limited syntrophic growth but had little affect on growth via sulfate-respiration. These results demonstrate that syntrophic growth and sulfate-respiration use largely independent energy generation pathways and imply that understanding of microbial processes sustaining nutrient cycling must consider lifestyles not captured in pure culture.« less

The Electron Transfer System of Syntrophically Grown Desulfovibrio vulgaris

DOE Office of Scientific and Technical Information (OSTI.GOV)

PBD; ENIGMA; GTL

2009-06-22

Interspecies hydrogen transfer between organisms producing and consuming hydrogen promotes the decomposition of organic matter in most anoxic environments. Although syntrophic couplings between hydrogen producers and consumers are a major feature of the carbon cycle, mechanisms for energy recovery at the extremely low free energies of reactions typical of these anaerobic communities have not been established. In this study, comparative transcriptional analysis of a model sulfate-reducing microbe, Desulfovibrio vulgaris Hildenborough, suggested the use of alternative electron transfer systems dependent upon growth modality. During syntrophic growth on lactate with a hydrogenotrophic methanogen, D. vulgaris up-regulated numerous genes involved in electron transfermore » and energy generation when compared with sulfate-limited monocultures. In particular, genes coding for the putative membrane-bound Coo hydrogenase, two periplasmic hydrogenases (Hyd and Hyn) and the well-characterized high-molecular weight cytochrome (Hmc) were among the most highly expressed and up-regulated. Additionally, a predicted operon coding for genes involved in lactate transport and oxidation exhibited up-regulation, further suggesting an alternative pathway for electrons derived from lactate oxidation during syntrophic growth. Mutations in a subset of genes coding for Coo, Hmc, Hyd and Hyn impaired or severely limited syntrophic growth but had little affect on growth via sulfate-respiration. These results demonstrate that syntrophic growth and sulfate-respiration use largely independent energy generation pathways and imply that understanding of microbial processes sustaining nutrient cycling must consider lifestyles not captured in pure culture.« less

Electrostatic orientation of the electron-transfer complex between plastocyanin and cytochrome c.

PubMed

Roberts, V A; Freeman, H C; Olson, A J; Tainer, J A; Getzoff, E D

1991-07-15

To understand the specificity and efficiency of protein-protein interactions promoting electron transfer, we evaluated the role of electrostatic forces in precollision orientation by the development of two new methods, computer graphics alignment of protein electrostatic fields and a systematic orientational search of intermolecular electrostatic energies for two proteins at present separation distances. We applied these methods to the plastocyanin/cytochrome c interaction, which is faster than random collision, but too slow for study by molecular dynamics techniques. Significant electrostatic potentials were concentrated on one-fourth (969 A2) of the plastocyanin surface, with the greatest negative potential centered on the Tyr-83 hydroxyl within the acidic patch, and on one-eighth (632 A2) of the cytochrome c surface, with the greatest positive potential centered near the exposed heme edge. Coherent electrostatic fields occurred only over these regions, suggesting that local, rather than global, charge complementarity controls productive recognition. The three energetically favored families of pre-collision orientations all directed the positive region surrounding the heme edge of cytochrome c toward the acidic patch of plastocyanin but differed in heme plane orientation. Analysis of electrostatic fields, electrostatic energies of precollision orientations with 12 and 6 A separation distances, and surface topographies suggested that the favored orientations should converge to productive complexes promoting a single electron-transfer pathway from the cytochrome c heme edge to Tyr-83 of plastocyanin. Direct interactions of the exposed Cu ligand in plastocyanin with the cytochrome c heme edge are not unfavorable sterically or electrostatically but should occur no faster than randomly, indicating that this is not the primary pathway for electron transfer.

Crystal Structure and Catalytic Mechanism of 7-Hydroxymethyl Chlorophyll a Reductase*

PubMed Central

Wang, Xiao; Liu, Lin

2016-01-01

7-Hydroxymethyl chlorophyll a reductase (HCAR) catalyzes the second half-reaction in chlorophyll b to chlorophyll a conversion. HCAR is required for the degradation of light-harvesting complexes and is necessary for efficient photosynthesis by balancing the chlorophyll a/b ratio. Reduction of the hydroxymethyl group uses redox cofactors [4Fe-4S] cluster and FAD to transfer electrons and is difficult because of the strong carbon-oxygen bond. Here, we report the crystal structure of Arabidopsis HCAR at 2.7-Å resolution and reveal that two [4Fe-4S]clusters and one FAD within a very short distance form a consecutive electron pathway to the substrate pocket. In vitro kinetic analysis confirms the ferredoxin-dependent electron transport chain, thus supporting a proton-activated electron transfer mechanism. HCAR resembles a partial reconstruction of an archaeal F420-reducing [NiFe] hydrogenase, which suggests a common mode of efficient proton-coupled electron transfer through conserved cofactor arrangements. Furthermore, the trimeric form of HCAR provides a biological clue of its interaction with light-harvesting complex II. PMID:27072131

Novel Electron-Phonon Relaxation Pathway in Graphite Revealed by Time-Resolved Raman Scattering and Angle-Resolved Photoemission Spectroscopy.

PubMed

Yang, Jhih-An; Parham, Stephen; Dessau, Daniel; Reznik, Dmitry

2017-01-19

Time dynamics of photoexcited electron-hole pairs is important for a number of technologies, in particular solar cells. We combined ultrafast pump-probe Raman scattering and photoemission to directly follow electron-hole excitations as well as the G-phonon in graphite after an excitation by an intense laser pulse. This phonon is known to couple relatively strongly to electrons. Cross-correlating effective electronic and phonon temperatures places new constraints on model-based fits. The accepted two-temperature model predicts that G-phonon population should start to increase as soon as excited electron-hole pairs are created and that the rate of increase should not depend strongly on the pump fluence. Instead we found that the increase of the G-phonon population occurs with a delay of ~65 fs. This time-delay is also evidenced by the absence of the so-called self-pumping for G phonons. It decreases with increased pump fluence. We show that these observations imply a new relaxation pathway: Instead of hot carriers transferring energy to G-phonons directly, the energy is first transferred to optical phonons near the zone boundary K-points, which then decay into G-phonons via phonon-phonon scattering. Our work demonstrates that phonon-phonon interactions must be included in any calculations of hot carrier relaxation in optical absorbers even when only short timescales are considered.

Electronic coupling through natural amino acids.

PubMed

Berstis, Laura; Beckham, Gregg T; Crowley, Michael F

2015-12-14

Myriad scientific domains concern themselves with biological electron transfer (ET) events that span across vast scales of rate and efficiency through a remarkably fine-tuned integration of amino acid (AA) sequences, electronic structure, dynamics, and environment interactions. Within this intricate scheme, many questions persist as to how proteins modulate electron-tunneling properties. To help elucidate these principles, we develop a model set of peptides representing the common α-helix and β-strand motifs including all natural AAs within implicit protein-environment solvation. Using an effective Hamiltonian strategy with density functional theory, we characterize the electronic coupling through these peptides, furthermore considering side-chain dynamics. For both motifs, predictions consistently show that backbone-mediated electronic coupling is distinctly sensitive to AA type (aliphatic, polar, aromatic, negatively charged and positively charged), and to side-chain orientation. The unique properties of these residues may be employed to design activated, deactivated, or switch-like superexchange pathways. Electronic structure calculations and Green's function analyses indicate that localized shifts in the electron density along the peptide play a role in modulating these pathways, and further substantiate the experimentally observed behavior of proline residues as superbridges. The distinct sensitivities of tunneling pathways to sequence and conformation revealed in this electronic coupling database help improve our fundamental understanding of the broad diversity of ET reactivity and provide guiding principles for peptide design.

Anisotropic Covalency Contributions to Superexchange Pathways in Type One Copper Active Sites

PubMed Central

2015-01-01

Type one (T1) Cu sites deliver electrons to catalytic Cu active sites: the mononuclear type two (T2) Cu site in nitrite reductases (NiRs) and the trinuclear Cu cluster in the multicopper oxidases (MCOs). The T1 Cu and the remote catalytic sites are connected via a Cys-His intramolecular electron-transfer (ET) bridge, which contains two potential ET pathways: P1 through the protein backbone and P2 through the H-bond between the Cys and the His. The high covalency of the T1 Cu–S(Cys) bond is shown here to activate the T1 Cu site for hole superexchange via occupied valence orbitals of the bridge. This covalency-activated electronic coupling (HDA) facilitates long-range ET through both pathways. These pathways can be selectively activated depending on the geometric and electronic structure of the T1 Cu site and thus the anisotropic covalency of the T1 Cu–S(Cys) bond. In NiRs, blue (π-type) T1 sites utilize P1 and green (σ-type) T1 sites utilize P2, with P2 being more efficient. Comparing the MCOs to NiRs, the second-sphere environment changes the conformation of the Cys-His pathway, which selectively activates HDA for superexchange by blue π sites for efficient turnover in catalysis. These studies show that a given protein bridge, here Cys-His, provides different superexchange pathways and electronic couplings depending on the anisotropic covalencies of the donor and acceptor metal sites. PMID:25310460

[Promoting efficiency of microbial extracellular electron transfer by synthetic biology].

PubMed

Li, Feng; Song, Hao

2017-03-25

Electroactive bacteria, including electrigenic bacteria (exoelectrogens) and electroautotrophic bacteria, implement microbial bioelectrocatalysis processes via bi-directional exchange of electrons and energy with environments, enabling a wide array of applications in environmental and energy fields, including microbial fuel cells (MFC), microbial electrolysis cells (MEC), microbial electrosynthesis (MES) to produce electricity and bulk fine chemicals. However, the low efficiency in the extracellular electron transfer (EET) of exoelectrogens and electrotrophic microbes limited their industrial applications. Here, we reviewed synthetic biology approaches to engineer electroactive microorganisms to break the bottleneck of their EET pathways, to achieve higher efficiency of EET of a number of electroactive microorganisms. Such efforts will lead to a breakthrough in the applications of these electroactive microorganisms and microbial electrocatalysis systems.

[The electronic health record: computerised provider order entry and the electronic instruction document as new functionalities].

PubMed

Derikx, Joep P M; Erdkamp, Frans L G; Hoofwijk, A G M

2013-01-01

An electronic health record (EHR) should provide 4 key functionalities: (a) documenting patient data; (b) facilitating computerised provider order entry; (c) displaying the results of diagnostic research; and (d) providing support for healthcare providers in the clinical decision-making process.- Computerised provider order entry into the EHR enables the electronic receipt and transfer of orders to ancillary departments, which can take the place of handwritten orders.- By classifying the computer provider order entries according to disorders, digital care pathways can be created. Such care pathways could result in faster and improved diagnostics.- Communicating by means of an electronic instruction document that is linked to a computerised provider order entry facilitates the provision of healthcare in a safer, more efficient and auditable manner.- The implementation of a full-scale EHR has been delayed as a result of economic, technical and legal barriers, as well as some resistance by physicians.

Oxidative bioelectrocatalysis: From natural metabolic pathways to synthetic metabolons and minimal enzyme cascades.

PubMed

Minteer, Shelley D

2016-05-01

Anodic bioelectrodes for biofuel cells are more complex than cathodic bioelectrodes for biofuel cells, because laccase and bilirubin oxidase can individually catalyze four electron reduction of oxygen to water, whereas most anodic enzymes only do a single two electron oxidation of a complex fuel (i.e. glucose oxidase oxidizing glucose to gluconolactone while generating 2 electrons of the total 24 electrons), so enzyme cascades are typically needed for complete oxidation of the fuel. This review article will discuss the lessons learned from natural metabolic pathways about multi-step oxidation and how those lessons have been applied to minimal or artificial enzyme cascades. This article is part of a Special Issue entitled Biodesign for Bioenergetics--the design and engineering of electronic transfer cofactors, proteins and protein networks, edited by Ronald L. Koder and J.L. Ross Anderson. Copyright © 2015. Published by Elsevier B.V.

Structure-Function of the Cytochrome b 6f Complex of Oxygenic Photosynthesis

DOE Office of Scientific and Technical Information (OSTI.GOV)

Cramer, W. A.; Yamashita, E.; Baniulis, D.

2014-03-20

Structure–function of the major integral membrane cytochrome b 6f complex that functions in cyanobacteria, algae, and green plants to transfer electrons between the two reaction center complexes in the electron transport chain of oxygenic photosynthesis is discussed in the context of recently obtained crystal structures of the complex and soluble domains of cytochrome f and the Rieske iron–sulfur protein. The energy-transducing function of the complex, generation of the proton trans-membrane electrochemical potential gradient, centers on the oxidation/reduction pathways of the plastoquinol/plastoquinone (QH 2/Q), the proton donor/acceptor within the complex. These redox reactions are carried out by five redox prosthetic groupsmore » embedded in each monomer, the high potential two iron–two sulfur cluster and the heme of cytochrome f on the electropositive side (p) of the complex, two noncovalently bound b-type hemes that cross the complex and the membrane, and a covalently bound c-type heme (c n) on the electronegative side (n). These five redox-active groups are organized in high- (cyt f/[2Fe–2S] and low-potential (hemes b p, b n, c n) electron transport pathways that oxidize and reduce the quinol and quinone on the p- and n-sides in a Q-cycle-type mechanism, while translocating as many as 2 H + to the p-side aqueous side for every electron transferred through the high potential chain to the photosystem I reaction center. The presence of heme c n and the connection of the n-side of the membrane and b 6f complex to the cyclic electron transport chain indicate that the Q cycle in the oxygenic photosynthetic electron transport chain differs from those connected to the bc 1 complex in the mitochondrial respiratory chain and the chain in photosynthetic bacteria. Inferences from the structure and C2 symmetry of the complex for the pathway of QH 2/Q transfer within the complex, problems posed by the presence of lipid in the inter-monomer cavity, and the narrow portal for QH2 passage through the p-side oxidation site proximal to the [2Fe–2S] cluster are discussed.« less

Quantum coherence spectroscopy reveals complex dynamics in bacterial light-harvesting complex 2 (LH2).

PubMed

Harel, Elad; Engel, Gregory S

2012-01-17

Light-harvesting antenna complexes transfer energy from sunlight to photosynthetic reaction centers where charge separation drives cellular metabolism. The process through which pigments transfer excitation energy involves a complex choreography of coherent and incoherent processes mediated by the surrounding protein and solvent environment. The recent discovery of coherent dynamics in photosynthetic light-harvesting antennae has motivated many theoretical models exploring effects of interference in energy transfer phenomena. In this work, we provide experimental evidence of long-lived quantum coherence between the spectrally separated B800 and B850 rings of the light-harvesting complex 2 (LH2) of purple bacteria. Spectrally resolved maps of the detuning, dephasing, and the amplitude of electronic coupling between excitons reveal that different relaxation pathways act in concert for optimal transfer efficiency. Furthermore, maps of the phase of the signal suggest that quantum mechanical interference between different energy transfer pathways may be important even at ambient temperature. Such interference at a product state has already been shown to enhance the quantum efficiency of transfer in theoretical models of closed loop systems such as LH2.

Quantum coherence spectroscopy reveals complex dynamics in bacterial light-harvesting complex 2 (LH2)

PubMed Central

Harel, Elad; Engel, Gregory S.

2012-01-01

Light-harvesting antenna complexes transfer energy from sunlight to photosynthetic reaction centers where charge separation drives cellular metabolism. The process through which pigments transfer excitation energy involves a complex choreography of coherent and incoherent processes mediated by the surrounding protein and solvent environment. The recent discovery of coherent dynamics in photosynthetic light-harvesting antennae has motivated many theoretical models exploring effects of interference in energy transfer phenomena. In this work, we provide experimental evidence of long-lived quantum coherence between the spectrally separated B800 and B850 rings of the light-harvesting complex 2 (LH2) of purple bacteria. Spectrally resolved maps of the detuning, dephasing, and the amplitude of electronic coupling between excitons reveal that different relaxation pathways act in concert for optimal transfer efficiency. Furthermore, maps of the phase of the signal suggest that quantum mechanical interference between different energy transfer pathways may be important even at ambient temperature. Such interference at a product state has already been shown to enhance the quantum efficiency of transfer in theoretical models of closed loop systems such as LH2. PMID:22215585

Hyphal formation of Candida albicans is controlled by electron transfer system

DOE Office of Scientific and Technical Information (OSTI.GOV)

Watanabe, Toshihiko; Ogasawara, Ayako; Mikami, Takeshi

2006-09-15

Most Candida albicans cells cultured in RPMI1640 medium at 37 deg. C grow in hyphal form in aerobic conditions, but they grow in yeast form in anaerobic conditions. The hyphal growth of C. albicans was inhibited in glucose-deficient conditions. Malonic acid, an inhibitor of succinate dehydrogenase, enhanced the yeast proliferation of C. albicans, indicating that the hyphal-formation signal was derived from the glycolysis system and the signal was transmitted to the electron transfer system via the citric acid cycle. Thenoyl trifluoro acetone (TTFA), an inhibitor of the signal transmission between complex II and Co Q, significantly inhibited the hyphal growthmore » of C. albicans. Antimycin, KCN, and oligomycin, inhibitors of complex III, IV, and V, respectively, did not inhibit the hyphal growth of C. albicans. The production of mRNAs for the hyphal formation signal was completely inhibited in anaerobic conditions. These results indicate that the electron transfer system functions upstream of the RAS1 signal pathway and activates the expression of the hyphal formation signal. Since the electron transfer system is inactivated in anaerobic conditions, C. albicans grew in yeast form in this condition.« less

Species differences in unlocking B-side electron transfer in bacterial reaction centers

DOE PAGES

Dylla, Nicholas P.; Faries, Kaitlyn M.; Wyllie, Ryan M.; ...

2016-06-21

The structure of the bacterial photosynthetic reaction center (RC) reveals symmetry-related electron transfer (ET) pathways, but only one path is used in native RCs. Analogous mutations have been made in two Rhodobacter (R.) species. A glutamic acid at position 133 in the M subunit increases transmembrane charge separation via the naturally inactive (B-side) path through impacts on primary ET in mutant R. sphaeroidesRCs. Prior work showed that the analogous substitution in the R. capsulatusRC also increases B-side activity, but mainly affects secondary ET. Finally, the overall yields of transmembrane ET are similar, but enabled in fundamentally different ways.

Species differences in unlocking B-side electron transfer in bacterial reaction centers

DOE Office of Scientific and Technical Information (OSTI.GOV)

Dylla, Nicholas P.; Faries, Kaitlyn M.; Wyllie, Ryan M.

The structure of the bacterial photosynthetic reaction center (RC) reveals symmetry-related electron transfer (ET) pathways, but only one path is used in native RCs. Analogous mutations have been made in two Rhodobacter (R.) species. A glutamic acid at position 133 in the M subunit increases transmembrane charge separation via the naturally inactive (B-side) path through impacts on primary ET in mutant R. sphaeroidesRCs. Prior work showed that the analogous substitution in the R. capsulatusRC also increases B-side activity, but mainly affects secondary ET. Finally, the overall yields of transmembrane ET are similar, but enabled in fundamentally different ways.

Oxygen activation by mononuclear nonheme iron dioxygenases involved in the degradation of aromatics.

PubMed

Wang, Yifan; Li, Jiasong; Liu, Aimin

2017-04-01

Molecular oxygen is utilized in numerous metabolic pathways fundamental for life. Mononuclear nonheme iron-dependent oxygenase enzymes are well known for their involvement in some of these pathways, activating O 2 so that oxygen atoms can be incorporated into their primary substrates. These reactions often initiate pathways that allow organisms to use stable organic molecules as sources of carbon and energy for growth. From the myriad of reactions in which these enzymes are involved, this perspective recounts the general mechanisms of aromatic dihydroxylation and oxidative ring cleavage, both of which are ubiquitous chemical reactions found in life-sustaining processes. The organic substrate provides all four electrons required for oxygen activation and insertion in the reactions mediated by extradiol and intradiol ring-cleaving catechol dioxygenases. In contrast, two of the electrons are provided by NADH in the cis-dihydroxylation mechanism of Rieske dioxygenases. The catalytic nonheme Fe center, with the aid of active site residues, facilitates these electron transfers to O 2 as key elements of the activation processes. This review discusses some general questions for the catalytic strategies of oxygen activation and insertion into aromatic compounds employed by mononuclear nonheme iron-dependent dioxygenases. These include: (1) how oxygen is activated, (2) whether there are common intermediates before oxygen transfer to the aromatic substrate, and (3) are these key intermediates unique to mononuclear nonheme iron dioxygenases?

The Electron Bifurcating FixABCX Protein Complex from Azotobacter vinelandii: Generation of Low-Potential Reducing Equivalents for Nitrogenase Catalysis.

PubMed

Ledbetter, Rhesa N; Garcia Costas, Amaya M; Lubner, Carolyn E; Mulder, David W; Tokmina-Lukaszewska, Monika; Artz, Jacob H; Patterson, Angela; Magnuson, Timothy S; Jay, Zackary J; Duan, H Diessel; Miller, Jacquelyn; Plunkett, Mary H; Hoben, John P; Barney, Brett M; Carlson, Ross P; Miller, Anne-Frances; Bothner, Brian; King, Paul W; Peters, John W; Seefeldt, Lance C

2017-08-15

The biological reduction of dinitrogen (N 2 ) to ammonia (NH 3 ) by nitrogenase is an energetically demanding reaction that requires low-potential electrons and ATP; however, pathways used to deliver the electrons from central metabolism to the reductants of nitrogenase, ferredoxin or flavodoxin, remain unknown for many diazotrophic microbes. The FixABCX protein complex has been proposed to reduce flavodoxin or ferredoxin using NADH as the electron donor in a process known as electron bifurcation. Herein, the FixABCX complex from Azotobacter vinelandii was purified and demonstrated to catalyze an electron bifurcation reaction: oxidation of NADH (E m = -320 mV) coupled to reduction of flavodoxin semiquinone (E m = -460 mV) and reduction of coenzyme Q (E m = 10 mV). Knocking out fix genes rendered Δrnf A. vinelandii cells unable to fix dinitrogen, confirming that the FixABCX system provides another route for delivery of electrons to nitrogenase. Characterization of the purified FixABCX complex revealed the presence of flavin and iron-sulfur cofactors confirmed by native mass spectrometry, electron paramagnetic resonance spectroscopy, and transient absorption spectroscopy. Transient absorption spectroscopy further established the presence of a short-lived flavin semiquinone radical, suggesting that a thermodynamically unstable flavin semiquinone may participate as an intermediate in the transfer of an electron to flavodoxin. A structural model of FixABCX, generated using chemical cross-linking in conjunction with homology modeling, revealed plausible electron transfer pathways to both high- and low-potential acceptors. Overall, this study informs a mechanism for electron bifurcation, offering insight into a unique method for delivery of low-potential electrons required for energy-intensive biochemical conversions.

The Electron Bifurcating FixABCX Protein Complex from Azotobacter vinelandii: Generation of Low-Potential Reducing Equivalents for Nitrogenase Catalysis

DOE PAGES

Ledbetter, Rhesa N.; Garcia Costas, Amaya M.; Lubner, Carolyn E.; ...

2017-07-13

The biological reduction of dinitrogen (N 2) to ammonia (NH 3) by nitrogenase is an energetically demanding reaction that requires low-potential electrons and ATP; however, pathways used to deliver the electrons from central metabolism to the reductants of nitrogenase, ferredoxin or flavodoxin, remain unknown for many diazotrophic microbes. The FixABCX protein complex has been proposed to reduce flavodoxin or ferredoxin using NADH as the electron donor in a process known as electron bifurcation. Herein, the FixABCX complex from Azotobacter vinelandii was purified and demonstrated to catalyze an electron bifurcation reaction: oxidation of NADH (E m = -320 mV) coupled tomore » reduction of flavodoxin semiquinone (E m = -460 mV) and reduction of coenzyme Q (E m = 10 mV). Knocking out fix genes rendered ..delta..rnf A. vinelandii cells unable to fix dinitrogen, confirming that the FixABCX system provides another route for delivery of electrons to nitrogenase. Characterization of the purified FixABCX complex revealed the presence of flavin and iron-sulfur cofactors confirmed by native mass spectrometry, electron paramagnetic resonance spectroscopy, and transient absorption spectroscopy. Transient absorption spectroscopy further established the presence of a short-lived flavin semiquinone radical, suggesting that a thermodynamically unstable flavin semiquinone may participate as an intermediate in the transfer of an electron to flavodoxin. A structural model of FixABCX, generated using chemical cross-linking in conjunction with homology modeling, revealed plausible electron transfer pathways to both high- and low-potential acceptors. Altogether, this study informs a mechanism for electron bifurcation, offering insight into a unique method for delivery of low-potential electrons required for energy-intensive biochemical conversions.« less

Carbon-dependent control of electron transfer and central carbon pathway genes for methane biosynthesis in the Archaean, Methanosarcina acetivorans strain C2A

PubMed Central

2010-01-01

Background The archaeon, Methanosarcina acetivorans strain C2A forms methane, a potent greenhouse gas, from a variety of one-carbon substrates and acetate. Whereas the biochemical pathways leading to methane formation are well understood, little is known about the expression of the many of the genes that encode proteins needed for carbon flow, electron transfer and/or energy conservation. Quantitative transcript analysis was performed on twenty gene clusters encompassing over one hundred genes in M. acetivorans that encode enzymes/proteins with known or potential roles in substrate conversion to methane. Results The expression of many seemingly "redundant" genes/gene clusters establish substrate dependent control of approximately seventy genes for methane production by the pathways for methanol and acetate utilization. These include genes for soluble-type and membrane-type heterodisulfide reductases (hdr), hydrogenases including genes for a vht-type F420 non-reducing hydrogenase, molybdenum-type (fmd) as well as tungsten-type (fwd) formylmethanofuran dehydrogenases, genes for rnf and mrp-type electron transfer complexes, for acetate uptake, plus multiple genes for aha- and atp-type ATP synthesis complexes. Analysis of promoters for seven gene clusters reveal UTR leaders of 51-137 nucleotides in length, raising the possibility of both transcriptional and translational levels of control. Conclusions The above findings establish the differential and coordinated expression of two major gene families in M. acetivorans in response to carbon/energy supply. Furthermore, the quantitative mRNA measurements demonstrate the dynamic range for modulating transcript abundance. Since many of these gene clusters in M. acetivorans are also present in other Methanosarcina species including M. mazei, and in M. barkeri, these findings provide a basis for predicting related control in these environmentally significant methanogens. PMID:20178638

Electron-Transfer Kinetics of Redox Centers Anchored to Metal Surfaces: Weak- versus Strong-Overlap Reaction Pathways.

DTIC Science & Technology

1983-11-01

constants ket are presented for the one-electron electroreduction of various Co1]:I(NH3)5X complexes bound to mercury, platinum, and gold surfaces...electroreduction of various Co^^(NH𔃽)𔃿X complexes bound to mercury, platinum, and gold surfaces via either small inorganic or extended organic ligands X. t...platinum, gold , and copper, to enable values of ke* to be obtained for the one-electron reduction of the surface-Douna_redox center.2.3 These

Multiple electron injection dynamics in linearly-linked two dye co-sensitized nanocrystalline metal oxide electrodes for dye-sensitized solar cells.

PubMed

Shen, Qing; Ogomi, Yuhei; Park, Byung-wook; Inoue, Takafumi; Pandey, Shyam S; Miyamoto, Akari; Fujita, Shinsuke; Katayama, Kenji; Toyoda, Taro; Hayase, Shuzi

2012-04-07

Understanding the electron transfer dynamics at the interface between dye sensitizer and semiconductor nanoparticle is very important for both a fundamental study and development of dye-sensitized solar cells (DSCs), which are a potential candidate for next generation solar cells. In this study, we have characterized the ultrafast photoexcited electron dynamics in a newly produced linearly-linked two dye co-sensitized solar cell using both a transient absorption (TA) and an improved transient grating (TG) technique, in which tin(IV) 2,11,20,29-tetra-tert-butyl-2,3-naphthalocyanine (NcSn) and cis-diisothiocyanato-bis(2,2'-bipyridyl-4,4'-dicarboxylato)ruthenium(II) bis(tetrabutylammonium) (N719) are molecularly and linearly linked and are bonded to the surface of a nanocrystalline tin dioxide (SnO(2)) electrode by a metal-O-metal linkage (i.e. SnO(2)-NcSn-N719). By comparing the TA and TG kinetics of NcSn, N719, and hybrid NcSn-N719 molecules adsorbed onto both of the SnO(2) and zirconium dioxide (ZrO(2)) nanocrystalline films, the forward and backward electron transfer dynamics in SnO(2)-NcSn-N719 were clarified. We found that there are two pathways for electron injection from the linearly-linked two dye molecules (NcSn-N719) to SnO(2). The first is a stepwise electron injection, in which photoexcited electrons first transfer from N719 to NcSn with a transfer time of 0.95 ps and then transfer from NcSn to the conduction band (CB) of SnO(2) with two timescales of 1.6 ps and 4.2 ps. The second is direct photoexcited electron transfer from N719 to the CB of SnO(2) with a timescale of 20-30 ps. On the other hand, back electron transfer from SnO(2) to NcSn is on a timescale of about 2 ns, which is about three orders of magnitude slower compared to the forward electron transfer from NcSn to SnO(2). The back electron transfer from NcSn to N719 is on a timescale of about 40 ps, which is about one order slower compared to the forward electron transfer from N719 to NcSn. These results demonstrate that photoexcited electrons can be effectively injected into SnO(2) from both of the N719 and NcSn dyes.

Sulfur-Mediated Electron Shuttling Sustains Microbial Long-Distance Extracellular Electron Transfer with the Aid of Metallic Iron Sulfides.

PubMed

Kondo, Katsuhito; Okamoto, Akihiro; Hashimoto, Kazuhito; Nakamura, Ryuhei

2015-07-07

In addition to serving as an energy source for microbial growth, iron sulfides are proposed to act as naturally occurring electrical wires that mediate long-distance extracellular electron transfer (EET) and bridge spatially discrete redox environments. These hypothetical EET reactions stand on the abilities of microbes to use the interfacial electrochemistry of metallic/semiconductive iron sulfides to maintain metabolisms; however, the mechanisms of these phenomena remain unexplored. To obtain insight into EET to iron sulfides, we monitored EET at the interface between Shewanella oneidensis MR-1 cells and biomineralized iron sulfides in an electrochemical cell. Respiratory current steeply increased with the concomitant formation of poorly crystalline mackinawite (FeS) minerals, indicating that S. oneidensis has the ability to exploit extracellularly formed metallic FeS for long-distance EET. Deletion of major proteins of the metal-reduction (Mtr) pathway (OmcA, MtrC, CymA, and PilD) caused only subtle effects on the EET efficiency, a finding that sharply contrasts the majority of studies that report that the Mtr pathway is indispensable for the reduction of metal oxides and electrodes. The gene expression analyses of polysulfide and thiosulfate reductase suggest the existence of a sulfur-mediated electron-shuttling mechanism by which HS(-) ions and water-soluble polysulfides (HS(n)(-), where n ≥ 2) generated in the periplasmic space deliver electrons from cellular metabolic processes to cell surface-associated FeS. The finding of this Mtr-independent pathway indicates that polysulfide reductases complement the function of outer-membrane cytochromes in EET reactions and, thus, significantly expand the number of microbial species potentially capable of long-distance EET in sulfur-rich anoxic environments.

DOE Office of Scientific and Technical Information (OSTI.GOV)

Matz, Dallas L.; Schalnat, Matthew C.; Pemberton, Jeanne E.

The reaction between small organic molecules and low work function metals is of interest in organometallic, astronomical, and optoelectronic device chemistry. Here, thin, solid-state, amorphous benzene and pyridine films are reacted with Ca at 30 K under ultrahigh vacuum with the reaction progress monitored by Raman spectroscopy. Although both films react with Ca to produce product species identifiable by their vibrational spectroscopic signatures, benzene is less reactive with Ca than pyridine. Benzene reacts by electron transfer from Ca to benzene producing multiple species including the phenyl radical anion, the phenyl radical, and the benzyne diradical. Pyridine initially reacts along amore » similar electron transfer pathway as indicated by the presence of the corresponding pyridyl radical and pyridyne diradical species, but these pyridyl radicals are less stable and subject to further ring-opening reactions that lead to a complex array of smaller molecule reaction products and ultimately amorphous carbon. The elucidation of this reaction pathway provides insight into the reactions of aromatics with Ca that are relevant in the areas of catalysis, astrochemistry, and organic optoelectronics.« less

Free-Energy Landscape and Proton Transfer Pathways in Oxidative Deamination by Methylamine Dehydrogenase.

PubMed

Zelleke, Theodros; Marx, Dominik

2017-01-18

The rate-determining step in the reductive half-reaction of the bacterial enzyme methylamine dehydrogenase, which is proton abstraction from the native substrate methylamine, is investigated using accelerated QM/MM molecular dynamics simulations at room temperature. Generation of the multidimensional thermal free-energy landscape without restriction of the degrees of freedom beyond a multidimensional reaction subspace maps two rather similar pathways for the underlying proton transfer to one of two aspartate carboxyl oxygen atoms, termed OD1 and OD2, which hydrogen bond with Thr122 and Trp108, respectively. Despite significant large-amplitude motion perpendicular to the one-dimensional proton transfer coordinate, due to fluctuations of the donor-acceptor distance of about 3 Å, it is found that the one-dimensional proton transfer free-energy profiles are essentially identical to the minimum free-energy pathways on the multidimensional free-energy landscapes for both proton transfer channels. Proton transfer to one of the acceptor oxygen atoms-the OD2 site-is slightly favored in methylamine dehydrogenase by approximately 2 kcal mol -1 , both kinetically and thermodynamically. Mechanistic analyses reveal that the hydrogen bond between Thr122β and OD1 is always present in the transition state independently of the proton transfer channel. Population analysis confirms that the electronic charge gained upon oxidation of the substrate is delocalized within the ring systems of the tryptophan tryptophylquinone cofactor. © 2017 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.

The photochemistry in Photosystem II at 5 K is different in visible and far-red light.

PubMed

Mokvist, Fredrik; Sjöholm, Johannes; Mamedov, Fikret; Styring, Stenbjörn

2014-07-08

We have earlier shown that all electron transfer reactions in Photosystem II are operational up to 800 nm at room temperature [Thapper, A., et al. (2009) Plant Cell 21, 2391-2401]. This led us to suggest an alternative charge separation pathway for far-red excitation. Here we extend these studies to a very low temperature (5 K). Illumination of Photosystem II (PS II) with visible light at 5 K is known to result in oxidation of almost similar amounts of YZ and the Cyt b559/ChlZ/CarD2 pathway. This is reproduced here using laser flashes at 532 nm, and we find the partition ratio between the two pathways to be 1:0.8 at 5 K [the partition ratio is here defined as (yield of YZ/CaMn4 oxidation):(yield of Cyt b559/ChlZ/CarD2 oxidation)]. The result using far-red laser flashes is very different. We find partition ratios of 1.8 at 730 nm, 2.7 at 740 nm, and >2.7 at 750 nm. No photochemistry involving these pathways is observed above 750 nm at this temperature. Thus, far-red illumination preferentially oxidizes YZ, while the Cyt b559/ChlZ/CarD2 pathway is hardly touched. We propose that the difference in the partition ratio between visible and far-red light at 5 K reflects the formation of a different first stable charge pair. In visible light, the first stable charge pair is considered to be PD1+QA-. In contrast, we propose that the electron hole is residing on the ChlD1 molecule after illumination by far-red light at 5 K, resulting in the first stable charge pair being ChlD1+QA-. ChlD1 is much closer to YZ (11.3 Å) than to any component in the Cyt b559/ChlZ/CarD2 pathway (shortest ChlD1-CarD2 distance of 28.8 Å). This would then explain that far-red illumination preferentially drives efficient electron transfer from YZ. We also discuss mechanisms for accounting for the absorption of the far-red light and the existence of hitherto unobserved charge transfer states. The involvement of two or more of the porphyrin molecules in the core of the Photosystem II reaction center is proposed.

Cation Effects on the Electron-Acceptor Side of Photosystem II.

PubMed

Khan, Sahr; Sun, Jennifer S; Brudvig, Gary W

2015-06-18

The normal pathway of electron transfer on the electron-acceptor side of photosystem II (PSII) involves electron transfer from quinone A, QA, to quinone B, QB. It is possible to redirect electrons from QA(-) to water-soluble Co(III) complexes, which opens a new avenue for harvesting electrons from water oxidation by immobilization of PSII on electrode surfaces. Herein, the kinetics of electron transfer from QA(-) to [Co(III)(terpy)2](3+) (terpy = 2,2';6',2″-terpyridine) are investigated with a spectrophotometric assay revealing that the reaction follows Michaelis-Menten saturation kinetics, is inhibited by cations, and is not affected by variation of the QA reduction potential. A negatively charged site on the stromal surface of the PSII protein complex, composed of glutamic acid residues near QA, is hypothesized to bind cations, especially divalent cations. The cations are proposed to tune the redox properties of QA through electrostatic interactions. These observations may thus explain the molecular basis of the effect of divalent cations like Ca(2+), Sr(2+), Mg(2+), and Zn(2+) on the redox properties of the quinones in PSII, which has previously been attributed to long-range conformational changes propagated from divalent cations binding to the Ca(II)-binding site in the oxygen-evolving complex on the lumenal side of the PSII complex.

Alternative mitochondrial electron transfer for the treatment of neurodegenerative diseases and cancers: Methylene blue connects the dots.

PubMed

Yang, Shao-Hua; Li, Wenjun; Sumien, Nathalie; Forster, Michael; Simpkins, James W; Liu, Ran

2017-10-01

Brain has exceptional high requirement for energy metabolism with glucose as the exclusive energy source. Decrease of brain energy metabolism and glucose uptake has been found in patients of Alzheimer's, Parkinson's and other neurodegenerative diseases, providing a clear link between neurodegenerative disorders and energy metabolism. On the other hand, cancers, including glioblastoma, have increased glucose uptake and rely on aerobic glycolysis for energy metabolism. The switch of high efficient oxidative phosphorylation to low efficient aerobic glycolysis pathway (Warburg effect) provides macromolecule for biosynthesis and proliferation. Current research indicates that methylene blue, a century old drug, can receive electron from NADH in the presence of complex I and donates it to cytochrome c, providing an alternative electron transfer pathway. Methylene blue increases oxygen consumption, decrease glycolysis, and increases glucose uptake in vitro. Methylene blue enhances glucose uptake and regional cerebral blood flow in rats upon acute treatment. In addition, methylene blue provides protective effect in neuron and astrocyte against various insults in vitro and in rodent models of Alzheimer's, Parkinson's, and Huntington's disease. In glioblastoma cells, methylene blue reverses Warburg effect by enhancing mitochondrial oxidative phosphorylation, arrests glioma cell cycle at s-phase, and inhibits glioma cell proliferation. Accordingly, methylene blue activates AMP-activated protein kinase, inhibits downstream acetyl-coA carboxylase and cyclin-dependent kinases. In summary, there is accumulating evidence providing a proof of concept that enhancement of mitochondrial oxidative phosphorylation via alternative mitochondrial electron transfer may offer protective action against neurodegenerative diseases and inhibit cancers proliferation. Copyright © 2015 Elsevier Ltd. All rights reserved.

Molecular alignment effect on the photoassociation process via a pump-dump scheme.

PubMed

Wang, Bin-Bin; Han, Yong-Chang; Cong, Shu-Lin

2015-09-07

The photoassociation processes via the pump-dump scheme for the heternuclear (Na + H → NaH) and the homonuclear (Na + Na → Na2) molecular systems are studied, respectively, using the time-dependent quantum wavepacket method. For both systems, the initial atom pair in the continuum of the ground electronic state (X(1)Σ(+)) is associated into the molecule in the bound states of the excited state (A(1)Σ(+)) by the pump pulse. Then driven by a time-delayed dumping pulse, the prepared excited-state molecule can be transferred to the bound states of the ground electronic state. It is found that the pump process can induce a superposition of the rovibrational levels |v, j〉 on the excited state, which can lead to the field-free alignment of the excited-state molecule. The molecular alignment can affect the dumping process by varying the effective coupling intensity between the two electronic states or by varying the population transfer pathways. As a result, the final population transferred to the bound states of the ground electronic state varies periodically with the delay time of the dumping pulse.

Molecular alignment effect on the photoassociation process via a pump-dump scheme

NASA Astrophysics Data System (ADS)

Wang, Bin-Bin; Han, Yong-Chang; Cong, Shu-Lin

2015-09-01

The photoassociation processes via the pump-dump scheme for the heternuclear (Na + H → NaH) and the homonuclear (Na + Na → Na2) molecular systems are studied, respectively, using the time-dependent quantum wavepacket method. For both systems, the initial atom pair in the continuum of the ground electronic state (X1Σ+) is associated into the molecule in the bound states of the excited state (A1Σ+) by the pump pulse. Then driven by a time-delayed dumping pulse, the prepared excited-state molecule can be transferred to the bound states of the ground electronic state. It is found that the pump process can induce a superposition of the rovibrational levels |v, j> on the excited state, which can lead to the field-free alignment of the excited-state molecule. The molecular alignment can affect the dumping process by varying the effective coupling intensity between the two electronic states or by varying the population transfer pathways. As a result, the final population transferred to the bound states of the ground electronic state varies periodically with the delay time of the dumping pulse.

Electronic coupling through natural amino acids

DOE Office of Scientific and Technical Information (OSTI.GOV)

Berstis, Laura; Beckham, Gregg T., E-mail: michael.crowley@nrel.gov, E-mail: gregg.beckham@nrel.gov; Crowley, Michael F., E-mail: michael.crowley@nrel.gov, E-mail: gregg.beckham@nrel.gov

2015-12-14

Myriad scientific domains concern themselves with biological electron transfer (ET) events that span across vast scales of rate and efficiency through a remarkably fine-tuned integration of amino acid (AA) sequences, electronic structure, dynamics, and environment interactions. Within this intricate scheme, many questions persist as to how proteins modulate electron-tunneling properties. To help elucidate these principles, we develop a model set of peptides representing the common α-helix and β-strand motifs including all natural AAs within implicit protein-environment solvation. Using an effective Hamiltonian strategy with density functional theory, we characterize the electronic coupling through these peptides, furthermore considering side-chain dynamics. For bothmore » motifs, predictions consistently show that backbone-mediated electronic coupling is distinctly sensitive to AA type (aliphatic, polar, aromatic, negatively charged and positively charged), and to side-chain orientation. The unique properties of these residues may be employed to design activated, deactivated, or switch-like superexchange pathways. Electronic structure calculations and Green’s function analyses indicate that localized shifts in the electron density along the peptide play a role in modulating these pathways, and further substantiate the experimentally observed behavior of proline residues as superbridges. The distinct sensitivities of tunneling pathways to sequence and conformation revealed in this electronic coupling database help improve our fundamental understanding of the broad diversity of ET reactivity and provide guiding principles for peptide design.« less

Fourier transform infrared difference and time-resolved infrared detection of the electron and proton transfer dynamics in photosynthetic water oxidation.

PubMed

Noguchi, Takumi

2015-01-01

Photosynthetic water oxidation, which provides the electrons necessary for CO₂ reduction and releases O₂ and protons, is performed at the Mn₄CaO₅ cluster in photosystem II (PSII). In this review, studies that assessed the mechanism of water oxidation using infrared spectroscopy are summarized focusing on electron and proton transfer dynamics. Structural changes in proteins and water molecules between intermediates known as Si states (i=0-3) were detected using flash-induced Fourier transform infrared (FTIR) difference spectroscopy. Electron flow in PSII and proton release from substrate water were monitored using the infrared changes in ferricyanide as an exogenous electron acceptor and Mes buffer as a proton acceptor. Time-resolved infrared (TRIR) spectroscopy provided information on the dynamics of proton-coupled electron transfer during the S-state transitions. In particular, a drastic proton movement during the lag phase (~200μs) before electron transfer in the S3→S0 transition was detected directly by monitoring the infrared absorption of a polarizable proton in a hydrogen bond network. Furthermore, the proton release pathways in the PSII proteins were analyzed by FTIR difference measurements in combination with site-directed mutagenesis, isotopic substitutions, and quantum chemical calculations. Therefore, infrared spectroscopy is a powerful tool for understanding the molecular mechanism of photosynthetic water oxidation. This article is part of a Special Issue entitled: Vibrational spectroscopies and bioenergetic systems. Copyright © 2014 Elsevier B.V. All rights reserved.

Electronic Coupling Calculations for Bridge-Mediated Charge Transfer Using Constrained Density Functional Theory (CDFT) and Effective Hamiltonian Approaches at the Density Functional Theory (DFT) and Fragment-Orbital Density Functional Tight Binding (FODFTB) Level

DOE PAGES

Gillet, Natacha; Berstis, Laura; Wu, Xiaojing; ...

2016-09-09

In this paper, four methods to calculate charge transfer integrals in the context of bridge-mediated electron transfer are tested. These methods are based on density functional theory (DFT). We consider two perturbative Green's function effective Hamiltonian methods (first, at the DFT level of theory, using localized molecular orbitals; second, applying a tight-binding DFT approach, using fragment orbitals) and two constrained DFT implementations with either plane-wave or local basis sets. To assess the performance of the methods for through-bond (TB)-dominated or through-space (TS)-dominated transfer, different sets of molecules are considered. For through-bond electron transfer (ET), several molecules that were originally synthesizedmore » by Paddon-Row and co-workers for the deduction of electronic coupling values from photoemission and electron transmission spectroscopies, are analyzed. The tested methodologies prove to be successful in reproducing experimental data, the exponential distance decay constant and the superbridge effects arising from interference among ET pathways. For through-space ET, dedicated p-stacked systems with heterocyclopentadiene molecules were created and analyzed on the basis of electronic coupling dependence on donor-acceptor distance, structure of the bridge, and ET barrier height. The inexpensive fragment-orbital density functional tight binding (FODFTB) method gives similar results to constrained density functional theory (CDFT) and both reproduce the expected exponential decay of the coupling with donor-acceptor distances and the number of bridging units. Finally, these four approaches appear to give reliable results for both TB and TS ET and present a good alternative to expensive ab initio methodologies for large systems involving long-range charge transfers.« less

Electronic Coupling Calculations for Bridge-Mediated Charge Transfer Using Constrained Density Functional Theory (CDFT) and Effective Hamiltonian Approaches at the Density Functional Theory (DFT) and Fragment-Orbital Density Functional Tight Binding (FODFTB) Level

DOE Office of Scientific and Technical Information (OSTI.GOV)

Gillet, Natacha; Berstis, Laura; Wu, Xiaojing

In this paper, four methods to calculate charge transfer integrals in the context of bridge-mediated electron transfer are tested. These methods are based on density functional theory (DFT). We consider two perturbative Green's function effective Hamiltonian methods (first, at the DFT level of theory, using localized molecular orbitals; second, applying a tight-binding DFT approach, using fragment orbitals) and two constrained DFT implementations with either plane-wave or local basis sets. To assess the performance of the methods for through-bond (TB)-dominated or through-space (TS)-dominated transfer, different sets of molecules are considered. For through-bond electron transfer (ET), several molecules that were originally synthesizedmore » by Paddon-Row and co-workers for the deduction of electronic coupling values from photoemission and electron transmission spectroscopies, are analyzed. The tested methodologies prove to be successful in reproducing experimental data, the exponential distance decay constant and the superbridge effects arising from interference among ET pathways. For through-space ET, dedicated p-stacked systems with heterocyclopentadiene molecules were created and analyzed on the basis of electronic coupling dependence on donor-acceptor distance, structure of the bridge, and ET barrier height. The inexpensive fragment-orbital density functional tight binding (FODFTB) method gives similar results to constrained density functional theory (CDFT) and both reproduce the expected exponential decay of the coupling with donor-acceptor distances and the number of bridging units. Finally, these four approaches appear to give reliable results for both TB and TS ET and present a good alternative to expensive ab initio methodologies for large systems involving long-range charge transfers.« less

Ultrafast electron and energy transfer in dye-sensitized iron oxide and oxyhydroxide nanoparticles.

PubMed

Gilbert, Benjamin; Katz, Jordan E; Huse, Nils; Zhang, Xiaoyi; Frandsen, Cathrine; Falcone, Roger W; Waychunas, Glenn A

2013-10-28

An emerging area in chemical science is the study of solid-phase redox reactions using ultrafast time-resolved spectroscopy. We have used molecules of the photoactive dye 2',7'-dichlorofluorescein (DCF) anchored to the surface of iron(III) oxide nanoparticles to create iron(II) surface atoms via photo-initiated interfacial electron transfer. This approach enables time-resolved study of the fate and mobility of electrons within the solid phase. However, complete analysis of the ultrafast processes following dye photoexcitation of the sensitized iron(III) oxide nanoparticles has not been reported. We addressed this topic by performing femtosecond transient absorption (TA) measurements of aqueous suspensions of uncoated and DCF-sensitized iron oxide and oxyhydroxide nanoparticles, and an aqueous iron(III)-dye complex. Following light absorption, excited state relaxation times of the dye of 115-310 fs were found for all samples. Comparison between TA dynamics on uncoated and dye-sensitized hematite nanoparticles revealed the dye de-excitation pathway to consist of a competition between electron and energy transfer to the nanoparticles. We analyzed the TA data for hematite nanoparticles using a four-state model of the dye-sensitized system, finding electron and energy transfer to occur on the same ultrafast timescale. The interfacial electron transfer rates for iron oxides are very close to those previously reported for DCF-sensitized titanium dioxide (for which dye-oxide energy transfer is energetically forbidden) even though the acceptor states are different. Comparison of the alignment of the excited states of the dye and the unoccupied states of these oxides showed that the dye injects into acceptor states of different symmetry (Ti t2gvs. Fe eg).

Electronic Coupling Calculations for Bridge-Mediated Charge Transfer Using Constrained Density Functional Theory (CDFT) and Effective Hamiltonian Approaches at the Density Functional Theory (DFT) and Fragment-Orbital Density Functional Tight Binding (FODFTB) Level.

PubMed

Gillet, Natacha; Berstis, Laura; Wu, Xiaojing; Gajdos, Fruzsina; Heck, Alexander; de la Lande, Aurélien; Blumberger, Jochen; Elstner, Marcus

2016-10-11

In this article, four methods to calculate charge transfer integrals in the context of bridge-mediated electron transfer are tested. These methods are based on density functional theory (DFT). We consider two perturbative Green's function effective Hamiltonian methods (first, at the DFT level of theory, using localized molecular orbitals; second, applying a tight-binding DFT approach, using fragment orbitals) and two constrained DFT implementations with either plane-wave or local basis sets. To assess the performance of the methods for through-bond (TB)-dominated or through-space (TS)-dominated transfer, different sets of molecules are considered. For through-bond electron transfer (ET), several molecules that were originally synthesized by Paddon-Row and co-workers for the deduction of electronic coupling values from photoemission and electron transmission spectroscopies, are analyzed. The tested methodologies prove to be successful in reproducing experimental data, the exponential distance decay constant and the superbridge effects arising from interference among ET pathways. For through-space ET, dedicated π-stacked systems with heterocyclopentadiene molecules were created and analyzed on the basis of electronic coupling dependence on donor-acceptor distance, structure of the bridge, and ET barrier height. The inexpensive fragment-orbital density functional tight binding (FODFTB) method gives similar results to constrained density functional theory (CDFT) and both reproduce the expected exponential decay of the coupling with donor-acceptor distances and the number of bridging units. These four approaches appear to give reliable results for both TB and TS ET and present a good alternative to expensive ab initio methodologies for large systems involving long-range charge transfers.

Efficient photosensitized splitting of the thymine dimer/oxetane unit on its modifying beta-cyclodextrin by a binding electron donor.

PubMed

Tang, Wen-Jian; Song, Qin-Hua; Wang, Hong-Bo; Yu, Jing-Yu; Guo, Qing-Xiang

2006-07-07

Two modified beta-cyclodextrins (beta-CDs) with a thymine dimer and a thymine oxetane adduct respectively, TD-CD and Ox-CD, have been prepared, and utilized to bind an electron-rich chromophore, indole or N,N-dimethylaniline (DMA), to form a supramolecular complex. We have examined the photosensitized splitting of the dimer/oxetane unit in TD-CD/Ox-CD by indole or DMA via an electron-transfer pathway, and observed high splitting efficiencies of the dimer/oxetane unit. On the basis of measurements of fluorescence spectra and splitting quantum yields, it is suggested that the splitting reaction occurs in a supramolecular complex by an inclusion interaction between the modified beta-CDs and DMA or indole. The back electron transfer, which leads low splitting efficiencies for the covalently-linked chromophore-dimer/oxetane compounds, is suppressed in the non-covalently-bound complex, and the mechanism has been discussed.

Direct observation of multistep energy transfer in LHCII with fifth-order 3D electronic spectroscopy.

PubMed

Zhang, Zhengyang; Lambrev, Petar H; Wells, Kym L; Garab, Győző; Tan, Howe-Siang

2015-07-31

During photosynthesis, sunlight is efficiently captured by light-harvesting complexes, and the excitation energy is then funneled towards the reaction centre. These photosynthetic excitation energy transfer (EET) pathways are complex and proceed in a multistep fashion. Ultrafast two-dimensional electronic spectroscopy (2DES) is an important tool to study EET processes in photosynthetic complexes. However, the multistep EET processes can only be indirectly inferred by correlating different cross peaks from a series of 2DES spectra. Here we directly observe multistep EET processes in LHCII using ultrafast fifth-order three-dimensional electronic spectroscopy (3DES). We measure cross peaks in 3DES spectra of LHCII that directly indicate energy transfer from excitons in the chlorophyll b (Chl b) manifold to the low-energy level chlorophyll a (Chl a) via mid-level Chl a energy states. This new spectroscopic technique allows scientists to move a step towards mapping the complete complex EET processes in photosynthetic systems.

Communication: Probing non-equilibrium vibrational relaxation pathways of highly excited C≡N stretching modes following ultrafast back-electron transfer.

PubMed

Lynch, Michael S; Slenkamp, Karla M; Khalil, Munira

2012-06-28

Fifth-order nonlinear visible-infrared spectroscopy is used to probe coherent and incoherent vibrational energy relaxation dynamics of highly excited vibrational modes indirectly populated via ultrafast photoinduced back-electron transfer in a trinuclear cyano-bridged mixed-valence complex. The flow of excess energy deposited into four C≡N stretching (ν(CN)) modes of the molecule is monitored by performing an IR pump-probe experiment as a function of the photochemical reaction (τ(vis)). Our results provide experimental evidence that the nuclear motions of the molecule are both coherently and incoherently coupled to the electronic charge transfer process. We observe that intramolecular vibrational relaxation dynamics among the highly excited ν(CN) modes change significantly en route to equilibrium. The experiment also measures a 7 cm(-1) shift in the frequency of a ∼57 cm(-1) oscillation reflecting a modulation of the coupling between the probed high-frequency ν(CN) modes for τ(vis) < 500 fs.

Construction and direct electrochemistry of orientation controlled laccase electrode.

PubMed

Li, Ying; Zhang, Jiwei; Huang, Xirong; Wang, Tianhong

2014-03-28

A laccase has multiple redox centres. Chemisorption of laccases on a gold electrode through a polypeptide tag introduced at the protein surface provides an isotropic orientation of laccases on the Au surface, which allows the orientation dependent study of the direct electrochemistry of laccase. In this paper, using genetic engineering technology, two forms of recombinant laccase which has Cys-6×His tag at the N or C terminus were generated. Via the Au-S linkage, the recombinant laccase was assembled orientationally on gold electrode. A direct electron transfer and a bioelectrocatalytic activity toward oxygen reduction were observed on the two orientation controlled laccase electrodes, but their electrochemical behaviors were found to be quite different. The orientation of laccase on the gold electrode affects both the electron transfer pathway and the electron transfer efficiency of O2 reduction. The present study is helpful not only to the in-depth understanding of the direct electrochemistry of laccase, but also to the development of laccase-based biofuel cells. Copyright © 2014 Elsevier Inc. All rights reserved.

Cross-benzoin and Stetter-type reactions mediated by KOtBu-DMF via an electron-transfer process.

PubMed

Ragno, Daniele; Zaghi, Anna; Di Carmine, Graziano; Giovannini, Pier Paolo; Bortolini, Olga; Fogagnolo, Marco; Molinari, Alessandra; Venturini, Alessandro; Massi, Alessandro

2016-10-18

The condensation of aromatic α-diketones (benzils) with aromatic aldehydes (benzoin-type reaction) and chalcones (Stetter-type reaction) in DMF in the presence of catalytic (25 mol%) KOtBu is reported. Both types of umpolung processes proceed with good efficiency and complete chemoselectivity. On the basis of spectroscopic evidence (MS analysis) of plausible intermediates and literature reports, the occurrence of different ionic pathways have been evaluated to elucidate the mechanism of a model cross-benzoin-like reaction along with a radical route initiated by an electron-transfer process to benzil from the carbamoyl anion derived from DMF. This mechanistic investigation has culminated in a different proposal, supported by calculations and a trapping experiment, based on double electron-transfer to benzil with formation of the corresponding enediolate anion as the key reactive intermediate. A mechanistic comparison between the activation modes of benzils in KOtBu-DMF and KOtBu-DMSO systems is also described.

Electron transfer and reaction mechanism of laccases.

PubMed

Jones, Stephen M; Solomon, Edward I

2015-03-01

Laccases are part of the family of multicopper oxidases (MCOs), which couple the oxidation of substrates to the four electron reduction of O2 to H2O. MCOs contain a minimum of four Cu's divided into Type 1 (T1), Type 2 (T2), and binuclear Type 3 (T3) Cu sites that are distinguished based on unique spectroscopic features. Substrate oxidation occurs near the T1, and electrons are transferred approximately 13 Å through the protein via the Cys-His pathway to the T2/T3 trinuclear copper cluster (TNC), where dioxygen reduction occurs. This review outlines the electron transfer (ET) process in laccases, and the mechanism of O2 reduction as elucidated through spectroscopic, kinetic, and computational data. Marcus theory is used to describe the relevant factors which impact ET rates including the driving force, reorganization energy, and electronic coupling matrix element. Then, the mechanism of O2 reaction is detailed with particular focus on the intermediates formed during the two 2e(-) reduction steps. The first 2e(-) step forms the peroxide intermediate, followed by the second 2e(-) step to form the native intermediate, which has been shown to be the catalytically relevant fully oxidized form of the enzyme.

Cascading electron and hole transfer dynamics in a CdS/CdTe core-shell sensitized with bromo-pyrogallol red (Br-PGR): slow charge recombination in type II regime.

PubMed

Maity, Partha; Debnath, Tushar; Chopra, Uday; Ghosh, Hirendra Nath

2015-02-14

Ultrafast cascading hole and electron transfer dynamics have been demonstrated in a CdS/CdTe type II core-shell sensitized with Br-PGR using transient absorption spectroscopy and the charge recombination dynamics have been compared with those of CdS/Br-PGR composite materials. Steady state optical absorption studies suggest that Br-PGR forms strong charge transfer (CT) complexes with both the CdS QD and CdS/CdTe core-shell. Hole transfer from the photo-excited QD and QD core-shell to Br-PGR was confirmed by both steady state and time-resolved emission spectroscopy. Charge separation was also confirmed by detecting electrons in the conduction band of the QD and the cation radical of Br-PGR as measured from femtosecond transient absorption spectroscopy. Charge separation in the CdS/Br-PGR composite materials was found to take place in three different pathways, by transferring the photo-excited hole of CdS to Br-PGR, electron injection from the photo-excited Br-PGR to the CdS QD, and direct electron transfer from the HOMO of Br-PGR to the conduction band of the CdS QD. However, in the CdS/CdTe/Br-PGR system hole transfer from the photo-excited CdS to Br-PGR and electron injection from the photo-excited Br-PGR to CdS take place after cascading through the CdTe shell QD. Charge separation also takes place via direct electron transfer from the Br-PGR HOMO to the conduction band of CdS/CdTe. Charge recombination (CR) dynamics between the electron in the conduction band of the CdS QD and the Br-PGR cation radical were determined by monitoring the bleach recovery kinetics. The CR dynamics were found to be much slower in the CdS/CdTe/Br-PGR system than in the CdS/Br-PGR system. The formation of the strong CT complex and the separation of charges cascading through the CdTe shell help to slow down charge recombination in the type II regime.

Reverse Methanogenesis and Respiration in Methanotrophic Archaea

PubMed Central

Koehorst, Jasper J.; Jetten, Mike S. M.; Stams, Alfons J. M.

2017-01-01

Anaerobic oxidation of methane (AOM) is catalyzed by anaerobic methane-oxidizing archaea (ANME) via a reverse and modified methanogenesis pathway. Methanogens can also reverse the methanogenesis pathway to oxidize methane, but only during net methane production (i.e., “trace methane oxidation”). In turn, ANME can produce methane, but only during net methane oxidation (i.e., enzymatic back flux). Net AOM is exergonic when coupled to an external electron acceptor such as sulfate (ANME-1, ANME-2abc, and ANME-3), nitrate (ANME-2d), or metal (oxides). In this review, the reversibility of the methanogenesis pathway and essential differences between ANME and methanogens are described by combining published information with domain based (meta)genome comparison of archaeal methanotrophs and selected archaea. These differences include abundances and special structure of methyl coenzyme M reductase and of multiheme cytochromes and the presence of menaquinones or methanophenazines. ANME-2a and ANME-2d can use electron acceptors other than sulfate or nitrate for AOM, respectively. Environmental studies suggest that ANME-2d are also involved in sulfate-dependent AOM. ANME-1 seem to use a different mechanism for disposal of electrons and possibly are less versatile in electron acceptors use than ANME-2. Future research will shed light on the molecular basis of reversal of the methanogenic pathway and electron transfer in different ANME types. PMID:28154498

Gas sensors boosted by two-dimensional h-BN enabled transfer on thin substrate foils: towards wearable and portable applications.

PubMed

Ayari, Taha; Bishop, Chris; Jordan, Matthew B; Sundaram, Suresh; Li, Xin; Alam, Saiful; ElGmili, Youssef; Patriarche, Gilles; Voss, Paul L; Salvestrini, Jean Paul; Ougazzaden, Abdallah

2017-11-09

The transfer of GaN based gas sensors to foreign substrates provides a pathway to enhance sensor performance, lower the cost and extend the applications to wearable, mobile or disposable systems. The main keys to unlocking this pathway is to grow and fabricate the sensors on large h-BN surface and to transfer them to the flexible substrate without any degradation of the performances. In this work, we develop a new generation of AlGaN/GaN gas sensors with boosted performances on a low cost flexible substrate. We fabricate 2-inch wafer scale AlGaN/GaN gas sensors on sacrificial two-dimensional (2D) nano-layered h-BN without any delamination or cracks and subsequently transfer sensors to an acrylic surface on metallic foil. This technique results in a modification of relevant device properties, leading to a doubling of the sensitivity to NO 2 gas and a response time that is more than 6 times faster than before transfer. This new approach for GaN-based sensor design opens new avenues for sensor improvement via transfer to more suitable substrates, and is promising for next-generation wearable and portable opto-electronic devices.

Reduction of low potential electron acceptors requires the CbcL inner membrane cytochrome of Geobacter sulfurreducens

DOE Office of Scientific and Technical Information (OSTI.GOV)

Zacharoff, Lori; Chan, Chi Ho; Bond, Daniel R.

2015-09-05

The respiration of metals by the bacterium Geobacter sulfurreducens requires electrons generated by metabolism to pass from the interior of the cell to electron acceptors beyond the cell membranes. The G. sulfurreducens inner membrane multiheme c-type cytochrome ImcH is required for respiration to extracellular electron acceptors with redox potentials greater than - 0.1 V vs. SHE, but ImcH is not essential for electron transfer to lower potential acceptors. In contrast, deletion of cbcL, encoding an inner membrane protein consisting of b-type and multiheme c-type cytochrome domains, severely affected reduction of low potential electron acceptors such as Fe(III)-oxides and electrodes poisedmore » at - 0.1 V vs. SHE. Catalytic cyclic voltammetry of a ΔcbcL strain growing on poised electrodes revealed a 50 mV positive shift in driving force required for electron transfer out of the cell. In non-catalytic conditions, low-potential peaks present in wild type biofilms were absent in ΔcbcL mutants. Expression of cbcL in trans increased growth at low redox potential and restored features to cyclic voltammetry. This evidence supports a model where CbcL is a component of a second electron transfer pathway out of the G. sulfurreducens inner membrane that dominates when redox potential is at or below - 0.1 V vs. SHE.« less

Reduction of low potential electron acceptors requires the CbcL inner membrane cytochrome of Geobacter sulfurreducens.

PubMed

Zacharoff, Lori; Chan, Chi Ho; Bond, Daniel R

2016-02-01

The respiration of metals by the bacterium Geobacter sulfurreducens requires electrons generated by metabolism to pass from the interior of the cell to electron acceptors beyond the cell membranes. The G. sulfurreducens inner membrane multiheme c-type cytochrome ImcH is required for respiration to extracellular electron acceptors with redox potentials greater than -0.1 V vs. SHE, but ImcH is not essential for electron transfer to lower potential acceptors. In contrast, deletion of cbcL, encoding an inner membrane protein consisting of b-type and multiheme c-type cytochrome domains, severely affected reduction of low potential electron acceptors such as Fe(III)-oxides and electrodes poised at -0.1 V vs. SHE. Catalytic cyclic voltammetry of a ΔcbcL strain growing on poised electrodes revealed a 50 mV positive shift in driving force required for electron transfer out of the cell. In non-catalytic conditions, low-potential peaks present in wild type biofilms were absent in ∆cbcL mutants. Expression of cbcL in trans increased growth at low redox potential and restored features to cyclic voltammetry. This evidence supports a model where CbcL is a component of a second electron transfer pathway out of the G. sulfurreducens inner membrane that dominates when redox potential is at or below -0.1 V vs. SHE. Copyright © 2015. Published by Elsevier B.V.

The mitochondrial electron transfer flavoprotein complex is essential for survival of Arabidopsis in extended darkness.

PubMed

Ishizaki, Kimitsune; Schauer, Nicolas; Larson, Tony R; Graham, Ian A; Fernie, Alisdair R; Leaver, Christopher J

2006-09-01

In mammals, the electron transfer flavoprotein (ETF) is a heterodimeric protein composed of two subunits, alpha and beta, that is responsible for the oxidation of at least nine mitochondrial matrix flavoprotein dehydrogenases. Electrons accepted by ETF are further transferred to the main respiratory chain via the ETF ubiquinone oxide reductase (ETFQO). Sequence analysis of the unique Arabidopsis homologues of two subunits of ETF revealed their high similarity to both subunits of the mammalian ETF. Yeast two-hybrid experiments showed that the Arabidopsis ETFalpha and ETFbeta can form a heteromeric protein. Isolation and characterization of two independent T-DNA insertional Arabidopsis mutants of the ETFbeta gene revealed accelerated senescence and early death compared to wild-type during extended darkness. Furthermore in contrast to wild-type, the etfb mutants demonstrated a significant accumulation of several amino acids, isovaleryl CoA and phytanoyl CoA during dark-induced carbohydrate deprivation. These phenotypic characteristics of etfb mutants are broadly similar to those that we observed previously in Arabidopsis etfqo mutants, suggesting functional association between ETF and ETFQO in Arabidopsis, and confirming the essential roles of the ETF/ETFQO electron transfer complex in the catabolism of leucine and involvement in the chlorophyll degradation pathway activated during dark-induced carbohydrate deprivation.

The Role of Electronic Excitations on Chemical Reaction Dynamics at Metal, Semiconductor and Nanoparticle Surfaces

DOE Office of Scientific and Technical Information (OSTI.GOV)

Tully, John C.

Chemical reactions are often facilitated and steered when carried out on solid surfaces, essential for applications such as heterogeneous catalysis, solar energy conversion, corrosion, materials processing, and many others. A critical factor that can determine the rates and pathways of chemical reactions at surfaces is the efficiency and specificity of energy transfer; how fast does energy move around and where does it go? For reactions on insulator surfaces energy transfer generally moves in and out of vibrations of the adsorbed molecule and the underlying substrate. By contrast, on metal surfaces, metallic nanoparticles and semiconductors, another pathway for energy flow opensmore » up, excitation and de-excitation of electrons. This so-called “nonadiabatic” mechanism often dominates the transfer of energy and can directly impact the course of a chemical reaction. Conventional computational methods such as molecular dynamics simulation do not account for this nonadiabatic behavior. The current DOE-BES funded project has focused on developing the underlying theoretical foundation and the computational methodology for the prediction of nonadiabatic chemical reaction dynamics at surfaces. The research has successfully opened up new methodology and new applications for molecular simulation. In particular, over the last three years, the “Electronic Friction” theory, pioneered by the PI, has now been developed into a stable and accurate computational method that is sufficiently practical to allow first principles “on-the-fly” simulation of chemical reaction dynamics at metal surfaces.« less

Observation of Electronic Excitation Transfer Through Light Harvesting Complex II Using Two-Dimensional Electronic-Vibrational Spectroscopy

DOE Office of Scientific and Technical Information (OSTI.GOV)

Lewis, Nicholas H. C.; Gruenke, Natalie L.; Oliver, Thomas A. A.

Light-harvesting complex II (LHCII) serves a central role in light harvesting for oxygenic photosynthesis and is arguably the most important photosynthetic antenna complex. In this article, we present two-dimensional electronic–vibrational (2DEV) spectra of LHCII isolated from spinach, demonstrating the possibility of using this technique to track the transfer of electronic excitation energy between specific pigments within the complex. We assign the spectral bands via comparison with the 2DEV spectra of the isolated chromophores, chlorophyll a and b, and present evidence that excitation energy between the pigments of the complex are observed in these spectra. Lastly, we analyze the essential componentsmore » of the 2DEV spectra using singular value decomposition, which makes it possible to reveal the relaxation pathways within this complex.« less

High-performance blue phosphorescent OLEDs using energy transfer from exciplex.

PubMed

Seino, Yuki; Sasabe, Hisahiro; Pu, Yong-Jin; Kido, Junji

2014-03-12

An efficient energy transfer from an exciplex between a sulfone and an arylamine derivatives to a blue phosphorescent emitter enables OLED performances among the best, of over 50 lm W(-1) at 100 cd m(-2) . The formation of the exciplex realizes a barrier-free hole-electron recombination pathway, thereby leading to high OLED performances with an extremely low driving voltage of 2.9 V at 100 cd m(-2) . © 2014 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

Rational construction of multiple interfaces in ternary heterostructure for efficient spatial separation and transfer of photogenerated carriers in the application of photocatalytic hydrogen evolution

NASA Astrophysics Data System (ADS)

Shi, Jian-Wen; Ma, Dandan; Zou, Yajun; Fan, Zhaoyang; Shi, Jinwen; Cheng, Linhao; Ji, Xin; Niu, Chunming

2018-03-01

The design of efficient and stable photocatalyst plays a critical role in the photocatalytic hydrogen evolution from water splitting. Herein, we develop a novel ZnS/CdS/ZnO ternary heterostructure by the in-situ sulfuration of CdS/ZnO, which includes four contact interfaces: CdS-ZnS interface, ZnS-ZnO interface, CdS-ZnO interface and ZnS-CdS-ZnO ternary interface, forming three charge carrier-transfer modes (type-I, type-II and direct Z-scheme) through five carrier-transfer pathways. As a result, the separation and transfer of photoexcited electron-hole pairs are promoted significantly, resulting in a high hydrogen evolution rate of 44.70 mmol h-1 g-1, which is 2, 3.7 and 8 times higher than those of binary heterostructures, CdS/ZnO, CdS/ZnS and ZnS/ZnO, respectively, and 26.5, 280 and 298 times higher than those of single CdS, ZnO and ZnS, respectively. As a counterpart ternary heterostructure, CdS/ZnS/ZnO contains only two interfaces: CdS-ZnS interface and ZnS-ZnO interface, which form two charge carrier-transfer modes (type-I and type-II) through two carrier-transfer pathways, leading to its much lower hydrogen evolution rate (27.25 mmol h-1 g-1) than ZnS/CdS/ZnO ternary heterostructure. This work is relevant for understanding the charge-transfer pathways between multi-interfaces in multicomponent heterojunctions.

Facet-dependent solar ammonia synthesis of BiOCl nanosheets via a proton-assisted electron transfer pathway

NASA Astrophysics Data System (ADS)

Li, Hao; Shang, Jian; Shi, Jingu; Zhao, Kun; Zhang, Lizhi

2016-01-01

Under the pressure of a fossil fuels shortage and global climate change, solar ammonia synthesis and the need to develop N2 fixation under mild conditions is becoming more urgent need; however, their intrinsic mechanisms still remain unclear. Herein, we demonstrate that the kinetic inertia of N2 can be overcome using oxygen vacancies (OVs) of BiOCl as the catalytic centers to create lower energy molecular steps, which are amendable for the solar light driven N-N triple bond cleavage via a proton-assisted electron transfer pathway. Moreover, the distinct structures of OVs on different BiOCl facets strongly determine the N2 fixation pathways by influencing both the adsorption structure and the activation level of N2. The fixation of terminal end-on bound N2 on the OVs of BiOCl {001} facets follows an asymmetric distal mode by selectively generating NH3, while the reduction of side-on bridging N2 on the OVs of BiOCl {010} facets is more energetically favorable in a symmetric alternating mode to produce N2H4 as the main intermediate.Under the pressure of a fossil fuels shortage and global climate change, solar ammonia synthesis and the need to develop N2 fixation under mild conditions is becoming more urgent need; however, their intrinsic mechanisms still remain unclear. Herein, we demonstrate that the kinetic inertia of N2 can be overcome using oxygen vacancies (OVs) of BiOCl as the catalytic centers to create lower energy molecular steps, which are amendable for the solar light driven N-N triple bond cleavage via a proton-assisted electron transfer pathway. Moreover, the distinct structures of OVs on different BiOCl facets strongly determine the N2 fixation pathways by influencing both the adsorption structure and the activation level of N2. The fixation of terminal end-on bound N2 on the OVs of BiOCl {001} facets follows an asymmetric distal mode by selectively generating NH3, while the reduction of side-on bridging N2 on the OVs of BiOCl {010} facets is more energetically favorable in a symmetric alternating mode to produce N2H4 as the main intermediate. Electronic supplementary information (ESI) available: Other experimental details, additional SEM and TEM images, X-ray diffraction patterns (XRD), UV-Vis diffuse reflectance spectra (DRS), and additional data. See DOI: 10.1039/c5nr07380d

Enhanced dark hydrogen fermentation by addition of ferric oxide nanoparticles using Enterobacter aerogenes.

PubMed

Lin, Richen; Cheng, Jun; Ding, Lingkan; Song, Wenlu; Liu, Min; Zhou, Junhu; Cen, Kefa

2016-05-01

Ferric oxide nanoparticles (FONPs) were used to facilitate dark hydrogen fermentation using Enterobacter aerogenes. The hydrogen yield of glucose increased from 164.5±2.29 to 192.4±1.14mL/g when FONPs concentration increased from 0 to 200mg/L. SEM images of E. aerogenes demonstrated the existence of bacterial nanowire among cells, suggesting FONPs served as electron conduits to enhance electron transfer. TEM showed cellular internalization of FONPs, indicating hydrogenase synthesis and activity was potentially promoted due to the released iron element. When further increasing FONPs concentration to 400mg/L, the hydrogen yield of glucose decreased to 147.2±2.54mL/g. Soluble metabolic products revealed FONPs enhanced acetate pathway of hydrogen production, but weakened ethanol pathway. This shift of metabolic pathways allowed more nicotinamide adenine dinucleotide for reducing proton to hydrogen. Copyright © 2016 Elsevier Ltd. All rights reserved.

Acid proliferation to improve the sensitivity of EUV resists: a pulse radiolysis study

NASA Astrophysics Data System (ADS)

Enomoto, Kazuyuki; Arimitsu, Koji; Yoshizawa, Atsutaro; Yamamoto, Hiroki; Oshima, Akihiro; Kozawa, Takahiro; Tagawa, Seiichi

2011-04-01

The yields of acid have been measured in the electron-beam irradiation of triphenylsulfonium triflate (TPS-Tf) and pinanediol monosulfonates, which consist of tosylate (PiTs), 4-fluorobenzenesulfonate (Pi1F), or 4-trifluoromethylbenzenesulfonate (Pi3F), as an acid amplifier blended in 4-hydroxystyrene matrixes. The acid yields efficiency decreases when PiTs is present, while its efficiency increases in the presence of Pi3F. Reactions of the electrons with TPS-Tf and pinanediol monosulfonates have been studied using pulse radiolysis in liquid tetrahydrofuran (THF) to evaluate the kinetic contributions to acid production. The THF-solvated electrons react with PiTs, Pi1F, and Pi3F to produce the corresponding radical anions; the rate constants are estimated to be 4.1, 5.1, and 9.2 × 1010 M-1 s-1, respectively. Electron transfer from PiTs•-, Pi1F•-, and Pi3F•- radical anions to TPS-Tf occurs with the rate constants of 5.7×1010, 1.2×1011, and 6.3 × 1010 M-1 s-1, respectively. The long-lived Pi3F•- efficiently undergoes the electron transfer to TPS-Tf to form the TPS-Tf•-, which subsequently decompose to generate TfOH. On the other hand, the decay channels of PiTs•- and Pi1F•-, which possess a relatively short lifetime, are presumably dependent on its reactions with solvated protons (charge recombination) rather than the electron transfer to TPS-Tf. The novel acid production pathway via the electron transfer from pinanediol monosulfonate radical anions to TPS-Tf is presented.

Influence of Proton Acceptors on the Proton-Coupled Electron Transfer Reaction Kinetics of a Ruthenium-Tyrosine Complex.

PubMed

Lennox, J Christian; Dempsey, Jillian L

2017-11-22

A polypyridyl ruthenium complex with fluorinated bipyridine ligands and a covalently bound tyrosine moiety was synthesized, and its photo-induced proton-coupled electron transfer (PCET) reactivity in acetonitrile was investigated with transient absorption spectroscopy. Using flash-quench methodology with methyl viologen as an oxidative quencher, a Ru 3+ species is generated that is capable of initiating the intramolecular PCET oxidation of the tyrosine moiety. Using a series of substituted pyridine bases, the reaction kinetics were found to vary as a function of proton acceptor concentration and identity, with no significant H/D kinetic isotope effect. Through analysis of the kinetics traces and comparison to a control complex without the tyrosine moiety, PCET reactivity was found to proceed through an equilibrium electron transfer followed by proton transfer (ET-PT) pathway in which irreversible deprotonation of the tyrosine radical cation shifts the ET equilibrium, conferring a base dependence on the reaction. Comprehensive kinetics modeling allowed for deconvolution of complex kinetics and determination of rate constants for each elementary step. Across the five pyridine bases explored, spanning a range of 4.2 pK a units, a linear free-energy relationship was found for the proton transfer rate constant with a slope of 0.32. These findings highlight the influence that proton transfer driving force exerts on PCET reaction kinetics.

A pathway for protons in nitric oxide reductase from Paracoccus denitrificans.

PubMed

Reimann, Joachim; Flock, Ulrika; Lepp, Håkan; Honigmann, Alf; Adelroth, Pia

2007-05-01

Nitric oxide reductase (NOR) from P. denitrificans is a membrane-bound protein complex that catalyses the reduction of NO to N(2)O (2NO+2e(-)+2H(+)-->N(2)O+H(2)O) as part of the denitrification process. Even though NO reduction is a highly exergonic reaction, and NOR belongs to the superfamily of O(2)-reducing, proton-pumping heme-copper oxidases (HCuOs), previous measurements have indicated that the reaction catalyzed by NOR is non-electrogenic, i.e. not contributing to the proton electrochemical gradient. Since electrons are provided by donors in the periplasm, this non-electrogenicity implies that the substrate protons are also taken up from the periplasm. Here, using direct measurements in liposome-reconstituted NOR during reduction of both NO and the alternative substrate O(2), we demonstrate that protons are indeed consumed from the 'outside'. First, multiple turnover reduction of O(2) resulted in an increase in pH on the outside of the NOR-vesicles. Second, comparison of electrical potential generation in NOR-liposomes during oxidation of the reduced enzyme by either NO or O(2) shows that the proton transfer signals are very similar for the two substrates proving the usefulness of O(2) as a model substrate for these studies. Last, optical measurements during single-turnover oxidation by O(2) show electron transfer coupled to proton uptake from outside the NOR-liposomes with a tau=15 ms, similar to results obtained for net proton uptake in solubilised NOR [U. Flock, N.J. Watmough, P. Adelroth, Electron/proton coupling in bacterial nitric oxide reductase during reduction of oxygen, Biochemistry 44 (2005) 10711-10719]. NOR must thus contain a proton transfer pathway leading from the periplasmic surface into the active site. Using homology modeling with the structures of HCuOs as templates, we constructed a 3D model of the NorB catalytic subunit from P. denitrificans in order to search for such a pathway. A plausible pathway, consisting of conserved protonatable residues, is suggested.

Influence of Sulfate-Reducing Bacteria on the Corrosion Behavior of High Strength Steel EQ70 under Cathodic Polarization

PubMed Central

Guan, Fang; Zhai, Xiaofan; Duan, Jizhou; Zhang, Meixia; Hou, Baorong

2016-01-01

Certain species of sulfate-reducing bacteria (SRB) use cathodes as electron donors for metabolism, and this electron transfer process may influence the proper protection potential choice for structures. The interaction between SRB and polarized electrodes had been the focus of numerous investigations. In this paper, the impact of cathodic protection (CP) on Desulfovibrio caledoniens metabolic activity and its influence on highs trength steel EQ70 were studied by bacterial analyses and electrochemical measurements. The results showed that EQ70 under -0.85 VSCE CP had a higher corrosion rate than that without CP, while EQ70 with -1.05 VSCE had a lower corrosion rate. The enhanced SRB metabolic activity at -0.85 VSCE was most probably caused by the direct electron transfer from the electrode polarized at -0.85 VSCE. This direct electron transfer pathway was unavailable in -1.05 VSCE. In addition, the application of cathodic protection led to the transformation of sulfide rusts into carbonates rusts. These observations have been employed to provide updated recommendations for the optimum CP potential for steel structures in the presence of SRB. PMID:27603928

Molecular alignment effect on the photoassociation process via a pump-dump scheme

DOE Office of Scientific and Technical Information (OSTI.GOV)

Wang, Bin-Bin; Han, Yong-Chang, E-mail: ychan@dlut.edu.cn; Cong, Shu-Lin

The photoassociation processes via the pump-dump scheme for the heternuclear (Na + H → NaH) and the homonuclear (Na + Na → Na{sub 2}) molecular systems are studied, respectively, using the time-dependent quantum wavepacket method. For both systems, the initial atom pair in the continuum of the ground electronic state (X{sup 1}Σ{sup +}) is associated into the molecule in the bound states of the excited state (A{sup 1}Σ{sup +}) by the pump pulse. Then driven by a time-delayed dumping pulse, the prepared excited-state molecule can be transferred to the bound states of the ground electronic state. It is found thatmore » the pump process can induce a superposition of the rovibrational levels |v, j〉 on the excited state, which can lead to the field-free alignment of the excited-state molecule. The molecular alignment can affect the dumping process by varying the effective coupling intensity between the two electronic states or by varying the population transfer pathways. As a result, the final population transferred to the bound states of the ground electronic state varies periodically with the delay time of the dumping pulse.« less

Modeling donor/acceptor interactions: Combined roles of theory and computation

DOE Office of Scientific and Technical Information (OSTI.GOV)

Newton, M.D.

2000-03-05

An extended superexchange model for electron transfer (ET) matrix elements (H{sub DA}) has been formulated as a superposition of McConnell-type pathways and implemented by combined use of configuration interaction wave functions (obtained using the INDO/s model of Zerner and co-workers) and the generalized Muliken-Hush formulation of charge-localized diabatic states. Applications are made for et (and hold transfer) in several donor/bridge/acceptor radical anion (and cation) systems, (DBA){sup {+-}}, allowing detailed comparison with experimental H{sub DA} estimates. For the case of oligo phenylene ethynylene (OPE) bridges, the role of {pi} and {sigma} electronic manifolds for different distributions of phenylene torsion angles ismore » analyzed in detail.« less

Biochemistry of Catabolic Reductive Dehalogenation.

PubMed

Fincker, Maeva; Spormann, Alfred M

2017-06-20

A wide range of phylogenetically diverse microorganisms couple the reductive dehalogenation of organohalides to energy conservation. Key enzymes of such anaerobic catabolic pathways are corrinoid and Fe-S cluster-containing, membrane-associated reductive dehalogenases. These enzymes catalyze the reductive elimination of a halide and constitute the terminal reductases of a short electron transfer chain. Enzymatic and physiological studies revealed the existence of quinone-dependent and quinone-independent reductive dehalogenases that are distinguishable at the amino acid sequence level, implying different modes of energy conservation in the respective microorganisms. In this review, we summarize current knowledge about catabolic reductive dehalogenases and the electron transfer chain they are part of. We review reaction mechanisms and the role of the corrinoid and Fe-S cluster cofactors and discuss physiological implications.

A study of information management in the patient surgical pathway in NHSScotland.

PubMed

Bouamrane, Matt-Mouley; Mair, Frances S

2013-01-01

We conducted a study of information management processes across the patient surgical pathway in NHSScotland. While the majority of general practitioners (GPs) consider electronic medical records systems as an essential and integral part of their work during the patient consultation, many were not fully satisfied with the functionalities of these systems. A majority of GPs considered that the national eReferral system streamlined referral processes. Almost all GPs reported marked variability in the quality of discharge information. Preoperative processes vary significantly across Scotland, with most services using paper-based systems. Insufficient use is made of information provided through the patient electronic referral leading to a considerable duplication of tasks already performed in primary care. Three health-boards have implemented electronic preoperative information systems. These have transformed clinical practices and facilitated communication and information-sharing among the multi-disciplinary team and within the health-boards. Substantial progress has been made towards improving information transfer and sharing within the surgical pathway in recent years. However, there remains scope for further improvements at the interface between services.

Quinone reduction via secondary B-branch electron transfer in mutant bacterial reaction centers.

PubMed

Laible, Philip D; Kirmaier, Christine; Udawatte, Chandani S M; Hofman, Samuel J; Holten, Dewey; Hanson, Deborah K

2003-02-18

Symmetry-related branches of electron-transfer cofactors-initiating with a primary electron donor (P) and terminating in quinone acceptors (Q)-are common features of photosynthetic reaction centers (RC). Experimental observations show activity of only one of them-the A branch-in wild-type bacterial RCs. In a mutant RC, we now demonstrate that electron transfer can occur along the entire, normally inactive B-branch pathway to reduce the terminal acceptor Q(B) on the time scale of nanoseconds. The transmembrane charge-separated state P(+)Q(B)(-) is created in this manner in a Rhodobacter capsulatus RC containing the F(L181)Y-Y(M208)F-L(M212)H-W(M250)V mutations (YFHV). The W(M250)V mutation quantitatively blocks binding of Q(A), thereby eliminating Q(B) reduction via the normal A-branch pathway. Full occupancy of the Q(B) site by the native UQ(10) is ensured (without the necessity of reconstitution by exogenous quinone) by purification of RCs with the mild detergent, Deriphat 160-C. The lifetime of P(+)Q(B)(-) in the YFHV mutant RC is >6 s (at pH 8.0, 298 K). This charge-separated state is not formed upon addition of competitive inhibitors of Q(B) binding (terbutryn or stigmatellin). Furthermore, this lifetime is much longer than the value of approximately 1-1.5 s found when P(+)Q(B)(-) is produced in the wild-type RC by A-side activity alone. Collectively, these results demonstrate that P(+)Q(B)(-) is formed solely by activity of the B-branch carriers in the YFHV RC. In comparison, P(+)Q(B)(-) can form by either the A or B branches in the YFH RC, as indicated by the biexponential lifetimes of approximately 1 and approximately 6-10 s. These findings suggest that P(+)Q(B)(-) states formed via the two branches are distinct and that P(+)Q(B)(-) formed by the B side does not decay via the normal (indirect) pathway that utilizes the A-side cofactors when present. These differences may report on structural and energetic factors that further distinguish the functional asymmetry of the two cofactor branches.

Heterocyclic Schiff bases as non toxic antioxidants: Solvent effect, structure activity relationship and mechanism of action

NASA Astrophysics Data System (ADS)

Shanty, Angamaly Antony; Mohanan, Puzhavoorparambil Velayudhan

2018-03-01

Phenolic heterocyclic imine based Schiff bases from Thiophene-2-carboxaldehyde and Pyrrole-2-carboxaldehyde were synthesized and characterized as novel antioxidants. The solvent effects of these Schiff bases were determined and compared with standard antioxidants, BHA employing DPPH assay and ABTS assay. Fixed reaction time and Steady state measurement were used for study. IC50 and EC50 were calculated. Structure-activity relationship revealed that the electron donating group in the phenolic ring increases the activity where as the electron withdrawing moiety decreases the activity. The Schiff base derivatives showed antioxidant property by two different pathways namely SPLET and HAT mechanisms in DPPH assay. While in ABTS method, the reaction between ABTS radical and Schiff bases involves electron transfer followed by proton transfer (ET-PT) mechanism. The cytotoxicity of these compounds has been evaluated by MTT assay. The results showed that all these compounds are non toxic in nature.

Dissociation of protonated N-(3-phenyl-2H-chromen-2-ylidene)-benzenesulfonamide in the gas phase: cyclization via sulfonyl cation transfer.

PubMed

Wang, Shanshan; Dong, Cheng; Yu, Lian; Guo, Cheng; Jiang, Kezhi

2016-01-15

In the tandem mass spectrometry of protonated N-(3-phenyl-2H-chromen-2-ylidene)benzenesulfonamides, the precursor ions have been observed to undergo gas-phase dissociation via two competing channels: (a) the predominant channel involves migration of the sulfonyl cation to the phenyl C atom and the subsequent loss of benzenesulfinic acid along with cyclization reaction, and (b) the minor one involves dissociation of the precursor ion to give an ion/neutral complex of [sulfonyl cation/imine], followed by decomposition to afford sulfonyl cation or the INC-mediated electron transfer to give an imine radical cation. The proposed reaction channels have been supported by theoretical calculations and D-labeling experiments. The gas-phase cyclization reaction originating from the N- to C-sulfonyl cation transfer has been first reported to the best of our knowledge. For the substituted sulfonamides, the presence of electron-donating groups (R(2) -) at the C-ring effectively facilitates the reaction channel of cyclization reaction, whereas that of electron-withdrawing groups inhibits this pathway. Copyright © 2015 John Wiley & Sons, Ltd.

Mesh-structured N-doped graphene@Sb2Se3 hybrids as an anode for large capacity sodium-ion batteries.

PubMed

Zhao, Wenxi; Li, Chang Ming

2017-02-15

A mesh-structured N-doped graphene@Sb 2 Se 3 (NGS) hybrid was one-pot prepared to realize N-doping, nanostructuring and hybridization for a sodium-ion battery anode to deliver much larger reversible specific capacity, faster interfacial electron transfer rate, better ionic and electronic transport, higher rate performance and longer cycle life stability in comparison to the plain Sb 2 Se 3 one. The better performance is ascribed to the unique intertwined porous mash-like structure associated with a strong synergistic effect of N-doped graphene for dramatic improvement of electronic and ionic conductivity by the unique porous structure, the specific capacity of graphene from N doping and fast interfacial electron transfer rate by N-doping induced surface effect and the structure-shortening insertion/desertion pathway of Na + . The detail electrochemical process on the NGS electrode is proposed and analyzed in terms of the experimental results. Copyright © 2016 Elsevier Inc. All rights reserved.

Kynurenine pathway metabolites and enzymes involved in redox reactions.

PubMed

González Esquivel, D; Ramírez-Ortega, D; Pineda, B; Castro, N; Ríos, C; Pérez de la Cruz, V

2017-01-01

Oxido-reduction reactions are a fundamental part of the life due to support many vital biological processes as cellular respiration and glucose oxidation. In the redox reactions, one substance transfers one or more electrons to another substance. An important electron carrier is the coenzyme NAD + , which is involved in many metabolic pathways. De novo biosynthesis of NAD + is through the kynurenine pathway, the major route of tryptophan catabolism, which is sensitive to redox environment and produces metabolites with redox capacity, able to alter biological functions that are controlled by redox-responsive signaling pathways. Kynurenine pathway metabolites have been implicated in the physiology process and in the physiopathology of many diseases; processes that also share others factors as dysregulation of calcium homeostasis, mitochondrial dysfunction, oxidative stress, inflammation and cell death, which impact the redox environment. This review examines in detail the available evidence in which kynurenine pathway metabolites participate in redox reactions and their effect on cellular redox homeostasis, since the knowledge of the main factors and mechanisms that lead to cell death in many neurodegenative disorders and other pathologies, such as mitochondrial dysfunction, oxidative stress and kynurenines imbalance, will allow to develop therapies using them as targets. This article is part of the Special Issue entitled 'The Kynurenine Pathway in Health and Disease'. Copyright © 2016 Elsevier Ltd. All rights reserved.

A first principles investigation of electron transfer between Fe(II) and U(VI) on insulating Al- vs. semiconducting Fe-oxide surfaces via the proximity effect

NASA Astrophysics Data System (ADS)

Taylor, S. D.; Marcano, M. C.; Becker, U.

2017-01-01

This study investigates how the intrinsic chemical and electronic properties of mineral surfaces and their associated electron transfer (ET) pathways influence the reduction of U(VI) by surface-associated Fe(II). Density functional theory (DFT), including the Hubbard U correction to the exchange-correlation functional, was used to investigate sorption/redox reactions and ET mechanisms between Fe(II) and U(VI) coadsorbed on isostructural, periodic (0 0 1) surfaces of the insulator corundum (α-Al2O3) vs. the semiconductor hematite (α-Fe2O3). Furthermore, the coadsorbed Fe(II) and U(VI) ions are spatially separated from one another on the surfaces (⩾5.9 Å) to observe whether electronic-coupling through the semiconducting hematite surface facilitates ET between the adsorbates, a phenomenon known as the proximity effect. The calculations show that the different chemical and electronic properties between the isostructural corundum and hematite (0 0 1) surfaces lead to considerably different ET mechanisms between Fe(II) and U(VI). ET on the insulating corundum (0 0 1) surface is limited by the adsorbates' structural configuration. When Fe(II) and U(VI) are spatially separated and do not directly interact with one another (e.g. via an inner-sphere complex), U(VI) reduction by Fe(II) cannot occur as there is no physical pathway enabling ET between the adsorbates. In contrast to the insulating corundum (0 0 1) surface, the hematite (0 0 1) surface can potentially participate in ET reactions due to the high number of electron acceptor sites from the Fe d-states near the Fermi level at the hematite surface. The adsorption of Fe(II) also introduces d-states near the Fermi level as well as shifts unoccupied d-states of the Fe cations at the hematite surface to lower energies, making the surface more conductive. In turn, electronic coupling through the surface can link the spatially separated adsorbates to one another and provide distinct ET pathways for an electron from Fe(II) to travel through the hematite surface and reach U(VI). The progression and extent of ET occurring on the semiconducting hematite (0 0 1) surface via the proximity effect depends on the electronic properties of the surface. ET between the spatially separated U(VI) and Fe(II) occurs most readily when orbitals between the Fe and U adsorbates overlap with those of neighboring O and Fe ions at the hematite surface, as shown by calculations without the Hubbard U correction. Analyses of the spins densities confirm that the U and Fe adsorbates were reduced and oxidized, respectively, (acquiring 0.33 μB and 0.11-0.20 μB, respectively), while Fe cations at the hematite surface were reduced (losing ⩽0.6 μB). If electrons are highly localized, the amount of orbital mixing and electronic coupling through the hematite surface decreases and in turn leads to a lower degree of spin transfer, as predicted by calculations with the Hubbard U correction. Thus, the proximity effect is a potential mechanism on semiconducting surfaces facilitating surface-mediated redox reactions, although its significance varies depending on the electronic properties and subsequent charge-carrying ability of the surface. These results provide insight into ET pathways and mechanisms on insulating Al- and semiconducting Fe oxide surfaces influencing the reduction U(VI) by Fe(II) that may subsequently limit uranium's transport in the subsurface.

Kinetic Analysis of Competitive Electrocatalytic Pathways: New Insights into Hydrogen Production with Nickel Electrocatalysts

DOE Office of Scientific and Technical Information (OSTI.GOV)

Wiedner, Eric S.; Brown, Houston J.; Helm, Monte L.

2016-01-20

The hydrogen production electrocatalyst Ni(PPh2NPh2)22+ (1) is capable of traversing multiple electrocatalytic pathways. When using dimethylformamidium, DMF(H)+, the mechanism of formation of H2 catalyzed by 1 changes from an ECEC to an EECC mechanism as the potential approaches the Ni(I/0) couple. Two recent electrochemical methods, current-potential analysis and foot-of-the-wave analysis (FOWA), were performed on 1 to measure the detailed chemical kinetics of the competing ECEC and EECC pathways. A sensitivity analysis was performed on the electrochemical methods using digital simulations to gain a better understanding of their strengths and limitations. Notably, chemical rate constants were significantly underestimated when not accountingmore » for electron transfer kinetics, even when electron transfer was fast enough to afford a reversible non-catalytic wave. The EECC pathway of 1 was found to be faster than the ECEC pathway under all conditions studied. Using buffered DMF: DMF(H)+ mixtures led to an increase in the catalytic rate constant (kobs) of the EECC pathway, but kobs for the ECEC pathway did not change when using buffered acid. Further kinetic analysis of the ECEC path revealed that added base increases the rate of isomerization of the exo-protonated Ni(0) isomers to the catalytically active endo-isomers, but decreases the net rate of protonation of Ni(I). FOWA on 1 did not provide accurate rate constants due to incomplete reduction of the exo-protonated Ni(I) intermediate at the foot of the wave, but FOWA could be used to estimate the reduction potential of this previously undetected intermediate. This research was supported as part of the Center for Molecular Electrocatalysis, an Energy Frontier Research Center funded by the U.S. Department of Energy, Office of Science, Office of Basic Energy Sciences. Pacific Northwest National Laboratory is operated by Battelle for the U.S. Department of Energy.« less

Adenovirus-mediated tissue factor pathway inhibitor gene transfer induces apoptosis by blocking the phosphorylation of JAK-2/STAT-3 pathway in vascular smooth muscle cells.

PubMed

Fu, Yu; Zhao, Yong; Liu, Yue; Zhu, Yejing; Chi, Jinyu; Hu, Jing; Zhang, Xiaohui; Yin, Xinhua

2012-10-01

In our previous study, we have demonstrated that tissue factor pathway inhibitor (TFPI) gene could induce vascular smooth muscle cell (VSMC) apoptosis. This study was conducted to investigate whether the overexpression of the TFPI gene can induce VSMC apoptosis by inhibiting JAK-2/STAT-3 pathway phosphorylation and thereby inhibiting the expression of such downstream targets as the apoptotic protein Bcl-2 and cell cycle protein cyclin D1. The effect of TFPI on the expression of survivin, a central molecule in cell survival, was also investigated. Rat VSMCs were infected with recombinant adenovirus containing either the TFPI (Ad-TFPI) or LacZ (Ad-LacZ) gene or DMEM in vitro. TFPI expression was detected by ELISA. TUNEL staining and electron microscope were carried out to determine the apoptosis of VSMCs. The expression levels of JAK-2, p-JAK-2, STAT-3, p-STAT-3, cyclin D1, Bcl-2 and survivin were examined by western blot analysis. TFPI protein was detected in the TFPI group after gene transfer and the peak expression was at the 3rd day. At the 3rd, 5th and 7th days after gene transfer, the apoptotic rates by TUNEL assay in the TFPI group were 10.91 ± 1.66%, 13.46 ± 1.28% and 17.04 ± 1.95%, respectively, whereas those in the LacZ group were 3.28 ± 0.89%, 4.01 ± 0.72% and 4.89 ± 1.17%, respectively. We observed cell contraction, slight mitochondrial swelling, nuclear pyknosis and apoptotic body formation in TFPI-treated VSMCs using electron microscopy. JAK-2, p-JAK-2, STAT-3, p-STAT-3, cyclin D1 and Bcl-2, which are all involved in the JAK-2/STAT-3 pathway, were detected in the VSMCs on the 3rd, 5th and 7th days after gene transfer, which is consistent with previously demonstrated time points when VSMCs apoptosis occurred. The expression levels of p-JAK-2, p-STAT-3, cyclin D1 and Bcl-2 were significantly decreased over time in the TFPI group (each P<0.05) but not in the Ad-LacZ and DMEM groups. However, this attenuation of expression was not observed for JAK-2 and STAT-3 in any of the groups at any time points after gene transfer (each P>0.05). The expression level of survivin in the TFPI group also weakened significantly over time compared with the levels in the Ad-LacZ and DMEM groups (each P<0.05) at the 3rd, 5th and 7th days after gene transfer. The results demonstrated that TFPI played an apoptosis-inducing role in VSMCs in a manner that involves both the suppression of JAK-2/STAT-3 pathway phosphorylation and the down-regulation of survivin. Our data show for the first time that targeting the JAK-2/STAT-3 pathway and survivin by overexpressing TFPI may be a new avenue for the treatment of restenosis. Copyright © 2012 Elsevier Inc. All rights reserved.

Analysis of a Range of Catabolic Mutants Provides Evidence That Phytanoyl-Coenzyme A Does Not Act as a Substrate of the Electron-Transfer Flavoprotein/Electron-Transfer Flavoprotein:Ubiquinone Oxidoreductase Complex in Arabidopsis during Dark-Induced Senescence1[W][OA

PubMed Central

Araújo, Wagner L.; Ishizaki, Kimitsune; Nunes-Nesi, Adriano; Tohge, Takayuki; Larson, Tony R.; Krahnert, Ina; Balbo, Ilse; Witt, Sandra; Dörmann, Peter; Graham, Ian A.; Leaver, Christopher J.; Fernie, Alisdair R.

2011-01-01

The process of dark-induced senescence in plants is not fully understood, however, the functional involvement of an electron-transfer flavoprotein/electron-transfer flavoprotein:ubiquinone oxidoreductase (ETF/ETFQO), has been demonstrated. Recent studies have revealed that the enzymes isovaleryl-coenzyme A (CoA) dehydrogenase and 2-hydroxyglutarate dehydrogenase act as important electron donors to this complex. In addition both enzymes play a role in the breakdown of cellular carbon storage reserves with isovaleryl-CoA dehydrogenase being involved in degradation of the branched-chain amino acids, phytol, and lysine while 2-hydroxyglutarate dehydrogenase is exclusively involved in lysine degradation. Given that the chlorophyll breakdown intermediate phytanoyl-CoA accumulates dramatically both in knockout mutants of the ETF/ETFQO complex and of isovaleryl-CoA dehydrogenase following growth in extended dark periods we have investigated the direct importance of chlorophyll breakdown for the supply of carbon and electrons during this process. For this purpose we isolated three independent Arabidopsis (Arabidopsis thaliana) knockout mutants of phytanoyl-CoA 2-hydroxylase and grew them under the same extended darkness regime as previously used. Despite the fact that these mutants accumulated phytanoyl-CoA and also 2-hydroxyglutarate they exhibited no morphological changes in comparison to the other mutants previously characterized. These results are consistent with a single entry point of phytol breakdown into the ETF/ETFQO system and furthermore suggest that phytol is not primarily metabolized by this pathway. Furthermore analysis of isovaleryl-CoA dehydrogenase/2-hydroxyglutarate dehydrogenase double mutants generated here suggest that these two enzymes essentially account for the entire electron input via the ETF complex. PMID:21788362

Laser-Matter Interaction in Dielectrics: Insight from Picosecond-Pulsed Second-Harmonic Generation in Periodically Poled LiTaO3

NASA Astrophysics Data System (ADS)

Louchev, Oleg A.; Wada, Satoshi; Panchenko, Vladislav Ya.

2017-08-01

We develop a modified two-temperature (2T) model of laser-matter interaction in dielectrics based on experimental insight from picosecond-pulsed high-frequency temperature-controlled second-harmonic (515 nm) generation in periodically poled stoichiometric LiTaO3 crystal and required for computational treatment of short-pulsed nonlinear optics and materials processing applications. We show that the incorporation of an extended set of recombination-kinetics-related energy-release and heat-exchange processes following short-pulsed photoionization by two-photon absorption of the second harmonic allows accurate simulation of the electron-lattice relaxation dynamics and electron-lattice temperature evolution in LiTaO3 crystal in nonlinear laser-frequency conversion. Our experimentally confirmed model and detailed simulation study show that two-photon ionization with the recombination mechanism via ion-electron-lattice interaction followed by a direct transfer of the recombination energy to the lattice is the main laser-matter energy-transfer pathway responsible for the majority of the crystal lattice heating (approximately 90%) continuing for approximately 50 ps after laser-pulse termination and competing with effect of electron-phonon energy transfer from the free electrons. This time delay is due to a recombination bottleneck which hinders faster relaxation to thermal equilibrium in photoionized dielectric crystal. Generally, our study suggests that in dielectrics photoionized by short-pulsed radiation with intensity range used in nonlinear laser-frequency conversion, the electron-lattice relaxation period is defined by the recombination-stage bottleneck of a few tens of picoseconds and not by the time of the electron-phonon energy transfer. This modification of the 2T model can be applied to a broad range of processes involving laser-matter interactions in dielectrics and semiconductors for charge density reaching the range of 1021- 1022 cm-3 .

Redox-dependent complex formation by an ATP-dependent activator of the corrinoid/iron-sulfur protein

PubMed Central

Hennig, Sandra E.; Jeoung, Jae-Hun; Goetzl, Sebastian; Dobbek, Holger

2012-01-01

Movement, cell division, protein biosynthesis, electron transfer against an electrochemical gradient, and many more processes depend on energy conversions coupled to the hydrolysis of ATP. The reduction of metal sites with low reduction potentials (E0′ < -500 mV) is possible by connecting an energetical uphill electron transfer with the hydrolysis of ATP. The corrinoid-iron/sulfur protein (CoFeSP) operates within the reductive acetyl-CoA pathway by transferring a methyl group from methyltetrahydrofolate bound to a methyltransferase to the [Ni-Ni-Fe4S4] cluster of acetyl-CoA synthase. Methylation of CoFeSP only occurs in the low-potential Co(I) state, which can be sporadically oxidized to the inactive Co(II) state, making its reductive reactivation necessary. Here we show that an open-reading frame proximal to the structural genes of CoFeSP encodes an ATP-dependent reductive activator of CoFeSP. Our biochemical and structural analysis uncovers a unique type of reductive activator distinct from the electron-transferring ATPases found to reduce the MoFe-nitrogenase and 2-hydroxyacyl-CoA dehydratases. The CoFeSP activator contains an ASKHA domain (acetate and sugar kinases, Hsp70, and actin) harboring the ATP-binding site, which is also present in the activator of 2-hydroxyacyl-CoA dehydratases and a ferredoxin-like [2Fe-2S] cluster domain acting as electron donor. Complex formation between CoFeSP and its activator depends on the oxidation state of CoFeSP, which provides evidence for a unique strategy to achieve unidirectional electron transfer between two redox proteins. PMID:22431597

DOE Office of Scientific and Technical Information (OSTI.GOV)

Chen, L. X.; Zhang, X.; Lockard, J. V.

Transient molecular structures along chemical reaction pathways are important for predicting molecular reactivity, understanding reaction mechanisms, as well as controlling reaction pathways. During the past decade, X-ray transient absorption spectroscopy (XTA, or LITR-XAS, laser-initiated X-ray absorption spectroscopy), analogous to the commonly used optical transient absorption spectroscopy, has been developed. XTA uses a laser pulse to trigger a fundamental chemical process, and an X-ray pulse(s) to probe transient structures as a function of the time delay between the pump and probe pulses. Using X-ray pulses with high photon flux from synchrotron sources, transient electronic and molecular structures of metal complexes havemore » been studied in disordered media from homogeneous solutions to heterogeneous solution-solid interfaces. Several examples from the studies at the Advanced Photon Source in Argonne National Laboratory are summarized, including excited-state metalloporphyrins, metal-to-ligand charge transfer (MLCT) states of transition metal complexes, and charge transfer states of metal complexes at the interface with semiconductor nanoparticles. Recent developments of the method are briefly described followed by a future prospective of XTA. It is envisioned that concurrent developments in X-ray free-electron lasers and synchrotron X-ray facilities as well as other table-top laser-driven femtosecond X-ray sources will make many breakthroughs and realise dreams of visualizing molecular movies and snapshots, which ultimately enable chemical reaction pathways to be controlled.« less

High yield of secondary B-side electron transfer in mutant Rhodobacter capsulatus reaction centers

DOE Office of Scientific and Technical Information (OSTI.GOV)

Kressel, Lucas; Faries, Kaitlyn M.; Wander, Marc J.

2014-08-01

From the crystal structures of reaction centers (RCs) from purple photosynthetic bacteria, two pathways for electron transfer (ET) are apparent but only one pathway (the A side) operates in the native protein-cofactor complex. Partial activation of the B-side pathway has unveiled the true inefficiencies of ET processes on that side in comparison to analogous reactions on the A side. Of significance are the relative rate constants for forward ET and the competing charge recombination reactions. On the B side, these rate constants are nearly equal for the secondary charge-separation step (ET from bacteriopheophytin to quinone), relegating the yield of thismore » process to < 50%. Herein we report efforts to optimize this step. In surveying all possible residues at position 131 in the M subunit, we discovered that when glutamic acid replaces the native valine the efficiency of the secondary ET is nearly two-fold higher than in the wild-type RC. The positive effect of M131 Glu is likely due to formation of a hydrogen bond with the ring V keto group of the B-side bacteriopheophytin leading to stabilization of the charge-separated state involving this cofactor. In conclusion, this change slows charge recombination by roughly a factor of two and affords the improved yield of the desired forward ET to the B-side quinone terminal acceptor.« less

Broadband ultrafast photoprotection by oxybenzone across the UVB and UVC spectral regions.

PubMed

Baker, Lewis A; Horbury, Michael D; Greenough, Simon E; Ashfold, Michael N R; Stavros, Vasilios G

2015-10-01

Recent studies have shed light on the energy dissipation mechanism of oxybenzone, a common ingredient in commercial sunscreens. After UVA photoexcitation, the dissipation mechanism may be understood in terms of an initial ultrafast excited state enol → keto tautomerisation, followed by nonadiabatic transfer to the ground electronic state and subsequent collisional relaxation to the starting enol tautomer. We expand on these studies using femtosecond transient electronic absorption spectroscopy to understand the non-radiative relaxation pathways of oxybenzone in cyclohexane and in methanol after UVB and UVC excitation. We find that the relaxation pathway may be understood in the same way as when exciting in the UVA region, concluding that oxybenzone displays proficient broadband non-radiative photoprotection, and thus photophysically justifying its inclusion in sunscreen mixtures.

Using Physical Organic Chemistry To Shape the Course of Electrochemical Reactions.

PubMed

Moeller, Kevin D

2018-05-09

While organic electrochemistry can look quite different to a chemist not familiar with the technique, the reactions are at their core organic reactions. As such, they are developed and optimized using the same physical organic chemistry principles employed during the development of any other organic reaction. Certainly, the electron transfer that triggers the reactions can require a consideration of new "wrinkles" to those principles, but those considerations are typically minimal relative to the more traditional approaches needed to manipulate the pathways available to the reactive intermediates formed downstream of that electron transfer. In this review, three very different synthetic challenges-the generation and trapping of radical cations, the development of site-selective reactions on microelectrode arrays, and the optimization of current in a paired electrolysis-are used to illustrate this point.

Dynamic Pattern Formation in Electron-Beam-Induced Etching [Emergent formation of dynamic topographic patterns in electron beam induced etching

DOE PAGES

Martin, Aiden A.; Bahm, Alan; Bishop, James; ...

2015-12-15

Here, we report highly ordered topographic patterns that form on the surface of diamond, span multiple length scales, and have a symmetry controlled by the precursor gas species used in electron-beam-induced etching (EBIE). The pattern formation dynamics reveals an etch rate anisotropy and an electron energy transfer pathway that is overlooked by existing EBIE models. Therefore, we, modify established theory such that it explains our results and remains universally applicable to EBIE. Furthermore, the patterns can be exploited in controlled wetting, optical structuring, and other emerging applications that require nano- and microscale surface texturing of a wide band-gap material.

Cardiolipin Fatty Acid Remodeling Regulates Mitochondrial Function by Modifying the Electron Entry Point in the Respiratory Chain

PubMed Central

Vergeade, Aurelia; Bertram, Clinton C.; Bikineyeva, Alfiya T.; Zackert, William E.; Zinkel, Sandra S.; May, James M.; Dikalov, Sergey I.; Roberts, L. Jackson; Boutaud, Olivier

2016-01-01

Modifications of cardiolipin (CL) levels or compositions are associated with changes in mitochondrial function in a wide range of pathologies. We have made the discovery that acetaminophen remodels CL fatty acids composition from tetralinoleoyl to linoleoyltrioleoyl-CL, a remodeling that is associated with decreased mitochondrial respiration. Our data show that CL remodeling causes a shift in electron entry from complex II to the β-oxidation electron transfer flavoprotein quinone oxidoreductase (ETF/QOR) pathway. These data demonstrate that electron entry in the respiratory chain is regulated by CL fatty acid composition and provide proof-of-concept that pharmacological intervention can be used to modify CL composition. PMID:27085476

Electron Mobility and Trapping in Ferrihydrite Nanoparticles

DOE Office of Scientific and Technical Information (OSTI.GOV)

Soltis, Jennifer A.; Schwartzberg, Adam M.; Zarzycki, Piotr

Iron is the most abundant transition metal in the Earth's crust, and naturally occurring iron oxide minerals play a commanding role in environmental redox reactions. Although iron oxide redox reactions are well studied, their precise mechanisms are not fully understood. Recent work has shown that these involve electron transfer pathways within the solid, suggesting that overall reaction rates could be dependent on electron mobility. Initial ultrafast spectroscopy studies of iron oxide nanoparticles sensitized by fluorescein derivatives supported a model for electron mobility based on polaronic hopping of electron charge carriers between iron sites, but the constitutive relationships between hopping mobilitiesmore » and interfacial charge transfer processes has remained obscured. We developed a coarse-grained lattice Monte Carlo model to simulate the collective mobilities and lifetimes of these photoinjected electrons with respect to recombination with adsorbed dye molecules for the essential nanophase ferrihydrite, and tested predictions made by the simulations using pump-probe spectroscopy. We acquired optical transient absorption spectra as a function of particle size and under a variety of solution conditions, and used cryogenic transmission electron microscopy to determine the aggregation state of the nanoparticles. We observed biphasic electron recombination kinetics over timescales that spanned picoseconds to microseconds, the slower regime of which was fit with a stretched exponential decay function. The recombination rates were weakly affected by nanoparticle size and aggregation state, suspension pH, and the injection of multiple electrons per nanoparticle. We conclude that electron mobility indeed limits the rate of interfacial electron transfer in these systems with the slowest processes relating to escape from deep traps, the presence of which outweighs the influence of environmental factors such as pH-dependent surface charge.« less

Electron Mobility and Trapping in Ferrihydrite Nanoparticles

DOE Office of Scientific and Technical Information (OSTI.GOV)

Soltis, Jennifer A.; Schwartzberg, Adam M.; Zarzycki, Piotr

Iron is the most abundant transition metal in the Earth’s crust, and naturally occurring iron oxide minerals play a commanding role in environmental redox reactions. Although iron oxide redox reactions are well-studied, their precise mechanisms are not fully understood. Recent work has shown that these involve electron transfer pathways within the solid, suggesting that overall reaction rates could be dependent upon electron mobility. Initial ultrafast spectroscopy studies of iron oxide nanoparticles sensitized by fluorescein derivatives supported a model for electron mobility based on polaronic hopping of electron charge carriers between iron sites, but the constitutive relationships between hopping mobilities andmore » interfacial charge transfer processes has remained obscured. In this paper, we developed a coarse-grained lattice Monte Carlo model to simulate the collective mobilities and lifetimes of these photoinjected electrons with respect to recombination with adsorbed dye molecules for essential nanophase ferrihydrite and tested predictions made by the simulations using pump–probe spectroscopy. We acquired optical transient absorption spectra as a function of the particle size and under a variety of solution conditions and used cryogenic transmission electron microscopy to determine the aggregation state of the nanoparticles. We observed biphasic electron recombination kinetics over time scales that spanned from picoseconds to microseconds, the slower regime of which was fit with a stretched exponential decay function. The recombination rates were weakly affected by the nanoparticle size and aggregation state, suspension pH, and injection of multiple electrons per nanoparticle. Finally, we conclude that electron mobility indeed limits the rate of interfacial electron transfer in these systems, with the slowest processes relating to escape from deep traps, the presence of which outweighs the influence of environmental factors, such as pH-dependent surface charge.« less

Electron Mobility and Trapping in Ferrihydrite Nanoparticles

DOE PAGES

Soltis, Jennifer A.; Schwartzberg, Adam M.; Zarzycki, Piotr; ...

2017-05-18

Iron is the most abundant transition metal in the Earth’s crust, and naturally occurring iron oxide minerals play a commanding role in environmental redox reactions. Although iron oxide redox reactions are well-studied, their precise mechanisms are not fully understood. Recent work has shown that these involve electron transfer pathways within the solid, suggesting that overall reaction rates could be dependent upon electron mobility. Initial ultrafast spectroscopy studies of iron oxide nanoparticles sensitized by fluorescein derivatives supported a model for electron mobility based on polaronic hopping of electron charge carriers between iron sites, but the constitutive relationships between hopping mobilities andmore » interfacial charge transfer processes has remained obscured. In this paper, we developed a coarse-grained lattice Monte Carlo model to simulate the collective mobilities and lifetimes of these photoinjected electrons with respect to recombination with adsorbed dye molecules for essential nanophase ferrihydrite and tested predictions made by the simulations using pump–probe spectroscopy. We acquired optical transient absorption spectra as a function of the particle size and under a variety of solution conditions and used cryogenic transmission electron microscopy to determine the aggregation state of the nanoparticles. We observed biphasic electron recombination kinetics over time scales that spanned from picoseconds to microseconds, the slower regime of which was fit with a stretched exponential decay function. The recombination rates were weakly affected by the nanoparticle size and aggregation state, suspension pH, and injection of multiple electrons per nanoparticle. Finally, we conclude that electron mobility indeed limits the rate of interfacial electron transfer in these systems, with the slowest processes relating to escape from deep traps, the presence of which outweighs the influence of environmental factors, such as pH-dependent surface charge.« less

Reconstruction and Evaluation of the Synthetic Bacterial MEP Pathway in Saccharomyces cerevisiae

PubMed Central

Partow, Siavash; Siewers, Verena; Daviet, Laurent; Schalk, Michel; Nielsen, Jens

2012-01-01

Isoprenoids, which are a large group of natural and chemical compounds with a variety of applications as e.g. fragrances, pharmaceuticals and potential biofuels, are produced via two different metabolic pathways, the mevalonate (MVA) pathway and the 2-C-methyl-D-erythritol 4-phosphate (MEP) pathway. Here, we attempted to replace the endogenous MVA pathway in Saccharomyces cerevisiae by a synthetic bacterial MEP pathway integrated into the genome to benefit from its superior properties in terms of energy consumption and productivity at defined growth conditions. It was shown that the growth of a MVA pathway deficient S. cerevisiae strain could not be restored by the heterologous MEP pathway even when accompanied by the co-expression of genes erpA, hISCA1 and CpIscA involved in the Fe-S trafficking routes leading to maturation of IspG and IspH and E. coli genes fldA and fpr encoding flavodoxin and flavodoxin reductase believed to be responsible for electron transfer to IspG and IspH. PMID:23285068

The Critical Role of Arabidopsis Electron-Transfer Flavoprotein:Ubiquinone Oxidoreductase during Dark-Induced StarvationW⃞

PubMed Central

Ishizaki, Kimitsune; Larson, Tony R.; Schauer, Nicolas; Fernie, Alisdair R.; Graham, Ian A.; Leaver, Christopher J.

2005-01-01

In mammals, electron-transfer flavoprotein:ubiquinone oxidoreductase (ETFQO) and electron-transfer flavoprotein (ETF) are functionally associated, and ETF accepts electrons from at least nine mitochondrial matrix flavoprotein dehydrogenases and transfers them to ubiquinone in the inner mitochondrial membrane. In addition, the mammalian ETF/ETFQO system plays a key role in β-oxidation of fatty acids and catabolism of amino acids and choline. By contrast, nothing is known of the function of ETF and ETFQO in plants. Sequence analysis of the unique Arabidopsis thaliana homologue of ETFQO revealed high similarity to the mammalian ETFQO protein. Moreover, green fluorescent protein cellular localization experiments suggested a mitochondrial location for this protein. RNA gel blot analysis revealed that Arabidopsis ETFQO transcripts accumulated in long-term dark-treated leaves. Analysis of three independent insertional mutants of Arabidopsis ETFQO revealed a dramatic reduction in their ability to withstand extended darkness, resulting in senescence and death within 10 d after transfer, whereas wild-type plants remained viable for at least 15 d. Metabolite profiling of dark-treated leaves of the wild type and mutants revealed a dramatic decline in sugar levels. In contrast with the wild type, the mutants demonstrated a significant accumulation of several amino acids, an intermediate of Leu catabolism, and, strikingly, high-level accumulation of phytanoyl-CoA. These data demonstrate the involvement of a mitochondrial protein, ETFQO, in the catabolism of Leu and potentially of other amino acids in higher plants and also imply a novel role for this protein in the chlorophyll degradation pathway activated during dark-induced senescence and sugar starvation. PMID:16055629

Remodeling pathway control of mitochondrial respiratory capacity by temperature in mouse heart: electron flow through the Q-junction in permeabilized fibers.

PubMed

Lemieux, Hélène; Blier, Pierre U; Gnaiger, Erich

2017-06-06

Fuel substrate supply and oxidative phosphorylation are key determinants of muscle performance. Numerous studies of mammalian mitochondria are carried out (i) with substrate supply that limits electron flow, and (ii) far below physiological temperature. To analyze potentially implicated biases, we studied mitochondrial respiratory control in permeabilized mouse myocardial fibers using high-resolution respirometry. The capacity of oxidative phosphorylation at 37 °C was nearly two-fold higher when fueled by physiological substrate combinations reconstituting tricarboxylic acid cycle function, compared with electron flow measured separately through NADH to Complex I or succinate to Complex II. The relative contribution of the NADH pathway to physiological respiratory capacity increased with a decrease in temperature from 37 to 25 °C. The apparent excess capacity of cytochrome c oxidase above physiological pathway capacity increased sharply under hypothermia due to limitation by NADH-linked dehydrogenases. This mechanism of mitochondrial respiratory control in the hypothermic mammalian heart is comparable to the pattern in ectotherm species, pointing towards NADH-linked mt-matrix dehydrogenases and the phosphorylation system rather than electron transfer complexes as the primary drivers of thermal sensitivity at low temperature. Delineating the link between stress and remodeling of oxidative phosphorylation is important for understanding metabolic perturbations in disease evolution and cardiac protection.

Prediction of FAD binding sites in electron transport proteins according to efficient radial basis function networks and significant amino acid pairs.

PubMed

Le, Nguyen-Quoc-Khanh; Ou, Yu-Yen

2016-07-30

Cellular respiration is a catabolic pathway for producing adenosine triphosphate (ATP) and is the most efficient process through which cells harvest energy from consumed food. When cells undergo cellular respiration, they require a pathway to keep and transfer electrons (i.e., the electron transport chain). Due to oxidation-reduction reactions, the electron transport chain produces a transmembrane proton electrochemical gradient. In case protons flow back through this membrane, this mechanical energy is converted into chemical energy by ATP synthase. The convert process is involved in producing ATP which provides energy in a lot of cellular processes. In the electron transport chain process, flavin adenine dinucleotide (FAD) is one of the most vital molecules for carrying and transferring electrons. Therefore, predicting FAD binding sites in the electron transport chain is vital for helping biologists understand the electron transport chain process and energy production in cells. We used an independent data set to evaluate the performance of the proposed method, which had an accuracy of 69.84 %. We compared the performance of the proposed method in analyzing two newly discovered electron transport protein sequences with that of the general FAD binding predictor presented by Mishra and Raghava and determined that the accuracy of the proposed method improved by 9-45 % and its Matthew's correlation coefficient was 0.14-0.5. Furthermore, the proposed method enabled reducing the number of false positives significantly and can provide useful information for biologists. We developed a method that is based on PSSM profiles and SAAPs for identifying FAD binding sites in newly discovered electron transport protein sequences. This approach achieved a significant improvement after we added SAAPs to PSSM features to analyze FAD binding proteins in the electron transport chain. The proposed method can serve as an effective tool for predicting FAD binding sites in electron transport proteins and can help biologists understand the functions of the electron transport chain, particularly those of FAD binding sites. We also developed a web server which identifies FAD binding sites in electron transporters available for academics.

Extracting electron transfer coupling elements from constrained density functional theory

NASA Astrophysics Data System (ADS)

Wu, Qin; Van Voorhis, Troy

2006-10-01

Constrained density functional theory (DFT) is a useful tool for studying electron transfer (ET) reactions. It can straightforwardly construct the charge-localized diabatic states and give a direct measure of the inner-sphere reorganization energy. In this work, a method is presented for calculating the electronic coupling matrix element (Hab) based on constrained DFT. This method completely avoids the use of ground-state DFT energies because they are known to irrationally predict fractional electron transfer in many cases. Instead it makes use of the constrained DFT energies and the Kohn-Sham wave functions for the diabatic states in a careful way. Test calculations on the Zn2+ and the benzene-Cl atom systems show that the new prescription yields reasonable agreement with the standard generalized Mulliken-Hush method. We then proceed to produce the diabatic and adiabatic potential energy curves along the reaction pathway for intervalence ET in the tetrathiafulvalene-diquinone (Q-TTF-Q) anion. While the unconstrained DFT curve has no reaction barrier and gives Hab≈17kcal /mol, which qualitatively disagrees with experimental results, the Hab calculated from constrained DFT is about 3kcal /mol and the generated ground state has a barrier height of 1.70kcal/mol, successfully predicting (Q-TTF-Q)- to be a class II mixed-valence compound.

Direct observation of ultrafast-electron-transfer reactions unravels high effectiveness of reductive DNA damage

PubMed Central

Nguyen, Jenny; Ma, Yuhan; Luo, Ting; Bristow, Robert G.; Jaffray, David A.; Lu, Qing-Bin

2011-01-01

Both water and electron-transfer reactions play important roles in chemistry, physics, biology, and the environment. Oxidative DNA damage is a well-known mechanism, whereas the relative role of reductive DNA damage is unknown. The prehydrated electron (), a novel species of electrons in water, is a fascinating species due to its fundamental importance in chemistry, biology, and the environment. is an ideal agent to observe reductive DNA damage. Here, we report both the first in situ femtosecond time-resolved laser spectroscopy measurements of ultrafast-electron-transfer (UET) reactions of with various scavengers (KNO3, isopropanol, and dimethyl sulfoxide) and the first gel electrophoresis measurements of DNA strand breaks induced by and OH• radicals co-produced by two-UV-photon photolysis of water. We strikingly found that the yield of reductive DNA strand breaks induced by each is twice the yield of oxidative DNA strand breaks induced by each OH• radical. Our results not only unravel the long-standing mystery about the relative role of radicals in inducing DNA damage under ionizing radiation, but also challenge the conventional notion that oxidative damage is the main pathway for DNA damage. The results also show the potential of femtomedicine as a new transdisciplinary frontier and the broad significance of UET reactions of in many processes in chemistry, physics, biology, and the environment. PMID:21730183

Freeze-Quench Magnetic Circular Dichroism Spectroscopic Study of the "Very Rapid" Intermediate in Xanthine Oxidase.

PubMed

Jones, Robert M.; Inscore, Frank E.; Hille, Russ; Kirk, Martin L.

1999-11-01

Freeze-quench magnetic circular dichroism spectroscopy (MCD) has been used to trap and study the excited-state electronic structure of the Mo(V) active site in a xanthine oxidase intermediate generated with substoichiometric concentrations of the slow substrate 2-hydroxy-6-methylpurine. EPR spectroscopy has shown that the intermediate observed in the MCD experiment is the "very rapid" intermediate, which lies on the main catalytic pathway. The low-energy (< approximately 30 000 cm(-1)) C-term MCD of this intermediate is remarkably similar to that of the model compound LMoO(bdt) (L = hydrotris(3,5-dimethyl-1-pyrazolyl)borate; bdt = 1,2-benzenedithiolate), and the MCD bands have been assigned as dithiolate S(ip) --> Mo d(xy) and S(op) --> Mo d(xz,yz) LMCT transitions. These transitions result from a coordination geometry of the intermediate where the Mo=O bond is oriented cis to the ene-1,2-dithiolate of the pyranopterin. Since X-ray crystallography has indicated that a terminal sulfido ligand is oriented cis to the ene-1,2-dithiolate in oxidized xanthine oxidase related Desulfovibrio gigas aldehyde oxidoreductase, we have suggested that a conformational change occurs upon substrate binding. The substrate-mediated conformational change is extremely significant with respect to electron-transfer regeneration of the active site, as covalent interactions between the redox-active Mo d(xy) orbital and the S(ip) orbitals of the ene-1,2-dithiolate are maximized when the oxo ligand is oriented cis to the dithiolate plane. This underlies the importance of the ene-1,2-dithiolate portion of the pyranopterin in providing an efficient superexchange pathway for electron transfer. The results of this study indicate that electron-transfer regeneration of the active site may be gated by the orientation of the Mo=O bond relative to the ene-1,2-dithiolate chelate. Poor overlap between the Mo d(xy) orbital and the S(ip) orbitals of the dithiolate in the oxidized enzyme geometry may provide a means of preventing one-electron reduction of the active site, resulting in enzyme inhibition with respect to the two-electron oxidation of native substrates.

A 4-dimethylaminobenzoate-functionalized Ti6-oxo cluster with a narrow band gap and enhanced photoelectrochemical activity: a combined experimental and computational study.

PubMed

Lv, Hai-Ting; Cui, Ying; Zhang, Yu-Min; Li, Hua-Min; Zou, Guo-Dong; Duan, Rui-Huan; Cao, Jun-Tao; Jing, Qiang-Shan; Fan, Yang

2017-09-28

Organic donor-π-bridge-acceptor (D-π-A) dyes with arylamines as an electron donor have been widely used as photosensitizers for dye-sensitized solar cells (DSSCs). However, titanium-oxo clusters (TOCs) functionalized with this kind of D-π-A structured dye-molecule have rarely been explored. In the present study, the 4-dimethylaminobenzoate-functionalized titanium-oxo cluster [Ti 6 (μ 3 -O) 6 (OiPr) 6 (DMABA) 6 ]·2C 6 H 5 CH 3 (DMABA = 4-dimethylaminobenzoate) was synthesized and structurally characterized by single-crystal X-ray diffraction. For comparison, two other Ti 6 -oxo clusters, namely [Ti 6 (μ 3 -O) 6 (OiPr) 6 (AD) 6 ] (AD = 1-adamantanecarboxylate) and [Ti 6 (μ 3 -O) 2 (μ 2 -O)(μ 2 -OiPr) 4 (OiPr) 10 (DMM) 2 ] (DMM = dimethylmalonate), were also studied. The DMABA-functionalized cluster exhibits a remarkably reduced band gap of ∼2.5 eV and much enhanced photocurrent response in comparison with the other two clusters. The electronic structures and electronic transitions of the clusters were studied by DFT and TDDFT calculations. The computational results suggest that the low-energy transitions of the DMABA-functionalized cluster have a substantial charge-transfer character arising from the DMABA → {Ti 6 } cluster core ligand-to-core charge transfer (LCCT), along with the DMABA-based intra-ligand charge transfer (ILCT). These low-energy charge transfer transitions provide efficient electron injection pathways for photon-to-electron conversion.

The cytochrome b6f complex at the crossroad of photosynthetic electron transport pathways.

PubMed

Tikhonov, Alexander N

2014-08-01

Regulation of photosynthetic electron transport at the level of the cytochrome b6f complex provides efficient performance of the chloroplast electron transport chain (ETC). In this review, after brief overview of the structural organization of the chloroplast ETC, the consideration of the problem of electron transport control is focused on the plastoquinone (PQ) turnover and its interaction with the b6f complex. The data available show that the rates of plastoquinol (PQH2) formation in PSII and its diffusion to the b6f complex do not limit the overall rate of electron transfer between photosystem II (PSII) and photosystem I (PSI). Analysis of experimental and theoretical data demonstrates that the rate-limiting step in the intersystem chain of electron transport is determined by PQH2 oxidation at the Qo-site of the b6f complex, which is accompanied by the proton release into the thylakoid lumen. The acidification of the lumen causes deceleration of PQH2 oxidation, thus impeding the intersystem electron transport. Two other mechanisms of regulation of the intersystem electron transport have been considered: (i) "state transitions" associated with the light-induced redistribution of solar energy between PSI and PSII, and (ii) redistribution of electron fluxes between alternative pathways (noncyclic electron transport and cyclic electron flow around PSI). Copyright © 2013 Elsevier Masson SAS. All rights reserved.

How exciton-vibrational coherences control charge separation in the photosystem II reaction center.

PubMed

Novoderezhkin, Vladimir I; Romero, Elisabet; van Grondelle, Rienk

2015-12-14

In photosynthesis absorbed sun light produces collective excitations (excitons) that form a coherent superposition of electronic and vibrational states of the individual pigments. Two-dimensional (2D) electronic spectroscopy allows a visualization of how these coherences are involved in the primary processes of energy and charge transfer. Based on quantitative modeling we identify the exciton-vibrational coherences observed in 2D photon echo of the photosystem II reaction center (PSII-RC). We find that the vibrations resonant with the exciton splittings can modify the delocalization of the exciton states and produce additional states, thus promoting directed energy transfer and allowing a switch between the two charge separation pathways. We conclude that the coincidence of the frequencies of the most intense vibrations with the splittings within the manifold of exciton and charge-transfer states in the PSII-RC is not occurring by chance, but reflects a fundamental principle of how energy conversion in photosynthesis was optimized.

The Role of 4-Hydroxyphenylpyruvate Dioxygenase in Enhancement of Solid-Phase Electron Transfer by Shewanella oneidensis MR-1

DOE Office of Scientific and Technical Information (OSTI.GOV)

Turick, Charles E.; Beliaev, Alex S.; Zakrajsek, Brian A.

2009-05-01

ABSTRACT - While mechanistic details of dissimilatory metal reduction are far from being understood, it is postulated that the electron transfer to solid metal oxides is mediated by outer membrane associated c-type cytochromes and electron shuttling compounds. This study focuses on the production of homogensitate in Shewanella oneidensis MR-1, an intermediate of the tyrosine degradation pathway, which is a precursor of a redox cycling metabolite, pyomelanin. We determined that two enzymes involved in this pathway, 4-hydroxyphenylpyruvate dioxygenase (4HPPD) and homogentisate 1,2-dioxygenase are responsible for homogentisate production and oxidation, respectively. Inhibition of 4-HPPD activity with the specific inhibitor sulcotrione ([2-(2- chloro-more » 4- methane sulfonylbenzoyl)-1,3-cyclohexanedione), and deletion of melA, a gene encoding 4-HPPD, resulted in no pyomelanin production by S. oneidensis MR-1. Conversely, deletion of hmgA, which encodes the putative homogentisate 1,2-dioxygenase, resulted in pyomelanin overproduction. The efficiency and rates at which MR-1 reduces hydrous ferric oxide were directly linked to the ability of mutant strains to produce pyomelanin. Electrochemical studies with whole cells demonstrated that pyomelanin substantially increases the formal potential (E°') of S. oneidensis MR-1. Based on our findings, environmental production of pyomelanin likely contributes to an increased solid-phase metal reduction capacity in S. oneidensis MR-1.« less

THE ROLE OF 4-HYDROXYPHENYLPYRUVATE DIOXYGENASE IN ENHANCEMENT OF SOLID-PHASE ELECTRON TRANSFER BY SHEWANELLA ONEIDENSIS MR-1

DOE Office of Scientific and Technical Information (OSTI.GOV)

Turick, C; Amy Ekechukwu, A

2007-06-01

While mechanistic details of dissimilatory metal reduction are far from being understood, it is postulated that the electron transfer to solid metal oxides is mediated by outer membrane-associated c-type cytochromes and redox active electron shuttling compounds. This study focuses on the production of homogensitate in Shewanella oneidensis MR-1, an intermediate of tyrosine degradation pathway, which is a precursor of a redox cycling metabolite, pyomelanin. In this study, we determined that two enzymes involved in this pathway, 4-hydroxyphenylpyruvate dioxygenase (4HPPD) and homogentisate 1,2-dioxygenase are responsible for homogentisate production and oxidation, respectively. Inhibition of 4-HPPD activity with the specific inhibitor sulcotrione (2-(2-chloro-4-methanemore » sulfonylbenzoyl)-1,3-cyclohexanedione), and deletion of melA, a gene encoding 4-HPPD, resulted in no pyomelanin production by S. oneidensis MR-1. Conversely, deletion of hmgA which encodes the putative homogentisate 1,2-dioxygenase, resulted in pyomelanin overproduction. The efficiency and rates, with which MR-1 reduces hydrous ferric oxide, were directly linked to the ability of mutant strains to produce pyomelanin. Electrochemical studies with whole cells demonstrated that pyomelanin substantially increases the formal potential (E{sup o}{prime}) of S. oneidensis MR-1. Based on this work, environmental production of pyomelanin likely contributes to an increased solid-phase metal reduction capacity in Shewanella oneidensis.« less

Clinical information transfer and data capture in the acute myocardial infarction pathway: an observational study.

PubMed

Kesavan, Sujatha; Kelay, Tanika; Collins, Ruth E; Cox, Benita; Bello, Fernando; Kneebone, Roger L; Sevdalis, Nick

2013-10-01

Acute myocardial infarctions (MIs) or heart attacks are the result of a complete or an incomplete occlusion of the lumen of the coronary artery with a thrombus. Prompt diagnosis and early coronary intervention results in maximum myocardial salvage, hence time to treat is of the essence. Adequate, accurate and complete information is vital during the early stages of admission of an MI patient and can impact significantly on the quality and safety of patient care. This study aimed to record how clinical information between different clinical teams during the journey of a patient in the MI care pathway is captured and to review the flow of information within this care pathway. A prospective, descriptive, structured observational study to assess (i) current clinical information systems (CIS) utilization and (ii) real-time information availability within an acute cardiac care setting was carried out. Completeness and availability of patient information capture across four key stages of the MI care pathway were assessed prospectively. Thirteen separate information systems were utilized during the four phases of the MI pathway. Observations revealed fragmented CIS utilization, with users accessing an average of six systems to gain a complete set of patient information. Data capture was found to vary between each pathway stage and in both patient cohort risk groupings. The highest level of information completeness (100%) was observed only in the discharge stage of the MI care pathway. The lowest level of information completeness (58%) was observed in the admission stage. The study highlights fragmentation, CIS duplication, and discrepancies in the current clinical information capture and data transfer across the MI care pathway in an acute cardiac care setting. The development of an integrated and user-friendly electronic data capture and transfer system would reduce duplication and would facilitate efficient and complete information provision at the point of care. © 2012 John Wiley & Sons Ltd.

Enhancing the performance of Escherichia coli-inoculated microbial fuel cells by introduction of the phenazine-1-carboxylic acid pathway.

PubMed

Feng, Jiao; Qian, Ying; Wang, Zhen; Wang, Xin; Xu, Sheng; Chen, Kequan; Ouyang, Pingkai

2018-06-10

Microbial fuel cells (MFCs) are a renewable green energy source that uses microorganisms to catalytically convert chemical energy into electrical energy. The efficiency of extracellular electron transfer (EET) from the microbe cell to the anode electrode plays a key role in the MFC. However, the insulating properties of the cell membrane limit the efficiency of EET. Herein, EET efficiency was improved by introducing a phenazine synthesis pathway into Escherichia coli. Through the heterologous expression of phzA1B1C1D1E1F1G1, phenazine-1-carboxylic acid production increased, and the maximum power density increased from 16.7 mW/m 2 to 181.1 mW/m 2 . Furthermore, the charge transfer resistance of 6.7 Ω decreased to 4.2 Ω, which reflected the enhancement of the EET efficiency and the electricity power output. Our results imply that introducing a heterologous electron shuttle into E. coli could be an efficient approach to improving the EET efficiency and performance of an MFC. Copyright © 2018 Elsevier B.V. All rights reserved.

Rational engineering of Geobacter sulfurreducens electron transfer components: A foundation for building improved Geobacter-based bioelectrochemical technologies

DOE PAGES

Dantas, Joana M.; Morgado, Leonor; Aklujkar, Muktak; ...

2015-07-30

Multiheme cytochromes have been implicated in Geobacter sulfurreducens extracellular electron transfer (EET). These proteins are potential targets to improve EET and enhance bioremediation and electrical current production by G. sulfurreducens. However, the functional characterization of multiheme cytochromes is particularly complex due to the co-existence of several microstates in solution, connecting the fully reduced and fully oxidized states. Throughout the last decade, new strategies have been developed to characterize multiheme redox proteins functionally and structurally. These strategies were used to reveal the functional mechanism of G. sulfurreducens multiheme cytochromes and also to identify key residues in these proteins for EET. Inmore » previous studies, we set the foundations for enhancement of the EET abilities of G. sulfurreducens by characterizing a family of five triheme cytochromes (PpcA-E). These periplasmic cytochromes are implicated in electron transfer between the oxidative reactions of metabolism in the cytoplasm and the reduction of extracellular terminal electron acceptors at the cell's outer surface. The results obtained suggested that PpcA can couple e -/H + transfer, a property that might contribute to the proton electrochemical gradient across the cytoplasmic membrane for metabolic energy production. The structural and functional properties of PpcA were characterized in detail and used for rational design of a family of 23 single site PpcA mutants. In this review, we summarize the functional characterization of the native and mutant proteins. Mutants that retain the mechanistic features of PpcA and adopt preferential e -/H + transfer pathways at lower reduction potential values compared to the wild-type protein were selected for in vivo studies as the best candidates to increase the electron transfer rate of G. sulfurreducens. For the first time G. sulfurreducens strains have been manipulated by the introduction of mutant forms of essential proteins with the aim to develop and improve bioelectrochemical technologies.« less

CypD(-/-) hearts have altered levels of proteins involved in Krebs cycle, branch chain amino acid degradation and pyruvate metabolism.

PubMed

Menazza, Sara; Wong, Renee; Nguyen, Tiffany; Wang, Guanghui; Gucek, Marjan; Murphy, Elizabeth

2013-03-01

Cyclophilin D (CypD) is a mitochondrial chaperone that has been shown to regulate the mitochondrial permeability transition pore (MPTP). MPTP opening is a major determinant of mitochondrial dysfunction and cardiomyocyte death during ischemia/reperfusion (I/R) injury. Mice lacking CypD have been widely used to study regulation of the MPTP, and it has been shown recently that genetic depletion of CypD correlates with elevated levels of mitochondrial Ca(2+). The present study aimed to characterize the metabolic changes in CypD(-/-) hearts. Initially, we used a proteomics approach to examine protein changes in CypD(-/-) mice. Using pathway analysis, we found that CypD(-/-) hearts have alterations in branched chain amino acid metabolism, pyruvate metabolism and the Krebs cycle. We tested whether these metabolic changes were due to inhibition of electron transfer from these metabolic pathways into the electron transport chain. As we found decreased levels of succinate dehydrogenase and electron transfer flavoprotein in the proteomics analysis, we examined whether activities of these enzymes might be altered. However, we found no alterations in their activities. The proteomics study also showed a 23% decrease in carnitine-palmitoyltransferase 1 (CPT1), which prompted us to perform a metabolomics analysis. Consistent with the decrease in CPT1, we found a significant decrease in C4/Ci4, C5-OH/C3-DC, C12:1, C14:1, C16:1, and C20:3 acyl carnitines in hearts from CypD(-/-) mice. In summary, CypD(-/-) hearts exhibit changes in many metabolic pathways and caution should be used when interpreting results from these mice as due solely to inhibition of the MPTP. Published by Elsevier Ltd.

Proton-Coupled Electron Transfer and a Tyrosine-Histidine Pair in a Photosystem II-Inspired β-Hairpin Maquette: Kinetics on the Picosecond Time Scale.

PubMed

Pagba, Cynthia V; McCaslin, Tyler G; Chi, San-Hui; Perry, Joseph W; Barry, Bridgette A

2016-02-25

Photosystem II (PSII) and ribonucleotide reductase employ oxidation and reduction of the tyrosine aromatic ring in radical transport pathways. Tyrosine-based reactions involve either proton-coupled electron transfer (PCET) or electron transfer (ET) alone, depending on the pH and the pKa of tyrosine's phenolic oxygen. In PSII, a subset of the PCET reactions are mediated by a tyrosine-histidine redox-driven proton relay, YD-His189. Peptide A is a PSII-inspired β-hairpin, which contains a single tyrosine (Y5) and histidine (H14). Previous electrochemical characterization indicated that Peptide A conducts a net PCET reaction between Y5 and H14, which have a cross-strand π-π interaction. The kinetic impact of H14 has not yet been explored. Here, we address this question through time-resolved absorption spectroscopy and 280-nm photolysis, which generates a neutral tyrosyl radical. The formation and decay of the neutral tyrosyl radical at 410 nm were monitored in Peptide A and its variant, Peptide C, in which H14 is replaced by cyclohexylalanine (Cha14). Significantly, both electron transfer (ET, pL 11, L = lyonium) and PCET (pL 9) were accelerated in Peptide A and C, compared to model tyrosinate or tyrosine at the same pL. Increased electronic coupling, mediated by the peptide backbone, can account for this rate acceleration. Deuterium exchange gave no significant solvent isotope effect in the peptides. At pL 9, but not at pL 11, the reaction rate decreased when H14 was mutated to Cha14. This decrease in rate is attributed to an increase in reorganization energy in the Cha14 mutant. The Y5-H14 mechanism in Peptide A is reminiscent of proton- and electron-transfer events involving YD-H189 in PSII. These results document a mechanism by which proton donors and acceptors can regulate the rate of PCET reactions.

Spectroscopic Characterization of YedY: The Role of Sulfur Coordination in a Mo(V) Sulfite Oxidase Family Enzyme Form

PubMed Central

Yang, Jing; Rothery, Richard; Sempombe, Joseph

2011-01-01

Electronic paramagnetic resonance, electronic absorption, and magnetic circular dichroism spectroscopies have been performed on YedY, a SUOX fold protein with a Mo domain that is remarkably similar to that found in chicken sulfite oxidase, A. thaliana plant sulfite oxidase, and the bacterial sulfite dehydrogenase from S. novella. Low-energy dithiolene→Mo and cysteine thiolate→Mo charge transfer bands have been assigned for the first time in a Mo(V) form of a SUOX fold protein, and the spectroscopic data have been used to interpret the results of bonding calculations. The analysis shows that second coordination sphere effects modulate dithiolene and cysteine sulfur covalency contributions to the Mo bonding scheme. Namely, a more acute Ooxo-Mo-SCys-C dihedral angle results in increased cysteine thiolate S→Mo charge transfer and a high g1 in the EPR spectrum. The spectrosocopic results, coupled with the available structural data, indicate that these second coordination sphere effects may play key roles in modulating the active site redox potential, facilitating hole superexchange pathways for electron transfer regeneration, and affecting the type of reactions catalyzed by sulfite oxidase family enzymes. PMID:19860477

Potential for direct interspecies electron transfer in an electric-anaerobic system to increase methane production from sludge digestion.

PubMed

Zhao, Zhiqiang; Zhang, Yaobin; Wang, Liying; Quan, Xie

2015-06-09

Direct interspecies electron transfer (DIET) between Geobacter species and Methanosaeta species is an alternative to interspecies hydrogen transfer (IHT) in anaerobic digester, which however has not been established in anaerobic sludge digestion as well as in bioelectrochemical systems yet. In this study, it was found that over 50% of methane production of an electric-anaerobic sludge digester was resulted from unknown pathway. Pyrosequencing analysis revealed that Geobacter species were significantly enriched with electrodes. Fluorescence in situ hybridization (FISH) further confirmed that the dominant Geobacter species enriched belonged to Geobacter metallireducens. Together with Methanosaeta species prevailing in the microbial communities, the direct electron exchange between Geobacter species and Methanosaeta species might be an important reason for the "unknown" increase of methane production. Conductivity of the sludge in this electric-anaerobic digester was about 30% higher than that of the sludge in a control digester without electrodes. This study not only revealed for the first time that DIET might be the important mechanism on the methanogenesis of bioelectrochemical system, but also provided a new method to enhance DIET by means of bioelectric enrichment of Geobacter species.

Potential for direct interspecies electron transfer in an electric-anaerobic system to increase methane production from sludge digestion

PubMed Central

Zhao, Zhiqiang; Zhang, Yaobin; Wang, Liying; Quan, Xie

2015-01-01

Direct interspecies electron transfer (DIET) between Geobacter species and Methanosaeta species is an alternative to interspecies hydrogen transfer (IHT) in anaerobic digester, which however has not been established in anaerobic sludge digestion as well as in bioelectrochemical systems yet. In this study, it was found that over 50% of methane production of an electric-anaerobic sludge digester was resulted from unknown pathway. Pyrosequencing analysis revealed that Geobacter species were significantly enriched with electrodes. Fluorescence in situ hybridization (FISH) further confirmed that the dominant Geobacter species enriched belonged to Geobacter metallireducens. Together with Methanosaeta species prevailing in the microbial communities, the direct electron exchange between Geobacter species and Methanosaeta species might be an important reason for the “unknown” increase of methane production. Conductivity of the sludge in this electric-anaerobic digester was about 30% higher than that of the sludge in a control digester without electrodes. This study not only revealed for the first time that DIET might be the important mechanism on the methanogenesis of bioelectrochemical system, but also provided a new method to enhance DIET by means of bioelectric enrichment of Geobacter species. PMID:26057581

Cell-secreted flavins bound to membrane cytochromes dictate electron transfer reactions to surfaces with diverse charge and pH.

PubMed

Okamoto, Akihiro; Kalathil, Shafeer; Deng, Xiao; Hashimoto, Kazuhito; Nakamura, Ryuhei; Nealson, Kenneth H

2014-07-11

The variety of solid surfaces to and from which microbes can deliver electrons by extracellular electron transport (EET) processes via outer-membrane c-type cytochromes (OM c-Cyts) expands the importance of microbial respiration in natural environments and industrial applications. Here, we demonstrate that the bifurcated EET pathway of OM c-Cyts sustains the diversity of the EET surface in Shewanella oneidensis MR-1 via specific binding with cell-secreted flavin mononucleotide (FMN) and riboflavin (RF). Microbial current production and whole-cell differential pulse voltammetry revealed that RF and FMN enhance EET as bound cofactors in a similar manner. Conversely, FMN and RF were clearly differentiated in the EET enhancement by gene-deletion of OM c-Cyts and the dependency of the electrode potential and pH. These results indicate that RF and FMN have specific binding sites in OM c-Cyts and highlight the potential roles of these flavin-cytochrome complexes in controlling the rate of electron transfer to surfaces with diverse potential and pH.

Electronic structural dependence of the photophysical properties of fluorescent heteroditopic ligands - implications in designing molecular fluorescent indicators.

PubMed

Younes, Ali H; Zhang, Lu; Clark, Ronald J; Davidson, Michael W; Zhu, Lei

2010-12-07

Two fluorescent heteroditopic ligands (2a and 2b) for zinc ion were synthesized and studied. The efficiencies of two photophysical processes, intramolecular charge transfer (ICT) and photoinduced electron transfer (PET), determine the magnitudes of emission bathochromic shift and enhancement, respectively, when a heteroditopic ligand forms mono- or dizinc complexes. The electron-rich 2b is characterized by a high degree of ICT in the excited state with little propensity for PET, which is manifested in a large bathochromic shift of emission upon Zn(2+) coordination without enhancement in fluorescence quantum yield. The electron-poor 2a displays the opposite photophysical consequence where Zn(2+) binding results in greatly enhanced emission without significant spectral shift. The electronic structural effects on the relative efficiencies of ICT and PET in 2a and 2b as well as the impact of Zn(2+)-coordination are probed using experimental and computational approaches. This study reveals that the delicate balance between various photophysical pathways (e.g. ICT and PET) engineered in a heteroditopic ligand is sensitively dependent on the electronic structure of the ligand, i.e. whether the fluorophore is electron-rich or poor, whether it possesses a donor-acceptor type of structure, and where the metal binding occurs.

An Inner Membrane Cytochrome Required Only for Reduction of High Redox Potential Extracellular Electron Acceptors

PubMed Central

Levar, Caleb E.; Chan, Chi Ho; Mehta-Kolte, Misha G.

2014-01-01

ABSTRACT Dissimilatory metal-reducing bacteria, such as Geobacter sulfurreducens, transfer electrons beyond their outer membranes to Fe(III) and Mn(IV) oxides, heavy metals, and electrodes in electrochemical devices. In the environment, metal acceptors exist in multiple chelated and insoluble forms that span a range of redox potentials and offer different amounts of available energy. Despite this, metal-reducing bacteria have not been shown to alter their electron transfer strategies to take advantage of these energy differences. Disruption of imcH, encoding an inner membrane c-type cytochrome, eliminated the ability of G. sulfurreducens to reduce Fe(III) citrate, Fe(III)-EDTA, and insoluble Mn(IV) oxides, electron acceptors with potentials greater than 0.1 V versus the standard hydrogen electrode (SHE), but the imcH mutant retained the ability to reduce Fe(III) oxides with potentials of ≤−0.1 V versus SHE. The imcH mutant failed to grow on electrodes poised at +0.24 V versus SHE, but switching electrodes to −0.1 V versus SHE triggered exponential growth. At potentials of ≤−0.1 V versus SHE, both the wild type and the imcH mutant doubled 60% slower than at higher potentials. Electrodes poised even 100 mV higher (0.0 V versus SHE) could not trigger imcH mutant growth. These results demonstrate that G. sulfurreducens possesses multiple respiratory pathways, that some of these pathways are in operation only after exposure to low redox potentials, and that electron flow can be coupled to generation of different amounts of energy for growth. The redox potentials that trigger these behaviors mirror those of metal acceptors common in subsurface environments where Geobacter is found. PMID:25425235

An inner membrane cytochrome required only for reduction of high redox potential extracellular electron acceptors

DOE PAGES

Levar, Caleb E.; Chan, Chi Ho; Mehta-Kolte, Misha G.; ...

2014-10-28

Dissimilatory metal-reducing bacteria, such as Geobacter sulfurreducens, transfer electrons beyond their outer membranes to Fe(III) and Mn(IV) oxides, heavy metals, and electrodes in electrochemical devices. In the environment, metal acceptors exist in multiple chelated and insoluble forms that span a range of redox potentials and offer different amounts of available energy. Despite this, metal-reducing bacteria have not been shown to alter their electron transfer strategies to take advantage of these energy differences. Disruption of imcH, encoding an inner membrane c-type cytochrome, eliminated the ability of G. sulfurreducens to reduce Fe(III) citrate, Fe(III)-EDTA, and insoluble Mn(IV) oxides, electron acceptors with potentialsmore » greater than 0.1 V versus the standard hydrogen electrode (SHE), but the imcH mutant retained the ability to reduce Fe(III) oxides with potentials of ≤–0.1 V versus SHE. The imcH mutant failed to grow on electrodes poised at +0.24 V versus SHE, but switching electrodes to –0.1 V versus SHE triggered exponential growth. At potentials of ≤–0.1 V versus SHE, both the wild type and the imcH mutant doubled 60% slower than at higher potentials. Electrodes poised even 100 mV higher (0.0 V versus SHE) could not trigger imcH mutant growth. These results demonstrate that G. sulfurreducens possesses multiple respiratory pathways, that some of these pathways are in operation only after exposure to low redox potentials, and that electron flow can be coupled to generation of different amounts of energy for growth. Redox potentials that trigger these behaviors mirror those of metal acceptors common in subsurface environments where Geobacter is found.« less

Molecular dynamics simulations of the orientation properties of cytochrome c on the surface of single-walled carbon nanotubes.

PubMed

Zhang, Bing; Xu, Jia; Mo, Shu-Fan; Yao, Jian-Xi; Dai, Song-Yuan

2016-12-01

Electron transfer between cytochrome c (Cytc) and electrodes can be influenced greatly by the orientation of protein on the surface of the electrodes. In the present study, different initial orientations of Cytc on the surface of five types of single-walled carbon nanotubes (SWNTs), with different diameters and chirality, were constructed. Properties of the orientations of proteins on the surface of these tubes were first investigated through molecular dynamics simulations. It was shown that variations in SWNT diameter do not significantly affect the orientation; however, the chirality of the SWNTs is crucial to the orientation of the heme embedded in Cytc, and the orientation of the protein can consequently be influenced by the heme orientation. A new electron pathway between Cytc and SWNT, which hopefully benefits electron transfer efficiency, has also been proposed. This study promises to provide theoretical guidance for the rational design of bio-sensors or bio-fuel cells by using Cytc-decorated carbon nanotube electrodes.

How the Number of Layers and Relative Position Modulate the Interlayer Electron Transfer in π-Stacked 2D Materials.

PubMed

Biancardi, Alessandro; Caraiani, Claudiu; Chan, Wai-Lun; Caricato, Marco

2017-04-06

Understanding the interfacial electron transfer (IET) between 2D layers is central to technological applications. We present a first-principles study of the IET between a zinc phthalocyanine film and few-layer graphene by using our recent method for the calculation of electronic coupling in periodic systems. The ultimate goal is the development of a predictive in silico approach for designing new 2D materials. We find IET to be critically dependent on the number of layers and their stacking orientation. In agreement with experiment, IET to single-layer graphene is shown to be faster than that to double-layer graphene due to interference effects between layers. We predict that additional graphene layers increase the number of IET pathways, eventually leading to a faster rate. These results shed new light on the subtle interplay between structure and IET, which may lead to more effective "bottom up" design strategies for these materials.

Electron transport limitation in P3HT:CdSe nanorods hybrid solar cells.

PubMed

Lek, Jun Yan; Xing, Guichuan; Sum, Tze Chien; Lam, Yeng Ming

2014-01-22

Hybrid solar cells have the potential to be efficient solar-energy-harvesting devices that can combine the benefits of solution-processable organic materials and the extended absorption offered by inorganic materials. In this work, an understanding of the factors limiting the performance of hybrid solar cells is explored. Through photovoltaic-device characterization correlated with transient absorption spectroscopy measurements, it was found that the interfacial charge transfer between the organic (P3HT) and inorganic (CdSe nanorods) components is not the factor limiting the performance of these solar cells. The insulating original ligands retard the charge recombination between the charge-transfer states across the CdSe-P3HT interface, and this is actually beneficial for charge collection. These cells are, in fact, limited by the subsequent electron collection via CdSe nanoparticles to the electrodes. Hence, the design of a more continuous electron-transport pathway should greatly improve the performance of hybrid solar cells in the future.

FAD oxidizes the ERO1-PDI electron transfer chain: The role of membrane integrity

DOE Office of Scientific and Technical Information (OSTI.GOV)

Papp, Eszter; Nardai, Gabor; Mandl, Jozsef

2005-12-16

The molecular steps of the electron transfer in the endoplasmic reticulum from the secreted proteins during their oxidation are relatively unknown. We present here that flavine adenine dinucleotide (FAD) is a powerful oxidizer of the oxidoreductase system, Ero1 and PDI, besides the proteins of rat liver microsomes and HepG2 hepatoma cells. Inhibition of FAD transport hindered the action of FAD. Microsomal membrane integrity was mandatory for all FAD-related oxidation steps downstream of Ero1. The PDI inhibitor bacitracin could inhibit FAD-mediated oxidation of microsomal proteins and PDI, but did not hinder the FAD-driven oxidation of Ero1. Our data demonstrated that Ero1more » can utilize FAD as an electron acceptor and that FAD-driven protein oxidation goes through the Ero1-PDI pathway and requires the integrity of the endoplasmic reticulum membrane. Our findings prompt further studies to elucidate the membrane-dependent steps of PDI oxidation and the role of FAD in redox folding.« less

Selective Electrocatalytic Reduction of Nitrite to Dinitrogen Based on Decoupled Proton-Electron Transfer.

PubMed

He, Daoping; Li, Yamei; Ooka, Hideshi; Go, Yoo Kyung; Jin, Fangming; Kim, Sun Hee; Nakamura, Ryuhei

2018-02-14

The development of denitrification catalysts which can reduce nitrate and nitrite to dinitrogen is critical for sustaining the nitrogen cycle. However, regulating the selectivity has proven to be a challenge, due to the difficulty of controlling complex multielectron/proton reactions. Here we report that utilizing sequential proton-electron transfer (SPET) pathways is a viable strategy to enhance the selectivity of electrochemical reactions. The selectivity of an oxo-molybdenum sulfide electrocatalyst toward nitrite reduction to dinitrogen exhibited a volcano-type pH dependence with a maximum at pH 5. The pH-dependent formation of the intermediate species (distorted Mo(V) oxo species) identified using operando electron paramagnetic resonance (EPR) and Raman spectroscopy was in accord with a mathematical prediction that the pK a of the reaction intermediates determines the pH-dependence of the SPET-derived product. By utilizing this acute pH dependence, we achieved a Faradaic efficiency of 13.5% for nitrite reduction to dinitrogen, which is the highest value reported to date under neutral conditions.

Ultraviolet Absorption Induces Hydrogen-Atom Transfer in G⋅C Watson-Crick DNA Base Pairs in Solution.

PubMed

Röttger, Katharina; Marroux, Hugo J B; Grubb, Michael P; Coulter, Philip M; Böhnke, Hendrik; Henderson, Alexander S; Galan, M Carmen; Temps, Friedrich; Orr-Ewing, Andrew J; Roberts, Gareth M

2015-12-01

Ultrafast deactivation pathways bestow photostability on nucleobases and hence preserve the structural integrity of DNA following absorption of ultraviolet (UV) radiation. One controversial recovery mechanism proposed to account for this photostability involves electron-driven proton transfer (EDPT) in Watson-Crick base pairs. The first direct observation is reported of the EDPT process after UV excitation of individual guanine-cytosine (G⋅C) Watson-Crick base pairs by ultrafast time-resolved UV/visible and mid-infrared spectroscopy. The formation of an intermediate biradical species (G[-H]⋅C[+H]) with a lifetime of 2.9 ps was tracked. The majority of these biradicals return to the original G⋅C Watson-Crick pairs, but up to 10% of the initially excited molecules instead form a stable photoproduct G*⋅C* that has undergone double hydrogen-atom transfer. The observation of these sequential EDPT mechanisms across intermolecular hydrogen bonds confirms an important and long debated pathway for the deactivation of photoexcited base pairs, with possible implications for the UV photochemistry of DNA. © 2015 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

In vitro metabolic engineering of bioelectricity generation by the complete oxidation of glucose.

PubMed

Zhu, Zhiguang; Zhang, Y-H Percival

2017-01-01

The direct generation of electricity from the most abundant renewable sugar, glucose, is an appealing alternative to the production of liquid biofuels and biohydrogen. However, enzyme-catalyzed bioelectricity generation from glucose suffers from low yields due to the incomplete oxidation of the six-carbon compound glucose via one or few enzymes. Here, we demonstrate a synthetic ATP- and CoA-free 12-enzyme pathway to implement the complete oxidation of glucose in vitro. This pathway is comprised of glucose phosphorylation via polyphosphate glucokinase, NADH generation catalyzed by glucose 6-phosphate dehydrogenase (G6PDH) and 6-phosphogluconate dehydrogenase (6PGDH), electron transfer from NADH to the anode, and glucose 6-phosphate regeneration via the non-oxidative pentose phosphate pathway and gluconeogenesis. The faraday efficiency from glucose to electrons via this pathway was as high as 98.8%, suggesting the generation of nearly 24 electrons per molecule of glucose. The generated current density was greatly increased from 2.8 to 6.9mAcm -2 by replacing a low-activity G6PDH with a high-activity G6PDH and introducing a new enzyme, 6-phosphogluconolactonase, between G6PDH and 6PGDH. These results suggest the great potential of high-yield bioelectricity generation through in vitro metabolic engineering. Copyright © 2016 International Metabolic Engineering Society. Published by Elsevier Inc. All rights reserved.

Quantitative structure-activity relationships for reactivities of sulfate and hydroxyl radicals with aromatic contaminants through single-electron transfer pathway.

PubMed

Luo, Shuang; Wei, Zongsu; Spinney, Richard; Villamena, Frederick A; Dionysiou, Dionysios D; Chen, Dong; Tang, Chong-Jian; Chai, Liyuan; Xiao, Ruiyang

2018-02-15

Sulfate radical anion (SO 4 •- ) and hydroxyl radical (OH) based advanced oxidation technologies has been extensively used for removal of aromatic contaminants (ACs) in waters. In this study, we investigated the Gibbs free energy (ΔG SET ∘ ) of the single electron transfer (SET) reactions for 76 ACs with SO 4 •- and OH, respectively. The result reveals that SO 4 •- possesses greater propensity to react with ACs through the SET channel than OH. We hypothesized that the electron distribution within the molecule plays an essential role in determining the ΔG SET ∘ and subsequent SET reactions. To test the hypothesis, a quantitative structure-activity relationship (QSAR) model was developed for predicting ΔG SET ∘ using the highest occupied molecular orbital energies (E HOMO ), a measure of electron distribution and donating ability. The standardized QSAR models are reported to be ΔG ° SET =-0.97×E HOMO - 181 and ΔG ° SET =-0.97×E HOMO - 164 for SO 4 •- and OH, respectively. The models were internally and externally validated to ensure robustness and predictability, and the application domain and limitations were discussed. The single-descriptor based models account for 95% of the variability for SO 4 •- and OH. These results provide the mechanistic insight into the SET reaction pathway of radical and non-radical bimolecular reactions, and have important applications for radical based oxidation technologies to remove target ACs in different waters. Copyright © 2017 Elsevier B.V. All rights reserved.

Reactivity index based on orbital energies.

PubMed

Tsuneda, Takao; Singh, Raman K

2014-05-30

This study shows that the chemical reactivities depend on the orbital energy gaps contributing to the reactions. In the process where a reaction only makes progress through charge transfer with the minimal structural transformation of the reactant, the orbital energy gap gradient (OEGG) between the electron-donating and electron-accepting orbitals is proven to be very low. Using this relation, a normalized reaction diagram is constructed by plotting the normalized orbital energy gap with respect to the normalized intrinsic reaction coordinate. Application of this reaction diagram to 43 fundamental reactions showed that the majority of the forward reactions provide small OEGGs in the initial stages, and therefore, the initial processes of the forward reactions are supposed to proceed only through charge transfer. Conversely, more than 60% of the backward reactions are found to give large OEGGs implying very slow reactions associated with considerable structural transformations. Focusing on the anti-activation-energy reactions, in which the forward reactions have higher barriers than those of the backward ones, most of these reactions are shown to give large OEGGs for the backward reactions. It is also found that the reactions providing large OEGGs in the forward directions inconsistent with the reaction rate constants are classified into SN 2, symmetric, and methyl radical reactions. Interestingly, several large-OEGG reactions are experimentally established to get around the optimum pathways. This indicates that the reactions can take significantly different pathways from the optimum ones provided no charge transfer proceeds spontaneously without the structural transformations of the reactants. Copyright © 2014 Wiley Periodicals, Inc.

CRISPRi-sRNA: Transcriptional-Translational Regulation of Extracellular Electron Transfer in Shewanella oneidensis.

PubMed

Cao, Yingxiu; Li, Xiaofei; Li, Feng; Song, Hao

2017-09-15

Extracellular electron transfer (EET) in Shewanella oneidensis MR-1, which is one of the most well-studied exoelectrogens, underlies many microbial electrocatalysis processes, including microbial fuel cells, microbial electrolysis cells, and microbial electrosynthesis. However, regulating the efficiency of EET remains challenging due to the lack of efficient genome regulation tools that regulate gene expression levels in S. oneidensis. Here, we systematically established a transcriptional regulation technology, i.e., clustered regularly interspaced short palindromic repeats interference (CRISPRi), in S. oneidensis MR-1 using green fluorescent protein (GFP) as a reporter. We used this CRISPRi technology to repress the expression levels of target genes, individually and in combination, in the EET pathways (e.g., the MtrCAB pathway and genes affecting the formation of electroactive biofilms in S. oneidensis), which in turn enabled the efficient regulation of EET efficiency. We then established a translational regulation technology, i.e., Hfq-dependent small regulatory RNA (sRNA), in S. oneidensis by repressing the GFP reporter and mtrA, which is a critical gene in the EET pathways in S. oneidensis. To achieve coordinated transcriptional and translational regulation at the genomic level, the CRISPRi and Hfq-dependent sRNA systems were incorporated into a single plasmid harbored in a recombinant S. oneidensis strain, which enabled an even higher efficiency of mtrA gene repression in the EET pathways than that achieved by the CRISPRi and Hfq-dependent sRNA system alone, as exhibited by the reduced electricity output. Overall, we developed a combined CRISPRi-sRNA method that enabled the synergistic transcriptional and translational regulation of target genes in S. oneidensis. This technology involving CRISPRi-sRNA transcriptional-translational regulation of gene expression at the genomic level could be applied to other microorganisms.

The Importance of Transition Metals in the Expanding Network of Microbial Metabolism in the Archean Eon

NASA Astrophysics Data System (ADS)

Moore, E. K.; Jelen, B. I.; Giovannelli, D.; Prabhu, A.; Raanan, H.; Falkowski, P. G.

2017-12-01

Deep time changes in Earth surface redox conditions, particularly due to global oxygenation, has impacted the availability of different metals and substrates that are central in biology. Oxidoreductase proteins are molecular nanomachines responsible for all biological electron transfer processes across the tree of life. These enzymes largely contain transition metals in their active sites. Microbial metabolic pathways form a global network of electron transfer, which expanded throughout the Archean eon. Older metabolisms (sulfur reduction, methanogenesis, anoxygenic photosynthesis) accessed negative redox potentials, while later evolving metabolisms (oxygenic photosynthesis, nitrification/denitrification, aerobic respiration) accessed positive redox potentials. The incorporation of different transition metals facilitated biological innovation and the expansion of the network of microbial metabolism. Network analysis was used to examine the connections between microbial taxa, metabolic pathways, crucial metallocofactors, and substrates in deep time by incorporating biosignatures preserved in the geologic record. Nitrogen fixation and aerobic respiration have the highest level of betweenness among metabolisms in the network, indicating that the oldest metabolisms are not the most central. Fe has by far the highest betweenness among metals. Clustering analysis largely separates High Metal Bacteria (HMB), Low Metal Bacteria (LMB), and Archaea showing that simple un-weighted links between taxa, metabolism, and metals have phylogenetic relevance. On average HMB have the highest betweenness among taxa, followed by Archaea and LMB. There is a correlation between the number of metallocofactors and metabolic pathways in representative bacterial taxa, but Archaea do not follow this trend. In many cases older and more recently evolved metabolisms were clustered together supporting previous findings that proliferation of metabolic pathways is not necessarily chronological.

Directional charge transfer mediated by mid-gap states: A transient absorption spectroscopy study of CdSe quantum dot/β-Pb 0.33V 2O 5 heterostructures

DOE PAGES

Milleville, Christopher C.; Pelcher, Kate E.; Sfeir, Matthew Y.; ...

2016-02-15

For solar energy conversion, not only must a semiconductor absorb incident solar radiation efficiently but also its photoexcited electron—hole pairs must further be separated and transported across interfaces. Charge transfer across interfaces requires consideration of both thermodynamic driving forces as well as the competing kinetics of multiple possible transfer, cooling, and recombination pathways. In this work, we demonstrate a novel strategy for extracting holes from photoexcited CdSe quantum dots (QDs) based on interfacing with β-Pb 0.33V 2O 5 nanowires that have strategically positioned midgap states derived from the intercalating Pb 2+ ions. Unlike midgap states derived from defects or dopants,more » the states utilized here are derived from the intrinsic crystal structure and are thus homogeneously distributed across the material. CdSe/β-Pb 0.33V 2O 5 heterostructures were assembled using two distinct methods: successive ionic layer adsorption and reaction (SILAR) and linker-assisted assembly (LAA). Transient absorption spectroscopy measurements indicate that, for both types of heterostructures, photoexcitation of CdSe QDs was followed by the transfer of electrons to the conduction band of β-Pb 0.33V 2O 5 nanowires and holes to the midgap states of β-Pb 0.33V 2O 5 nanowires. Holes were transferred on time scales less than 1 ps, whereas electrons were transferred more slowly on time scales of ~2 ps. In contrast, for analogous heterostructures consisting of CdSe QDs interfaced with V 2O 5 nanowires (wherein midgap states are absent), only electron transfer was observed. Interestingly, electron transfer was readily achieved for CdSe QDs interfaced with V 2O 5 nanowires by the SILAR method; however, for interfaces incorporating molecular linkers, electron transfer was observed only upon excitation at energies substantially greater than the bandgap absorption threshold of CdSe. Furthermore, transient absorbance decay traces reveal longer excited-state lifetimes (1–3 μs) for CdSe/β-Pb 0.33V 2O 5 heterostructures relative to bare β-Pb 0.33V 2O 5 nanowires (0.2 to 0.6 μs); the difference is attributed to surface passivation of intrinsic surface defects in β-Pb 0.33V 2O 5 upon interfacing with CdSe.« less

Inhibition of melanosome transfer results in skin lightening.

PubMed

Seiberg, M; Paine, C; Sharlow, E; Andrade-Gordon, P; Costanzo, M; Eisinger, M; Shapiro, S S

2000-08-01

The chemical basis of melanogenesis is well documented, but the mechanism of melanosome transfer and the regulation of pigmentation by keratinocyte-melanocyte interactions are not well understood. Therefore we examined the effects of serine protease inhibitors on skin pigmentation and found that the protease-activated receptor 2, expressed on keratinocytes, may regulate pigmentation via keratinocyte-melanocyte interactions. Here we show that modulation of protease-activated receptor 2 activation affects melanosome transfer into keratinocytes, resulting in changes in pigment production and deposition. SLIGRL, the protease-activated receptor 2 activating peptide, enhanced melanosome ingestion by keratinocytes, thus increasing pigment deposition. RWJ-50353, a serine protease inhibitor, led to reduced pigment deposition in melanocytes and depigmentation. Electron microscopy studies illustrated an accumulation of immature melanosomes inside melanocytes and abnormal dendrite dynamics in RWJ-50353-treated epidermal equivalents. RWJ-50353 induced a visible and dose-dependent skin lightening effect in the dark-skinned Yucatan swine. Examinations by electron microscopy indicated that the in vivo transfer of melanosomes from melanocytes to keratinocytes was affected. Our data suggest that modulation of keratinocyte-melanocyte interactions via the protease-activated receptor 2 pathway affects melanosome transfer. The use of RWJ-50353 to modulate protease-activated receptor 2 activation could lead to a new class of depigmenting agents.

Interfacial hydration, dynamics and electron transfer: multi-scale ET modeling of the transient [myoglobin, cytochrome b5] complex.

PubMed

Keinan, Shahar; Nocek, Judith M; Hoffman, Brian M; Beratan, David N

2012-10-28

Formation of a transient [myoglobin (Mb), cytochrome b(5) (cyt b(5))] complex is required for the reductive repair of inactive ferri-Mb to its functional ferro-Mb state. The [Mb, cyt b(5)] complex exhibits dynamic docking (DD), with its cyt b(5) partner in rapid exchange at multiple sites on the Mb surface. A triple mutant (Mb(3M)) was designed as part of efforts to shift the electron-transfer process to the simple docking (SD) regime, in which reactive binding occurs at a restricted, reactive region on the Mb surface that dominates the docked ensemble. An electrostatically-guided brownian dynamics (BD) docking protocol was used to generate an initial ensemble of reactive configurations of the complex between unrelaxed partners. This ensemble samples a broad and diverse array of heme-heme distances and orientations. These configurations seeded all-atom constrained molecular dynamics simulations (MD) to generate relaxed complexes for the calculation of electron tunneling matrix elements (T(DA)) through tunneling-pathway analysis. This procedure for generating an ensemble of relaxed complexes combines the ability of BD calculations to sample the large variety of available conformations and interprotein distances, with the ability of MD to generate the atomic level information, especially regarding the structure of water molecules at the protein-protein interface, that defines electron-tunneling pathways. We used the calculated T(DA) values to compute ET rates for the [Mb(wt), cyt b(5)] complex and for the complex with a mutant that has a binding free energy strengthened by three D/E → K charge-reversal mutations, [Mb(3M), cyt b(5)]. The calculated rate constants are in agreement with the measured values, and the mutant complex ensemble has many more geometries with higher T(DA) values than does the wild-type Mb complex. Interestingly, water plays a double role in this electron-transfer system, lowering the tunneling barrier as well as inducing protein interface remodeling that screens the repulsion between the negatively-charged propionates of the two hemes.

Rapid Characterization of Bacterial Electrogenicity Using a Single-Sheet Paper-Based Electrofluidic Array

PubMed Central

Gao, Yang; Hassett, Daniel J.; Choi, Seokheun

2017-01-01

Electrogenicity, or bacterial electron transfer capacity, is an important application which offers environmentally sustainable advances in the fields of biofuels, wastewater treatment, bioremediation, desalination, and biosensing. Significant boosts in this technology can be achieved with the growth of synthetic biology that manipulates microbial electron transfer pathways, thereby potentially significantly improving their electrogenic potential. There is currently a need for a high-throughput, rapid, and highly sensitive test array to evaluate the electrogenic properties of newly discovered and/or genetically engineered bacterial species. In this work, we report a single-sheet, paper-based electrofluidic (incorporating both electronic and fluidic structure) screening platform for rapid, sensitive, and potentially high-throughput characterization of bacterial electrogenicity. This novel screening array uses (i) a commercially available wax printer for hydrophobic wax patterning on a single sheet of paper and (ii) water-dispersed electrically conducting polymer mixture, poly(3,4-ethylenedioxythiophene):polystyrene sulfonate, for full integration of electronic and fluidic components into the paper substrate. The engineered 3-D, microporous, hydrophilic, and conductive paper structure provides a large surface area for efficient electron transfer. This results in rapid and sensitive power assessment of electrogenic bacteria from a microliter sample volume. We validated the effectiveness of the sensor array using hypothesis-driven genetically modified Pseudomonas aeruginosa mutant strains. Within 20 min, we observed that the sensor platform successfully measured the electricity-generating capacities of five isogenic mutants of P. aeruginosa while distinguishing their differences from genetically unmodified bacteria. PMID:28798914

Direct determination of resonance energy transfer in photolyase: structural alignment for the functional state.

PubMed

Tan, Chuang; Guo, Lijun; Ai, Yuejie; Li, Jiang; Wang, Lijuan; Sancar, Aziz; Luo, Yi; Zhong, Dongping

2014-11-13

Photoantenna is essential to energy transduction in photoinduced biological machinery. A photoenzyme, photolyase, has a light-harvesting pigment of methenyltetrahydrofolate (MTHF) that transfers its excitation energy to the catalytic flavin cofactor FADH¯ to enhance DNA-repair efficiency. Here we report our systematic characterization and direct determination of the ultrafast dynamics of resonance energy transfer from excited MTHF to three flavin redox states in E. coli photolyase by capturing the intermediates formed through the energy transfer and thus excluding the electron-transfer quenching pathway. We observed 170 ps for excitation energy transferring to the fully reduced hydroquinone FADH¯, 20 ps to the fully oxidized FAD, and 18 ps to the neutral semiquinone FADH(•), and the corresponding orientation factors (κ(2)) were determined to be 2.84, 1.53 and 1.26, respectively, perfectly matching with our calculated theoretical values. Thus, under physiological conditions and over the course of evolution, photolyase has adopted the optimized orientation of its photopigment to efficiently convert solar energy for repair of damaged DNA.

Long-Range Superexchange in Electron Transport Proteins

NASA Astrophysics Data System (ADS)

Gruschus, James Michael

A new Hamiltonian model for the calculation of long-range electronic couplings in complex molecular systems is presented. These couplings make possible the electron transfers occurring at several critical steps in photosynthesis and respiration. The couplings studied are demonstrated to arise from a mechanism known as superexchange, where the electrons of the insulating medium are intimately involved in the delocalization of the donor wavefunction tail, allowing significant interaction with the acceptor at much greater separations than could be achieved were the medium absent. Superexchange phenomena in molecules of moderate complexity are first compared to couplings calculated with the model Hamiltonian, with very encouraging results. The method is then applied to several cytochrome c proteins where electron transfer has been measured between a zinc-substituted porphyrin and a ruthenium complex ligated to several sites at the protein surface. The calculated couplings are in unprecedented agreement with experiment. Novel, analytical derivatives of the superexchange coupling with respect to the orbital energies and interactions are then carried out on these proteins yielding the general, chemically relevant result that the entire three-dimensional zone between redox sites is important in mediating the superexchange coupling, in contrast to the prevailing assumption that the coupling can be characterized by a one-dimensional pathway consisting primarily of chains of bonded atoms. In addition, the derivatives provide the most comprehensive ever, atom-by -atom visualization of the superexchange process. Using AMBER molecular dynamics trajectories of the cytochrome c proteins, the effect of structural fluctuations on superexchange is examined. The calculated couplings show a substantial variability, a result contrary to the constant coupling implicit in most present-day transfer rate theory. Couplings are also calculated on surfaces enveloping several variants of cytochrome c, as well as plastocyanin, cytochrome b _5, and cytochrome c peroxidase. The surfaces reveal important clues as to which conformations of the electron transport protein complexes actually give rise to electron transfer, a subject of broad biological interest.

Alteration of intracellular protein expressions as a key mechanism of the deterioration of bacterial denitrification caused by copper oxide nanoparticles.

PubMed

Su, Yinglong; Zheng, Xiong; Chen, Yinguang; Li, Mu; Liu, Kun

2015-10-28

The increasing production and utilization of copper oxide nanoparticles (CuO NPs) result in the releases into the environment. However, the influence of CuO NPs on bacterial denitrification, one of the most important pathways to transform nitrate to dinitrogen in environment, has seldom been studied. Here we reported that CuO NPs caused a significant alteration of key protein expressions of a model denitrifier, Paracoccus denitrificans, leading to severe inhibition to denitrification. Total nitrogen removal efficiency was decreased from 98.3% to 62.1% with the increase of CuO NPs from 0.05 to 0.25 mg/L. Cellular morphology and integrity studies indicated that nanoparticles entered the cells. The proteomic bioinformatics analysis showed that CuO NPs caused regulation of proteins involved in nitrogen metabolism, electron transfer and substance transport. The down-regulation of GtsB protein (responsible for glucose transport) decreased the production of NADH (electron donor for denitrification). Also, the expressions of key electron-transfer proteins (including NADH dehydrogenase and cytochrome) were suppressed by CuO NPs, which adversely affected electrons transfer for denitrification. Further investigation revealed that CuO NPs significantly inhibited the expressions and catalytic activities of nitrate reductase and nitrite reductase. These results provided a fundamental understanding of the negative influences of CuO NPs on bacterial denitrification.

Alteration of intracellular protein expressions as a key mechanism of the deterioration of bacterial denitrification caused by copper oxide nanoparticles

PubMed Central

Su, Yinglong; Zheng, Xiong; Chen, Yinguang; Li, Mu; Liu, Kun

2015-01-01

The increasing production and utilization of copper oxide nanoparticles (CuO NPs) result in the releases into the environment. However, the influence of CuO NPs on bacterial denitrification, one of the most important pathways to transform nitrate to dinitrogen in environment, has seldom been studied. Here we reported that CuO NPs caused a significant alteration of key protein expressions of a model denitrifier, Paracoccus denitrificans, leading to severe inhibition to denitrification. Total nitrogen removal efficiency was decreased from 98.3% to 62.1% with the increase of CuO NPs from 0.05 to 0.25 mg/L. Cellular morphology and integrity studies indicated that nanoparticles entered the cells. The proteomic bioinformatics analysis showed that CuO NPs caused regulation of proteins involved in nitrogen metabolism, electron transfer and substance transport. The down-regulation of GtsB protein (responsible for glucose transport) decreased the production of NADH (electron donor for denitrification). Also, the expressions of key electron-transfer proteins (including NADH dehydrogenase and cytochrome) were suppressed by CuO NPs, which adversely affected electrons transfer for denitrification. Further investigation revealed that CuO NPs significantly inhibited the expressions and catalytic activities of nitrate reductase and nitrite reductase. These results provided a fundamental understanding of the negative influences of CuO NPs on bacterial denitrification. PMID:26508362

Extracting electron transfer coupling elements from constrained density functional theory

DOE Office of Scientific and Technical Information (OSTI.GOV)

Wu Qin; Van Voorhis, Troy

2006-10-28

Constrained density functional theory (DFT) is a useful tool for studying electron transfer (ET) reactions. It can straightforwardly construct the charge-localized diabatic states and give a direct measure of the inner-sphere reorganization energy. In this work, a method is presented for calculating the electronic coupling matrix element (H{sub ab}) based on constrained DFT. This method completely avoids the use of ground-state DFT energies because they are known to irrationally predict fractional electron transfer in many cases. Instead it makes use of the constrained DFT energies and the Kohn-Sham wave functions for the diabatic states in a careful way. Test calculationsmore » on the Zn{sub 2}{sup +} and the benzene-Cl atom systems show that the new prescription yields reasonable agreement with the standard generalized Mulliken-Hush method. We then proceed to produce the diabatic and adiabatic potential energy curves along the reaction pathway for intervalence ET in the tetrathiafulvalene-diquinone (Q-TTF-Q) anion. While the unconstrained DFT curve has no reaction barrier and gives H{sub ab}{approx_equal}17 kcal/mol, which qualitatively disagrees with experimental results, the H{sub ab} calculated from constrained DFT is about 3 kcal/mol and the generated ground state has a barrier height of 1.70 kcal/mol, successfully predicting (Q-TTF-Q){sup -} to be a class II mixed-valence compound.« less

UV excitation of single DNA and RNA strands produces high yields of exciplex states between two stacked bases

PubMed Central

Takaya, Tomohisa; Su, Charlene; de La Harpe, Kimberly; Crespo-Hernández, Carlos E.; Kohler, Bern

2008-01-01

Excited electronic states created by UV excitation of the diribonucleoside monophosphates ApA, ApG, ApC, ApU, and CpG were studied by the femtosecond transient-absorption technique. Bleach recovery signals recorded at 252 nm show that long-lived excited states are formed in all five dinucleosides. The lifetimes of these states exceed those measured in equimolar mixtures of the constituent mononucleotides by one to two orders of magnitude, indicating that electronic coupling between proximal nucleobases dramatically slows the relaxation of excess electronic energy. The decay rates of the long-lived states decrease with increasing energy of the charge-transfer state produced by transferring an electron from one base to another. The charge-transfer character of the long-lived states revealed by this analysis supports their assignment to excimer or exciplex states. Identical bleach recovery signals were seen for ApA, (A)4, and poly(A) at delay times >10 ps after photoexcitation. This indicates that excited states localized on a stack of just two bases are the common trap states independent of the number of stacked nucleotides. The fraction of initial excitations that decay to long-lived exciplex states is approximately equal to the fraction of stacked bases determined by NMR measurements. This supports a model in which excitations associated with two stacked bases decay to exciplex states, whereas excitations in unstacked bases decay via ultrafast internal conversion. These results establish the importance of charge transfer-quenching pathways for UV-irradiated RNA and DNA in room-temperature solution. PMID:18647840

UV excitation of single DNA and RNA strands produces high yields of exciplex states between two stacked bases.

PubMed

Takaya, Tomohisa; Su, Charlene; de La Harpe, Kimberly; Crespo-Hernández, Carlos E; Kohler, Bern

2008-07-29

Excited electronic states created by UV excitation of the diribonucleoside monophosphates ApA, ApG, ApC, ApU, and CpG were studied by the femtosecond transient-absorption technique. Bleach recovery signals recorded at 252 nm show that long-lived excited states are formed in all five dinucleosides. The lifetimes of these states exceed those measured in equimolar mixtures of the constituent mononucleotides by one to two orders of magnitude, indicating that electronic coupling between proximal nucleobases dramatically slows the relaxation of excess electronic energy. The decay rates of the long-lived states decrease with increasing energy of the charge-transfer state produced by transferring an electron from one base to another. The charge-transfer character of the long-lived states revealed by this analysis supports their assignment to excimer or exciplex states. Identical bleach recovery signals were seen for ApA, (A)(4), and poly(A) at delay times >10 ps after photoexcitation. This indicates that excited states localized on a stack of just two bases are the common trap states independent of the number of stacked nucleotides. The fraction of initial excitations that decay to long-lived exciplex states is approximately equal to the fraction of stacked bases determined by NMR measurements. This supports a model in which excitations associated with two stacked bases decay to exciplex states, whereas excitations in unstacked bases decay via ultrafast internal conversion. These results establish the importance of charge transfer-quenching pathways for UV-irradiated RNA and DNA in room-temperature solution.

Long distance electron-transfer mechanism in peptidylglycine alpha-hydroxylating monooxygenase: a perfect fitting for a water bridge.

PubMed

de la Lande, Aurélien; Martí, Sergio; Parisel, Olivier; Moliner, Vicent

2007-09-26

The active sites of copper enzymes have been the subject of many theoretical and experimental investigations from a number of years. Such studies have embraced topics devoted to the modeling of the first coordination sphere at the metallic cations up to the development of biomimetic, or bioinspired, catalytic systems. At least from the theoretical viewpoint, fewer efforts have been dedicated to elucidate how the two copper cations act concertedly in noncoupled dicopper enzymes such as peptidylglycine alpha-hydroxylating monooxygenase (PHM) and dopamine beta-monooxygenase (DbetaM). In these metalloenzymes, an electronic transfer is assumed between the two distant copper cations (11 A). Recent experimental results suggest that this transfer occurs through water molecules, a phenomenon which has been theoretically evidenced to be of high efficiency in the case of cytochrome b5 (Science, 2005, 310, 1311). In the present contribution dedicated to PHM, we overpass the common theoretical approaches dedicated to the electronic and geometrical structures of sites CuM or CuH restricted to their first coordination spheres and aim at directly comparing theoretical results to the experimentally measured activity of the PHM enzyme. To achieve this goal, molecular dynamics simulations were performed on wild-type and various mutants of PHM. More precisely, we provide an estimate of the electron-transfer efficiency between the CuM and CuH sites by means of such molecular dynamics simulations coupled to Marcus theory joined to the Beratan model to approximate the required coupling matrix elements. The theoretical results are compared to the kinetics measurements performed on wild and mutated PHM. The present work, the dynamic aspects of which are essential, accounts for the experimental results issued from mutagenesis. It supports the conclusion that an electronic transfer can occur between two copper(I) sites along a bridge involving a set of hydrogen and chemical bonds. Residue Gln170 is evidenced to be the keystone of this water-mediated pathway.

Ultrafast Spin Crossover in [FeII (bpy)3 ]2+ : Revealing Two Competing Mechanisms by Extreme Ultraviolet Photoemission Spectroscopy.

PubMed

Moguilevski, Alexandre; Wilke, Martin; Grell, Gilbert; Bokarev, Sergey I; Aziz, Saadullah G; Engel, Nicholas; Raheem, Azhr A; Kühn, Oliver; Kiyan, Igor Yu; Aziz, Emad F

2017-03-03

Photoinduced spin-flip in Fe II complexes is an ultrafast phenomenon that has the potential to become an alternative to conventional processing and magnetic storage of information. Following the initial excitation by visible light into the singlet metal-to-ligand charge-transfer state, the electronic transition to the high-spin quintet state may undergo different pathways. Here we apply ultrafast XUV (extreme ultraviolet) photoemission spectroscopy to track the low-to-high spin dynamics in the aqueous iron tris-bipyridine complex, [Fe(bpy) 3 ] 2+ , by monitoring the transient electron density distribution among excited states with femtosecond time resolution. Aided by first-principles calculations, this approach enables us to reveal unambiguously both the sequential and direct de-excitation pathways from singlet to quintet state, with a branching ratio of 4.5:1. © 2017 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.

Rapid Dye Regeneration Mechanism of Dye-Sensitized Solar Cells.

PubMed

Jeon, Jiwon; Park, Young Choon; Han, Sang Soo; Goddard, William A; Lee, Yoon Sup; Kim, Hyungjun

2014-12-18

During the light-harvesting process of dye-sensitized solar cells (DSSCs), the hole localized on the dye after the charge separation yields an oxidized dye, D(+). The fast regeneration of D(+) using the redox pair (typically the I(-)/I3(-) couple) is critical for the efficient DSSCs. However, the kinetic processes of dye regeneration remain uncertain, still promoting vigorous debates. Here, we use molecular dynamics simulations to determine that the inner-sphere electron-transfer pathway provides a rapid dye regeneration route of ∼4 ps, where penetration of I(-) next to D(+) enables an immediate electron transfer, forming a kinetic barrier. This explains the recently reported ultrafast dye regeneration rate of a few picoseconds determined experimentally. We expect that our MD based comprehensive understanding of the dye regeneration mechanism will provide a helpful guideline in designing TiO2-dye-electrolyte interfacial systems for better performing DSSCs.

Biological construction of single-walled carbon nanotube electron transfer pathways in dye-sensitized solar cells.

PubMed

Inoue, Ippei; Watanabe, Kiyoshi; Yamauchi, Hirofumi; Ishikawa, Yasuaki; Yasueda, Hisashi; Uraoka, Yukiharu; Yamashita, Ichiro

2014-10-01

We designed and mass-produced a versatile protein supramolecule that can be used to manufacture a highly efficient dye-sensitized solar cell (DSSC). Twelve single-walled carbon-nanotube (SWNT)-binding and titanium-mineralizing peptides were genetically integrated on a cage-shaped dodecamer protein (CDT1). A process involving simple mixing of highly conductive SWNTs with CDT1 followed by TiO2 biomineralization produces a high surface-area/weight TiO2 -(anatase)-coated intact SWNT nanocomposite under environmentally friendly conditions. A DSSC with a TiO2 photoelectrode containing 0.2 wt % of the SWNT-TiO2 nanocomposite shows a current density improvement by 80% and a doubling of the photoelectric conversion efficiency. The SWNT-TiO2 nanocomposite transfers photon-generated electrons from dye molecules adsorbed on the TiO2 to the anode electrode swiftly. © 2014 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

Photoinduced electron transfer pathways in hydrogen-evolving reduced graphene oxide-boosted hybrid nano-bio catalyst.

PubMed

Wang, Peng; Dimitrijevic, Nada M; Chang, Angela Y; Schaller, Richard D; Liu, Yuzi; Rajh, Tijana; Rozhkova, Elena A

2014-08-26

Photocatalytic production of clean hydrogen fuels using water and sunlight has attracted remarkable attention due to the increasing global energy demand. Natural and synthetic dyes can be utilized to sensitize semiconductors for solar energy transformation using visible light. In this study, reduced graphene oxide (rGO) and a membrane protein bacteriorhodopsin (bR) were employed as building modules to harness visible light by a Pt/TiO2 nanocatalyst. Introduction of the rGO boosts the nano-bio catalyst performance that results in hydrogen production rates of approximately 11.24 mmol of H2 (μmol protein)(-1) h(-1). Photoelectrochemical measurements show a 9-fold increase in photocurrent density when TiO2 electrodes were modified with rGO and bR. Electron paramagnetic resonance and transient absorption spectroscopy demonstrate an interfacial charge transfer from the photoexcited rGO to the semiconductor under visible light.

Electronic Energy Transfer in New Polymer Nanocomposite Assemblies

DTIC Science & Technology

1994-07-13

for public release and sale; its distribution is unlimited. OL AISTfrRACT fMaimunt 20o war*) New light-harvesting thin film supramolecular assemblies...be supression or reduction of exciplex formation between excited donor molecules and ground state acceptor molecules that may lead to nonradiative...nonradiative excited state decay exists other than EET.33 One possibility for this nonradiative and non-EET pathway is exciplex formation between the

Malate-aspartate shuttle and exogenous NADH/cytochrome c electron transport pathway as two independent cytosolic reducing equivalent transfer systems.

PubMed

Abbrescia, Daniela Isabel; La Piana, Gianluigi; Lofrumento, Nicola Elio

2012-02-15

In mammalian cells aerobic oxidation of glucose requires reducing equivalents produced in glycolytic phase to be channelled into the phosphorylating respiratory chain for the reduction of molecular oxygen. Data never presented before show that the oxidation rate of exogenous NADH supported by the malate-aspartate shuttle system (reconstituted in vitro with isolated liver mitochondria) is comparable to the rate obtained on activation of the cytosolic NADH/cytochrome c electron transport pathway. The activities of these two reducing equivalent transport systems are independent of each other and additive. NADH oxidation induced by the malate-aspartate shuttle is inhibited by aminooxyacetate and by rotenone and/or antimycin A, two inhibitors of the respiratory chain, while the NADH/cytochrome c system remains insensitive to all of them. The two systems may simultaneously or mutually operate in the transfer of reducing equivalents from the cytosol to inside the mitochondria. In previous reports we suggested that the NADH/cytochrome c system is expected to be functioning in apoptotic cells characterized by the presence of cytochrome c in the cytosol. As additional new finding the activity of reconstituted shuttle system is linked to the amount of α-ketoglutarate generated inside the mitochondria by glutamate dehydrogenase rather than by aspartate aminotransferase. Copyright © 2011 Elsevier Inc. All rights reserved.

Fragment molecular orbital study on electron tunneling mechanisms in bacterial photosynthetic reaction center.

PubMed

Kitoh-Nishioka, Hirotaka; Ando, Koji

2012-11-01

The tunneling mechanisms of electron transfers (ETs) in photosynthetic reaction center of Blastochloris viridis are studied by the ab initio fragment molecular orbital (FMO) method combined with the generalized Mulliken-Hush (GMH) and the bridge Green function (GF) calculations of the electronic coupling T(DA) and the tunneling current method for the ET pathway analysis at the fragment-based resolution. For the ET from batctriopheophytin (H(L)) to menaquinone (MQ), a major tunneling current through Trp M250 and a minor back flow via Ala M215, Ala M216, and His M217 are quantified. For the ET from MQ to ubiquinone, the major tunneling pathway via the nonheme Fe(2+) and His L190 is identified as well as minor pathway via His M217 and small back flows involving His L230, Glu M232, and His M264. At the given molecular structure from X-ray experiment, the spin state of the Fe(2+) ion, its replacement by Zn(2+), or its removal are found to affect the T(DA) value by factors within 2.2. The calculated T(DA) values, together with experimentally estimated values of the driving force and the reorganization energy, give the ET rates in reasonable agreement with experiments.

Exploring Photoinduced Excited State Evolution in Heterobimetallic Ru(II)-Co(III) Complexes.

PubMed

Kuhar, Korina; Fredin, Lisa A; Persson, Petter

2015-06-18

Quantum chemical calculations provide detailed theoretical information concerning key aspects of photoinduced electron and excitation transfer processes in supramolecular donor-acceptor systems, which are particularly relevant to fundamental charge separation in emerging molecular approaches for solar energy conversion. Here we use density functional theory (DFT) calculations to explore the excited state landscape of heterobimetallic Ru-Co systems with varying degrees of interaction between the two metal centers, unbound, weakly bound, and tightly bound systems. The interplay between structural and electronic factors involved in various excited state relaxation processes is examined through full optimizations of multiple charge/spin states of each of the investigated systems. Low-energy relaxed heterobimetallic states of energy transfer and excitation transfer character are characterized in terms of energy, structure, and electronic properties. These findings support the notion of efficient photoinduced charge separation from a Ru(II)-Co(III) ground state, via initial optical excitation of the Ru-center, to low-energy Ru(III)-Co(II) states. The strongly coupled system has significant involvement of the conjugated bridge, qualitatively distinguishing it from the other two weakly coupled systems. Finally, by constructing potential energy surfaces for the three systems where all charge/spin state combinations are projected onto relevant reaction coordinates, excited state decay pathways are explored.

Ion Trap Collisional Activation of c and z• Ions Formed via Gas-Phase Ion/Ion Electron Transfer Dissociation

PubMed Central

Han, Hongling; Xia, Yu; McLuckey, Scott A.

2008-01-01

A series of c- and z•-type product ions formed via gas-phase electron transfer ion/ion reactions between protonated polypeptides with azobenzene radical anions are subjected to ion trap collision activation in a linear ion trap. Fragment ions including a-, b-, y-type and ammonia-loss ions are typically observed in collision induced dissociation (CID) of c ions, showing almost identical CID patterns as those of the C-terminal amidated peptides consisting of the same sequences. Collisional activation of z• species mainly gives rise to side-chain losses and peptide backbone cleavages resulting in a-, b-, c-, x-, y-and z-type ions. Most of the fragmentation pathways of z• species upon ion trap CID can be accounted for by radical driven processes. The side-chain losses from z• species are different from the small losses observed from the charge-reduced peptide molecular species in electron transfer dissociation (ETD), which indicates rearrangement of the radical species. Characteristic side-chain losses are observed for several amino acid residues, which are useful to predict their presence in peptide/protein ions. Furthermore, the unique side-chain losses from leucine and isoleucine residues allow facile distinction of these two isomeric residues. PMID:17608403

Electrochemical oxidation of ciprofloxacin in two different processes: the electron transfer process on the anode surface and the indirect oxidation process in bulk solutions.

PubMed

Shen, Bo; Wen, Xianghua; Korshin, Gregory V

2018-05-14

Herein, the rotating disk electrode technique was used for the first time to investigate the effects of mass-transfer limitations and pH on the electrochemical oxidation of CPX, to determine the kinetics of CPX oxidation and to explore intrinsic mechanisms during the electron transfer process. Firstly, cyclic voltammetry revealed that an obvious irreversible CPX oxidation peak was observed within the potential window from 0.70 to 1.30 V at all pHs. Based on the Levich equation, the electrochemical oxidation of CPX in the electron transfer process was found to be controlled by both diffusion and kinetic processes when pH = 2, 5, 7 and 9; the diffusion coefficient of CPX at pH = 2 was calculated to be 1.5 × 10-7 cm2 s-1. Kinetic analysis indicated that the reaction on the electrode surface was adsorption-controlled compared to a diffusion process; the surface concentration of electroactive species was estimated to be 1.15 × 10-9 mol cm-2, the standard rate constant of the surface reaction was calculated to be 1.37 s-1, and CPX oxidation was validated to be a two-electron transfer process. Finally, a possible CPX oxidation pathway during the electron transfer process was proposed. The electrochemical degradation of CPX on a Ti-based anode was also conducted subsequently to investigate the electrochemical oxidation of CPX in the indirect oxidation process in bulk solutions. The effects of pH and current density were determined and compared to related literature results. The oxidation of CPX at different pHs is believed to be the result of a counterbalance between favorable and unfavorable factors, namely electromigration and side reactions of oxygen evolution, respectively. The effects of current density indicated a diffusion- and reaction-controlled process at low currents followed by a reaction-controlled process at high currents. The results presented in this study provide better understanding of the electrochemical oxidation of CPX and would enable the development of new treatment methods based on electrochemistry.

[Molecular responses of photosynthetic apparatus of plants to long term irradiance changes].

PubMed

Adamiec, Małgorzata; Jackowski, Grzegorz

2008-01-01

In response to long term (at least 1-3 h) irradiance changes the responses are elicited at the level of structure and function of photosynthetic apparatus of plants which are thought to be aimed to keep the balance between the level of excitation energy funneled to the reaction centers of the photosystems by energetic antennae and the utilization of this energy in the form of photosynthetic electron transfer and dark reactions. At high vs medium irradiances the rate of excitation energy transfer via LHCII is reduced while the rate of electron flow and photosynthetic dark reactions is increased. The reaction at LHCII level stems from the reduction of its pool per PSII reaction center and the regulatory events comprise changes in the expression of LHCII apoproteins and/or chi b biosynthesis. The basis for higher electron flow capabilities lies in significant increases in the content of some electron carriers and the catalytic activity of ATP synthase. The upregulation of photosynthetic dark reaction in turn is due to the activation of signaling pathways leading to the increase in the pool and catalytic activities of rubisco and other Calvin cycle enzymes.

Atomic Resolution Modeling of the Ferredoxin:[FeFe] Hydrogenase Complex from Chlamydomonas reinhardtii

PubMed Central

Chang, Christopher H.; King, Paul W.; Ghirardi, Maria L.; Kim, Kwiseon

2007-01-01

The [FeFe] hydrogenases HydA1 and HydA2 in the green alga Chlamydomonas reinhardtii catalyze the final reaction in a remarkable metabolic pathway allowing this photosynthetic organism to produce H2 from water in the chloroplast. A [2Fe-2S] ferredoxin is a critical branch point in electron flow from Photosystem I toward a variety of metabolic fates, including proton reduction by hydrogenases. To better understand the binding determinants involved in ferredoxin:hydrogenase interactions, we have modeled Chlamydomonas PetF1 and HydA2 based on amino-acid sequence homology, and produced two promising electron-transfer model complexes by computational docking. To characterize these models, quantitative free energy calculations at atomic resolution were carried out, and detailed analysis of the interprotein interactions undertaken. The protein complex model we propose for ferredoxin:HydA2 interaction is energetically favored over the alternative candidate by 20 kcal/mol. This proposed model of the electron-transfer complex between PetF1 and HydA2 permits a more detailed view of the molecular events leading up to H2 evolution, and suggests potential mutagenic strategies to modulate electron flow to HydA2. PMID:17660315

Atomic resolution modeling of the ferredoxin:[FeFe] hydrogenase complex from Chlamydomonas reinhardtii.

PubMed

Chang, Christopher H; King, Paul W; Ghirardi, Maria L; Kim, Kwiseon

2007-11-01

The [FeFe] hydrogenases HydA1 and HydA2 in the green alga Chlamydomonas reinhardtii catalyze the final reaction in a remarkable metabolic pathway allowing this photosynthetic organism to produce H(2) from water in the chloroplast. A [2Fe-2S] ferredoxin is a critical branch point in electron flow from Photosystem I toward a variety of metabolic fates, including proton reduction by hydrogenases. To better understand the binding determinants involved in ferredoxin:hydrogenase interactions, we have modeled Chlamydomonas PetF1 and HydA2 based on amino-acid sequence homology, and produced two promising electron-transfer model complexes by computational docking. To characterize these models, quantitative free energy calculations at atomic resolution were carried out, and detailed analysis of the interprotein interactions undertaken. The protein complex model we propose for ferredoxin:HydA2 interaction is energetically favored over the alternative candidate by 20 kcal/mol. This proposed model of the electron-transfer complex between PetF1 and HydA2 permits a more detailed view of the molecular events leading up to H(2) evolution, and suggests potential mutagenic strategies to modulate electron flow to HydA2.

Energy transfer dynamics in trimers and aggregates of light-harvesting complex II probed by 2D electronic spectroscopy

DOE Office of Scientific and Technical Information (OSTI.GOV)

Enriquez, Miriam M.; Zhang, Cheng; Tan, Howe-Siang, E-mail: howesiang@ntu.edu.sg

2015-06-07

The pathways and dynamics of excitation energy transfer between the chlorophyll (Chl) domains in solubilized trimeric and aggregated light-harvesting complex II (LHCII) are examined using two-dimensional electronic spectroscopy (2DES). The LHCII trimers and aggregates exhibit the unquenched and quenched excitonic states of Chl a, respectively. 2DES allows direct correlation of excitation and emission energies of coupled states over population time delays, hence enabling mapping of the energy flow between Chls. By the excitation of the entire Chl b Q{sub y} band, energy transfer from Chl b to Chl a states is monitored in the LHCII trimers and aggregates. Global analysismore » of the two-dimensional (2D) spectra reveals that energy transfer from Chl b to Chl a occurs on fast and slow time scales of 240–270 fs and 2.8 ps for both forms of LHCII. 2D decay-associated spectra resulting from the global analysis identify the correlation between Chl states involved in the energy transfer and decay at a given lifetime. The contribution of singlet–singlet annihilation on the kinetics of Chl energy transfer and decay is also modelled and discussed. The results show a marked change in the energy transfer kinetics in the time range of a few picoseconds. Owing to slow energy equilibration processes, long-lived intermediate Chl a states are present in solubilized trimers, while in aggregates, the population decay of these excited states is significantly accelerated, suggesting that, overall, the energy transfer within the LHCII complexes is faster in the aggregated state.« less

Microbial catabolic activities are naturally selected by metabolic energy harvest rate.

PubMed

González-Cabaleiro, Rebeca; Ofiţeru, Irina D; Lema, Juan M; Rodríguez, Jorge

2015-12-01

The fundamental trade-off between yield and rate of energy harvest per unit of substrate has been largely discussed as a main characteristic for microbial established cooperation or competition. In this study, this point is addressed by developing a generalized model that simulates competition between existing and not experimentally reported microbial catabolic activities defined only based on well-known biochemical pathways. No specific microbial physiological adaptations are considered, growth yield is calculated coupled to catabolism energetics and a common maximum biomass-specific catabolism rate (expressed as electron transfer rate) is assumed for all microbial groups. Under this approach, successful microbial metabolisms are predicted in line with experimental observations under the hypothesis of maximum energy harvest rate. Two microbial ecosystems, typically found in wastewater treatment plants, are simulated, namely: (i) the anaerobic fermentation of glucose and (ii) the oxidation and reduction of nitrogen under aerobic autotrophic (nitrification) and anoxic heterotrophic and autotrophic (denitrification) conditions. The experimentally observed cross feeding in glucose fermentation, through multiple intermediate fermentation pathways, towards ultimately methane and carbon dioxide is predicted. Analogously, two-stage nitrification (by ammonium and nitrite oxidizers) is predicted as prevailing over nitrification in one stage. Conversely, denitrification is predicted in one stage (by denitrifiers) as well as anammox (anaerobic ammonium oxidation). The model results suggest that these observations are a direct consequence of the different energy yields per electron transferred at the different steps of the pathways. Overall, our results theoretically support the hypothesis that successful microbial catabolic activities are selected by an overall maximum energy harvest rate.

Biosynthesis and bioproduction of coenzyme Q10 by yeasts and other organisms.

PubMed

Kawamukai, Makoto

2009-06-22

CoQ (coenzyme Q), an isoprenylated benzoquinone, is a well-known component of the electron-transfer system in eukaryotes. The main role of CoQ is to transfer electrons from NADH dehydrogenase and succinate dehydrogenase to CoQ:cytochrome c reductase in the respiratory chain. However, recent evidence indicates that an involvement in respiration is not the only role of CoQ. The second apparent role of CoQ is its anti-oxidation property, and other novel roles for CoQ, such as in disulfide-bond formation, sulfide oxidation and pyrimidine metabolism, have been reported. CoQ10, having ten isoprene units in the isoprenoid side chain, has been used as a medicine and is now commercially popular as a food supplement. Two yeast species, namely the budding yeast Saccharomyces cerevisiae, which produces CoQ6, and the fission yeast Schizosaccharomyces pombe, which produces CoQ10, are the main subjects of the present minireview because they have greatly contributed to our basic knowledge of CoQ biosynthesis among eukaryotes. The biosynthetic pathway that converts p-hydroxybenzoate into CoQ consists of eight steps in yeasts. The five enzymes involved in the biosynthetic pathway have been identified in both yeasts, yet the functions of three proteins were still not known. Analyses of the biosynthetic pathway in yeasts also contribute to the understanding of human genetic diseases related to CoQ deficiency. In the present minireview I focus on the biochemical and commercial aspects of CoQ in yeasts and in other organisms for comparison.

Photochemistry of 1- and 2-Naphthols and Their Water Clusters: The Role of 1 ππ*(La ) Mediated Hydrogen Transfer to Carbon Atoms.

PubMed

Novak, Jurica; Prlj, Antonio; Basarić, Nikola; Corminboeuf, Clémence; Došlić, Nađa

2017-06-16

The computational analysis of the isomer- and conformer-dependent photochemistry of 1- and 2-naphthols and their microsolvated water clusters is motivated by their very different excited state reactivities. We present evidence that 1- and 2-naphthol follow distinct excited state deactivation pathways. The deactivation of 2-naphthols, 2-naphthol water clusters, as well as of the anti conformer of 1-naphthol is mediated by the optically dark 1 πσ* state. The dynamics of the 1 πσ* surface leads to the homolytic cleavage of the OH bond. On the contrary, the excited state deactivation of syn 1-naphthol and 1-naphthol water clusters follows an uncommon reaction pathway. Upon excitation to the bright 1 ππ*(L a ) state, a highly specific excited state hydrogen transfer (ESHT) to carbon atoms C8 and C5 takes place, yielding 1,8- and 1,5-naphthoquinone methides. The ESHT pathway arises from the intrinsic electronic properties of the 1 ππ*(L a ) state of 1-naphthols. © 2017 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.

Diabatization for Time-Dependent Density Functional Theory: Exciton Transfers and Related Conical Intersections.

PubMed

Tamura, Hiroyuki

2016-11-23

Intermolecular exciton transfers and related conical intersections are analyzed by diabatization for time-dependent density functional theory. The diabatic states are expressed as a linear combination of the adiabatic states so as to emulate the well-defined reference states. The singlet exciton coupling calculated by the diabatization scheme includes contributions from the Coulomb (Förster) and electron exchange (Dexter) couplings. For triplet exciton transfers, the Dexter coupling, charge transfer integral, and diabatic potentials of stacked molecules are calculated for analyzing direct and superexchange pathways. We discuss some topologies of molecular aggregates that induce conical intersections on the vanishing points of the exciton coupling, namely boundary of H- and J-aggregates and T-shape aggregates, as well as canceled exciton coupling to the bright state of H-aggregate, i.e., selective exciton transfer to the dark state. The diabatization scheme automatically accounts for the Berry phase by fixing the signs of reference states while scanning the coordinates.

PSI Mehler reaction is the main alternative photosynthetic electron pathway in Symbiodinium sp., symbiotic dinoflagellates of cnidarians.

PubMed

Roberty, Stéphane; Bailleul, Benjamin; Berne, Nicolas; Franck, Fabrice; Cardol, Pierre

2014-10-01

Photosynthetic organisms have developed various photoprotective mechanisms to cope with exposure to high light intensities. In photosynthetic dinoflagellates that live in symbiosis with cnidarians, the nature and relative amplitude of these regulatory mechanisms are a matter of debate. In our study, the amplitude of photosynthetic alternative electron flows (AEF) to oxygen (chlororespiration, Mehler reaction), the mitochondrial respiration and the Photosystem I (PSI) cyclic electron flow were investigated in strains belonging to three clades (A1, B1 and F1) of Symbiodinium. Cultured Symbiodinium strains were maintained under identical environmental conditions, and measurements of oxygen evolution, fluorescence emission and absorption changes at specific wavelengths were used to evaluate PSI and PSII electron transfer rates (ETR). A light- and O2 -dependent ETR was observed in all strains. This electron transfer chain involves PSII and PSI and is insensitive to inhibitors of mitochondrial activity and carbon fixation. We demonstrate that in all strains, the Mehler reaction responsible for photoreduction of oxygen by the PSI under high light, is the main AEF at the onset and at the steady state of photosynthesis. This sustained photosynthetic AEF under high light intensities acts as a photoprotective mechanism and leads to an increase of the ATP/NADPH ratio. © 2014 The Authors New Phytologist © 2014 New Phytologist Trust.

Mechanism of amperometric biosensor with electronic-type-controlled carbon nanotube

NASA Astrophysics Data System (ADS)

Hidaka, Hiroki; Nowaki, Kohei; Muguruma, Hitoshi

2016-03-01

An amperometric enzyme biosensor with electronic-type-controlled (metallic and semiconducting) single-walled carbon nanotubes (CNTs) is presented. In this research, we investigate how the electronic types of CNTs influence the amperometric response of enzyme biosensors and what their working mechanisms are. The biosensor of interest is for glucose detection using enzyme glucose oxidase (GOD). In the presence of oxygen, the response of a metallic CNT-GOD electrode was 2.5 times more sensitive than that of a semiconducting CNT-GOD electrode. In contrast, in the absence of oxygen, the response of the semiconducting CNT-GOD electrode was retained, whereas that of the metallic CNT-GOD electrode was significantly reduced. This indicates that direct electron transfer occurred with the semiconducting CNT-GOD electrode, whereas the metallic CNT-GOD electrode was dominated by a hydrogen peroxide pathway caused by an enzymatic reaction. Electrochemical impedance spectroscopy was used to show that the semiconducting CNT network has less resistance for electron transfer than the metallic CNT network. The optimized glucose biosensor revealed a sensitivity of 5.6 µA mM-1 cm-2 at +0.6 V vs Ag/AgCl, a linear dynamic range of 0.025-1.4 mM, and a response time of 8 s.

Promotion of Iron Oxide Reduction and Extracellular Electron Transfer in Shewanella oneidensis by DMSO

PubMed Central

Cheng, Yuan-Yuan; Li, Bing-Bing; Li, Dao-Bo; Chen, Jie-Jie; Li, Wen-Wei; Tong, Zhong-Hua; Wu, Chao; Yu, Han-Qing

2013-01-01

The dissimilatory metal reducing bacterium Shewanella oneidensis MR-1, known for its capacity of reducing iron and manganese oxides, has great environmental impacts. The iron oxides reducing process is affected by the coexistence of alternative electron acceptors in the environment, while investigation into it is limited so far. In this work, the impact of dimethyl sulphoxide (DMSO), a ubiquitous chemical in marine environment, on the reduction of hydrous ferric oxide (HFO) by S. oneidensis MR-1 was investigated. Results show that DMSO promoted HFO reduction by both wild type and ΔdmsE, but had no effect on the HFO reduction by ΔdmsB, indicating that such a promotion was dependent on the DMSO respiration. With the DMSO dosing, the levels of extracellular flavins and omcA expression were significantly increased in WT and further increased in ΔdmsE. Bioelectrochemical analysis show that DMSO also promoted the extracellular electron transfer of WT and ΔdmsE. These results demonstrate that DMSO could stimulate the HFO reduction through metabolic and genetic regulation in S. oneidensis MR-1, rather than compete for electrons with HFO. This may provide a potential respiratory pathway to enhance the microbial electron flows for environmental and engineering applications. PMID:24244312

Photo-induced oxidative damage to dissolved free amino acids by the photosensitizer polycyclic musk tonalide: Transformation kinetics and mechanisms.

PubMed

Fang, Hansun; Gao, Yanpeng; Wang, Honghong; Yin, Hongliang; Li, Guiying; An, Taicheng

2017-05-15

Residue from the polycyclic musks (PCMs) in household and personal care products may harm human beings through skin exposure. To understand the health effects of PCMs when exposed to sunlight at molecular level, both experimental and computational methods were employed to investigate the photosensitized oxidation performance of 19 natural amino acids, the most basic unit of life. Results showed that a typical PCM, tonalide, acts as a photosensitizer to significantly increase photo-induced oxidative damage to amino acids. Both common and exceptional transformation pathways occurred during the photosensitization damage of amino acids. Experimental tests further identified the different mechanisms involved. The common transformation pathway occurred through the electron transfer from α amino-group of amino acids, accompanying with the formation of O 2 •- . This pathway was controlled by the electronic density of N atom in α amino-group. The exceptional transformation pathway was identified only for five amino acids, mainly due to the reactions with reactive oxygen species, e.g. 1 O 2 and excited triplet state molecules. Additionally, tonalide photo-induced transformation products could further accelerate the photosensitization of all amino acids with the common pathway. This study may support the protection of human health, and suggests the possible need to further restrict polycyclic musks use. Copyright © 2017 Elsevier Ltd. All rights reserved.

Characterization of a unique [FeS] cluster in the electron transfer chain of the oxygen tolerant [NiFe] hydrogenase from Aquifex aeolicus.

PubMed

Pandelia, Maria-Eirini; Nitschke, Wolfgang; Infossi, Pascale; Giudici-Orticoni, Marie-Thérèse; Bill, Eckhard; Lubitz, Wolfgang

2011-04-12

Iron-sulfur clusters are versatile electron transfer cofactors, ubiquitous in metalloenzymes such as hydrogenases. In the oxygen-tolerant Hydrogenase I from Aquifex aeolicus such electron "wires" form a relay to a diheme cytb, an integral part of a respiration pathway for the reduction of O(2) to water. Amino acid sequence comparison with oxygen-sensitive hydrogenases showed conserved binding motifs for three iron-sulfur clusters, the nature and properties of which were unknown so far. Electron paramagnetic resonance spectra exhibited complex signals that disclose interesting features and spin-coupling patterns; by redox titrations three iron-sulfur clusters were identified in their usual redox states, a [3Fe4S] and two [4Fe4S], but also a unique high-potential (HP) state was found. On the basis of (57)Fe Mössbauer spectroscopy we attribute this HP form to a superoxidized state of the [4Fe4S] center proximal to the [NiFe] site. The unique environment of this cluster, characterized by a surplus cysteine coordination, is able to tune the redox potentials and make it compliant with the [4Fe4S](3+) state. It is actually the first example of a biological [4Fe4S] center that physiologically switches between 3+, 2+, and 1+ oxidation states within a very small potential range. We suggest that the (1 + /2+) redox couple serves the classical electron transfer reaction, whereas the superoxidation step is associated with a redox switch against oxidative stress.

Characterization of a unique [FeS] cluster in the electron transfer chain of the oxygen tolerant [NiFe] hydrogenase from Aquifex aeolicus

PubMed Central

Pandelia, Maria-Eirini; Nitschke, Wolfgang; Infossi, Pascale; Giudici-Orticoni, Marie-Thérèse; Bill, Eckhard; Lubitz, Wolfgang

2011-01-01

Iron-sulfur clusters are versatile electron transfer cofactors, ubiquitous in metalloenzymes such as hydrogenases. In the oxygen-tolerant Hydrogenase I from Aquifex aeolicus such electron “wires” form a relay to a diheme cytb, an integral part of a respiration pathway for the reduction of O2 to water. Amino acid sequence comparison with oxygen-sensitive hydrogenases showed conserved binding motifs for three iron-sulfur clusters, the nature and properties of which were unknown so far. Electron paramagnetic resonance spectra exhibited complex signals that disclose interesting features and spin-coupling patterns; by redox titrations three iron-sulfur clusters were identified in their usual redox states, a [3Fe4S] and two [4Fe4S], but also a unique high-potential (HP) state was found. On the basis of 57Fe Mössbauer spectroscopy we attribute this HP form to a superoxidized state of the [4Fe4S] center proximal to the [NiFe] site. The unique environment of this cluster, characterized by a surplus cysteine coordination, is able to tune the redox potentials and make it compliant with the [4Fe4S]3+ state. It is actually the first example of a biological [4Fe4S] center that physiologically switches between 3+, 2+, and 1+ oxidation states within a very small potential range. We suggest that the (1 + /2+) redox couple serves the classical electron transfer reaction, whereas the superoxidation step is associated with a redox switch against oxidative stress. PMID:21444783

A Hidden Transhydrogen Activity of a FMN-Bound Diaphorase under Anaerobic Conditions

DTIC Science & Technology

2016-05-04

RESEARCH ARTICLE A Hidden Transhydrogen Activity of a FMN- Bound Diaphorase under Anaerobic Conditions John Collins1, Ting Zhang1, Scott Huston1... metabolic pathways for facilitating the electron transfer from one molecule to another in redox reactions. Transhy- drogenase plays an important role in...March 2, 2016 Accepted: April 20, 2016 Published: May 4, 2016 Copyright: © 2016 Collins et al. This is an open access article distributed under the

Short-term regulation and alternative pathways of photosynthetic electron transport in Hibiscus rosa-sinensis leaves.

PubMed

Trubitsin, Boris V; Vershubskii, Alexey V; Priklonskii, Vladimir I; Tikhonov, Alexander N

2015-11-01

In this work, using the EPR and PAM-fluorometry methods, we have studied induction events of photosynthetic electron transport in Hibiscus rosa-sinensis leaves. The methods used are complementary, providing efficient tools for in situ monitoring of P700 redox transients and photochemical activity of photosystem II (PSII). The induction of P700(+) in dark-adapted leaves is characterized by the multiphase kinetics with a lag-phase, which duration elongates with the dark-adaptation time. Analyzing effects of the uncoupler monensin and artificial electron carrier methylviologen (MV) on photooxidation of P700 and slow induction of chlorophyll a fluorescence (SIF), we could ascribe different phases of transient kinetics of electron transport processes in dark-adapted leaves to the following regulatory mechanisms: (i) acceleration of electron transfer on the acceptor side of PSI, (ii) pH-dependent modulation of the intersystem electron flow, and (iii) re-distribution of electron fluxes between alternative (linear, cyclic, and pseudocyclic) pathways. Monensin significantly decreases a level of P700(+) and inhibits SIF. MV, which mediates electron flow from PSI to O2 with consequent formation of H2O2, promotes a rapid photooxidation of P700 without any lag-phase peculiar to untreated leaves. MV-mediated water-water cycle (H2O→PSII→PSI→MV→O2→H2O2→H2O) is accompanied by generation of ascorbate free radicals. This suggests that the ascorbate peroxidase system of defense against reactive oxygen species is active in chloroplasts of H. rosa-sinensis leaves. In DCMU-treated chloroplasts with inhibited PSII, the contribution of cyclic electron flow is insignificant as compared to linear electron flow. For analysis of induction events, we have simulated electron transport processes within the framework of our generalized mathematical model of oxygenic photosynthesis, which takes into account pH-dependent mechanisms of electron transport control and re-distribution of electron fluxes between alternative pathways. The model adequately describes the main peculiarities of P700(+) induction and dynamics of the intersystem electron transport. Copyright © 2015 Elsevier B.V. All rights reserved.

Electronically type-sorted carbon nanotube-based electrochemical biosensors with glucose oxidase and dehydrogenase.

PubMed

Muguruma, Hitoshi; Hoshino, Tatsuya; Nowaki, Kohei

2015-01-14

An electrochemical enzyme biosensor with electronically type-sorted (metallic and semiconducting) single-walled carbon nanotubes (SWNTs) for use in aqueous media is presented. This research investigates how the electronic types of SWNTs influence the amperometric response of enzyme biosensors. To conduct a clear evaluation, a simple layer-by-layer process based on a plasma-polymerized nano thin film (PPF) was adopted because a PPF is an inactive matrix that can form a well-defined nanostructure composed of SWNTs and enzyme. For a biosensor with the glucose oxidase (GOx) enzyme in the presence of oxygen, the response of a metallic SWNT-GOx electrode was 2 times larger than that of a semiconducting SWNT-GOx electrode. In contrast, in the absence of oxygen, the response of the semiconducting SWNT-GOx electrode was retained, whereas that of the metallic SWNT-GOx electrode was significantly reduced. This indicates that direct electron transfer occurred with the semiconducting SWNT-GOx electrode, whereas the metallic SWNT-GOx electrode was dominated by a hydrogen peroxide pathway caused by an enzymatic reaction. For a biosensor with the glucose dehydrogenase (GDH; oxygen-independent catalysis) enzyme, the response of the semiconducting SWNT-GDH electrode was 4 times larger than that of the metallic SWNT-GDH electrode. Electrochemical impedance spectroscopy was used to show that the semiconducting SWNT network has less resistance for electron transfer than the metallic SWNT network. Therefore, it was concluded that semiconducting SWNTs are more suitable than metallic SWNTs for electrochemical enzyme biosensors in terms of direct electron transfer as a detection mechanism. This study makes a valuable contribution toward the development of electrochemical biosensors that employ sorted SWNTs and various enzymes.

Theoretical study of dynamic electron-spin-polarization via the doublet-quartet quantum-mixed state and time-resolved ESR spectra of the quartet high-spin state.

PubMed

Teki, Yoshio; Matsumoto, Takafumi

2011-04-07

The mechanism of the unique dynamic electron polarization of the quartet (S = 3/2) high-spin state via a doublet-quartet quantum-mixed state and detail theoretical calculations of the population transfer are reported. By the photo-induced electron transfer, the quantum-mixed charge-separate state is generated in acceptor-donor-radical triad (A-D-R). This mechanism explains well the unique dynamic electron polarization of the quartet state of A-D-R. The generation of the selectively populated quantum-mixed state and its transfer to the strongly coupled pure quartet and doublet states have been treated both by a perturbation approach and by exact numerical calculations. The analytical solutions show that generation of the quantum-mixed states with the selective populations after de-coherence and/or accompanying the (complete) dephasing during the charge-recombination are essential for the unique dynamic electron polarization. Thus, the elimination of the quantum coherence (loss of the quantum information) is the key process for the population transfer from the quantum-mixed state to the quartet state. The generation of high-field polarization on the strongly coupled quartet state by the charge-recombination process can be explained by a polarization transfer from the quantum-mixed charge-separate state. Typical time-resolved ESR patterns of the quantum-mixed state and of the strongly coupled quartet state are simulated based on the generation mechanism of the dynamic electron polarization. The dependence of the spectral pattern of the quartet high-spin state has been clarified for the fine-structure tensor and the exchange interaction of the quantum-mixed state. The spectral pattern of the quartet state is not sensitive towards the fine-structure tensor of the quantum-mixed state, because this tensor contributes only as a perturbation in the population transfer to the spin-sublevels of the quartet state. Based on the stochastic Liouville equation, it is also discussed why the selective population in the quantum-mixed state is generated for the "finite field" spin-sublevels. The numerical calculations of the elimination of the quantum coherence (de-coherence and/or dephasing) are demonstrated. A new possibility of the enhanced intersystem crossing pathway in solution is also proposed.

Major Pathways to Electron Distribution Function Formation in Regions of Diffuse Aurora

NASA Technical Reports Server (NTRS)

Khazanov, George V.; Sibeck, David G.; Zesta, Eftyhia

2017-01-01

This paper discusses the major pathways of electron distribution function formation in the region of diffuse aurora. The diffuse aurora accounts for about of 75% of the auroral energy precipitating into the upper atmosphere, and its origin has been the subject of much discussion. We show that an earthward stream of precipitating electrons initially injected from the Earth's plasma sheet via wave-particle interactions degrades in the atmosphere toward lower energies and produces secondary electrons via impact ionization of the neutral atmosphere. These electrons of magnetospheric origin are then reflected back into the magnetosphere along closed dipolar magnetic field lines, leading to a series of reflections and consequent magnetospheric interactions that greatly augment the initially precipitating flux at the upper ionospheric boundary (700-800 km). To date this, systematic magnetosphere-ionosphere coupling element has not been included in auroral research models, and, as we demonstrate in this article, has a dramatic effect (200-300%) on the formation of the precipitating fluxes that result in the diffuse aurora. It is shown that wave-particle interaction processes that drive precipitating fluxes in the region of diffuse aurora from the magnetospheric altitudes are only the first step in the formation of electron precipitation at ionospheric altitudes, and they cannot be separated from the atmospheric collisional machine that redistributes and transfers their energy inside the magnetosphere-ionosphere-atmosphere coupling system.

Major pathways to electron distribution function formation in regions of diffuse aurora

NASA Astrophysics Data System (ADS)

Khazanov, George V.; Sibeck, David G.; Zesta, Eftyhia

2017-04-01

This paper discusses the major pathways of electron distribution function formation in the region of diffuse aurora. The diffuse aurora accounts for about of 75% of the auroral energy precipitating into the upper atmosphere, and its origin has been the subject of much discussion. We show that an earthward stream of precipitating electrons initially injected from the Earth's plasma sheet via wave-particle interactions degrades in the atmosphere toward lower energies and produces secondary electrons via impact ionization of the neutral atmosphere. These electrons of magnetospheric origin are then reflected back into the magnetosphere along closed dipolar magnetic field lines, leading to a series of reflections and consequent magnetospheric interactions that greatly augment the initially precipitating flux at the upper ionospheric boundary (700-800 km). To date this, systematic magnetosphere-ionosphere coupling element has not been included in auroral research models, and, as we demonstrate in this article, has a dramatic effect (200-300%) on the formation of the precipitating fluxes that result in the diffuse aurora. It is shown that wave-particle interaction processes that drive precipitating fluxes in the region of diffuse aurora from the magnetospheric altitudes are only the first step in the formation of electron precipitation at ionospheric altitudes, and they cannot be separated from the atmospheric "collisional machine" that redistributes and transfers their energy inside the magnetosphere-ionosphere-atmosphere coupling system.

Exploring the biochemistry at the extracellular redox frontier of bacterial mineral Fe(III) respiration

DOE Office of Scientific and Technical Information (OSTI.GOV)

Richardson, David J.; Edwards, Marcus; White, Gaye F.

2012-06-01

Many species of the bacterial Shewanella genus are notable for their ability to respire in anoxic environments utilizing insoluble minerals of Fe(III) and Mn(IV) as extracellular electron acceptors. In Shewanella oneidensis, the process is dependent on the decahaem electron-transport proteins that lie at the extracellular face of the outer membrane where they can contact the insoluble mineral substrates. These extracellular proteins are charged with electrons provided by an inter-membrane electron-transfer pathway that links the extracellular face of the outer membrane with the inner cytoplasmic membrane and thereby intracellular electron sources. In the present paper, we consider the common structural featuresmore » of two of these outermembrane decahaem cytochromes, MtrC and MtrF, and bring this together with biochemical, spectroscopic and voltammetric data to identify common and distinct properties of these prototypical members of different clades of the outer-membrane decahaem cytochrome superfamily.« less

Effect of five-membered ring and heteroatom substitution on charge transport properties of perylene discotic derivatives: A theoretical approach

DOE Office of Scientific and Technical Information (OSTI.GOV)

Navarro, Amparo, E-mail: anavarro@ujaen.es; Fernández-Liencres, M. Paz; Peña-Ruiz, Tomás

2016-08-07

Density functional theory calculations were carried out to investigate the evolvement of charge transport properties of a set of new discotic systems as a function of ring and heteroatom (B, Si, S, and Se) substitution on the basic structure of perylene. The replacement of six-membered rings by five-membered rings in the reference compound has shown a prominent effect on the electron reorganization energy that decreases ∼0.2 eV from perylene to the new carbon five-membered ring derivative. Heteroatom substitution with boron also revealed to lower the LUMO energy level and increase the electron affinity, therefore lowering the electron injection barrier comparedmore » to perylene. Since the rate of the charge transfer between two molecules in columnar discotic systems is strongly dependent on the orientation of the stacked cores, the total energy and transfer integral of a dimer as a disc is rotated with respect to the other along the stacking axis have been predicted. Aimed at obtaining a more realistic approach to the bulk structure, the molecular geometry of clusters made up of five discs was fully optimized, and charge transfer rate and mobilities were estimated for charge transport along a one dimensional pathway. Heteroatom substitution with selenium yields electron transfer integral values ∼0.3 eV with a relative disc orientation of 25°, which is the preferred angle according to the dimer energy profile. All the results indicate that the tetraselenium-substituted derivative, not synthetized so far, could be a promising candidate among those studied in this work for the fabrication of n-type semiconductors based on columnar discotic liquid crystals materials.« less

Effect of five-membered ring and heteroatom substitution on charge transport properties of perylene discotic derivatives: A theoretical approach.

PubMed

Navarro, Amparo; Fernández-Liencres, M Paz; Peña-Ruiz, Tomás; García, Gregorio; Granadino-Roldán, José M; Fernández-Gómez, Manuel

2016-08-07

Density functional theory calculations were carried out to investigate the evolvement of charge transport properties of a set of new discotic systems as a function of ring and heteroatom (B, Si, S, and Se) substitution on the basic structure of perylene. The replacement of six-membered rings by five-membered rings in the reference compound has shown a prominent effect on the electron reorganization energy that decreases ∼0.2 eV from perylene to the new carbon five-membered ring derivative. Heteroatom substitution with boron also revealed to lower the LUMO energy level and increase the electron affinity, therefore lowering the electron injection barrier compared to perylene. Since the rate of the charge transfer between two molecules in columnar discotic systems is strongly dependent on the orientation of the stacked cores, the total energy and transfer integral of a dimer as a disc is rotated with respect to the other along the stacking axis have been predicted. Aimed at obtaining a more realistic approach to the bulk structure, the molecular geometry of clusters made up of five discs was fully optimized, and charge transfer rate and mobilities were estimated for charge transport along a one dimensional pathway. Heteroatom substitution with selenium yields electron transfer integral values ∼0.3 eV with a relative disc orientation of 25°, which is the preferred angle according to the dimer energy profile. All the results indicate that the tetraselenium-substituted derivative, not synthetized so far, could be a promising candidate among those studied in this work for the fabrication of n-type semiconductors based on columnar discotic liquid crystals materials.

Proton-Coupled Electron Transfer in a Strongly Coupled Photosystem II-Inspired Chromophore–Imidazole–Phenol Complex: Stepwise Oxidation and Concerted Reduction

DOE PAGES

Manbeck, Gerald F.; Fujita, Etsuko; Concepcion, Javier J.

2016-08-18

Proton-coupled electron-transfer (PCET) reactions were studied in acetonitrile for a Photosystem II (PSII) inspired [Ru(bpy) 2(phen-imidazole-Ph(OH)( tBu) 2)] 2+, in which Ru(III) generated by a flash-quench sequence oxidizes the appended phenol and the proton is transferred to the hydrogen bonded imidazole base. In contrast to related systems, the donor and acceptor are strongly coupled, as indicated by the shift in the Ru III/IIcouple upon phenol oxidation, and intramolecular oxidation of the phenol by Ru(III) is energetically favorable by both stepwise or concerted pathways. The phenol oxidation occurs via a stepwise ET-PT mechanism with k ET = 2.7 × 10 7more » s ₋1 and a kinetic isotope effect (KIE) of 0.99 ± 0.03. The electron transfer reaction was characterized as adiabatic with λ DA = 1.16 eV and 280 < H DA < 540 cm ₋1 consistent with strong electronic coupling and slow solvent dynamics. Reduction of the phenoxyl radical by the quencher radical was examined as the analogue of the redox reaction between the PSII tyrosyl radical and the oxygen evolving complex (OEC). In our PSII-inspired complex, the recombination reaction activation energy is < 2 kcal mol ₋1. In conclusion, the reaction is nonadiabatic (V PCET ~ 22 cm ₋1 (H) and 49 cm ₋1 (D)), concerted, and exhibits an unexpected inverse KIE of 0.55 that is attributed to greater overlap of the reactant vibronic ground state with the OD vibronic states of the proton acceptor due to the smaller quantum spacing of the deuterium vibrational levels.« less

Surface Mn(II) oxidation actuated by a multicopper oxidase in a soil bacterium leads to the formation of manganese oxide minerals

PubMed Central

Zhang, Zhen; Zhang, Zhongming; Chen, Hong; Liu, Jin; Liu, Chang; Ni, Hong; Zhao, Changsong; Ali, Muhammad; Liu, Fan; Li, Lin

2015-01-01

In this manuscript, we report that a bacterial multicopper oxidase (MCO266) catalyzes Mn(II) oxidation on the cell surface, resulting in the surface deposition of Mn(III) and Mn(IV) oxides and the gradual formation of bulky oxide aggregates. These aggregates serve as nucleation centers for the formation of Mn oxide micronodules and Mn-rich sediments. A soil-borne Escherichia coli with high Mn(II)-oxidizing activity formed Mn(III)/Mn(IV) oxide deposit layers and aggregates under laboratory culture conditions. We engineered MCO266 onto the cell surfaces of both an activity-negative recipient and wild-type strains. The results confirmed that MCO266 governs Mn(II) oxidation and initiates the formation of deposits and aggregates. By contrast, a cell-free substrate, heat-killed strains, and intracellularly expressed or purified MCO266 failed to catalyze Mn(II) oxidation. However, purified MCO266 exhibited Mn(II)-oxidizing activity when combined with cell outer membrane component (COMC) fractions in vitro. We demonstrated that Mn(II) oxidation and aggregate formation occurred through an oxygen-dependent biotic transformation process that requires a certain minimum Mn(II) concentration. We propose an approximate electron transfer pathway in which MCO266 transfers only one electron to convert Mn(II) to Mn(III) and then cooperates with other COMC electron transporters to transfer the other electron required to oxidize Mn(III) to Mn(IV). PMID:26039669

Surface Mn(II) oxidation actuated by a multicopper oxidase in a soil bacterium leads to the formation of manganese oxide minerals.

PubMed

Zhang, Zhen; Zhang, Zhongming; Chen, Hong; Liu, Jin; Liu, Chang; Ni, Hong; Zhao, Changsong; Ali, Muhammad; Liu, Fan; Li, Lin

2015-06-03

In this manuscript, we report that a bacterial multicopper oxidase (MCO266) catalyzes Mn(II) oxidation on the cell surface, resulting in the surface deposition of Mn(III) and Mn(IV) oxides and the gradual formation of bulky oxide aggregates. These aggregates serve as nucleation centers for the formation of Mn oxide micronodules and Mn-rich sediments. A soil-borne Escherichia coli with high Mn(II)-oxidizing activity formed Mn(III)/Mn(IV) oxide deposit layers and aggregates under laboratory culture conditions. We engineered MCO266 onto the cell surfaces of both an activity-negative recipient and wild-type strains. The results confirmed that MCO266 governs Mn(II) oxidation and initiates the formation of deposits and aggregates. By contrast, a cell-free substrate, heat-killed strains, and intracellularly expressed or purified MCO266 failed to catalyze Mn(II) oxidation. However, purified MCO266 exhibited Mn(II)-oxidizing activity when combined with cell outer membrane component (COMC) fractions in vitro. We demonstrated that Mn(II) oxidation and aggregate formation occurred through an oxygen-dependent biotic transformation process that requires a certain minimum Mn(II) concentration. We propose an approximate electron transfer pathway in which MCO266 transfers only one electron to convert Mn(II) to Mn(III) and then cooperates with other COMC electron transporters to transfer the other electron required to oxidize Mn(III) to Mn(IV).

Hydrogen Bond Network between Amino Acid Radical Intermediates on the Proton-Coupled Electron Transfer Pathway of E. coli α2 Ribonucleotide Reductase

PubMed Central

2015-01-01

Ribonucleotide reductases (RNRs) catalyze the conversion of ribonucleotides to deoxyribonucleotides in all organisms. In all Class Ia RNRs, initiation of nucleotide diphosphate (NDP) reduction requires a reversible oxidation over 35 Å by a tyrosyl radical (Y122•, Escherichia coli) in subunit β of a cysteine (C439) in the active site of subunit α. This radical transfer (RT) occurs by a specific pathway involving redox active tyrosines (Y122 ⇆ Y356 in β to Y731 ⇆ Y730 ⇆ C439 in α); each oxidation necessitates loss of a proton coupled to loss of an electron (PCET). To study these steps, 3-aminotyrosine was site-specifically incorporated in place of Y356-β, Y731- and Y730-α, and each protein was incubated with the appropriate second subunit β(α), CDP and effector ATP to trap an amino tyrosyl radical (NH2Y•) in the active α2β2 complex. High-frequency (263 GHz) pulse electron paramagnetic resonance (EPR) of the NH2Y•s reported the gx values with unprecedented resolution and revealed strong electrostatic effects caused by the protein environment. 2H electron–nuclear double resonance (ENDOR) spectroscopy accompanied by quantum chemical calculations provided spectroscopic evidence for hydrogen bond interactions at the radical sites, i.e., two exchangeable H bonds to NH2Y730•, one to NH2Y731• and none to NH2Y356•. Similar experiments with double mutants α-NH2Y730/C439A and α-NH2Y731/Y730F allowed assignment of the H bonding partner(s) to a pathway residue(s) providing direct evidence for colinear PCET within α. The implications of these observations for the PCET process within α and at the interface are discussed. PMID:25516424

Anaerobic Dehalogenation of Chloroanilines by Dehalococcoides mccartyi Strain CBDB1 and Dehalobacter Strain 14DCB1 via Different Pathways as Related to Molecular Electronic Structure.

PubMed

Zhang, Shangwei; Wondrousch, Dominik; Cooper, Myriel; Zinder, Stephen H; Schüürmann, Gerrit; Adrian, Lorenz

2017-04-04

Dehalococcoides mccartyi strain CBDB1 and Dehalobacter strain 14DCB1 are organohalide-respiring microbes of the phyla Chloroflexi and Firmicutes, respectively. Here, we report the transformation of chloroanilines by these two bacterial strains via dissimilar dehalogenation pathways and discuss the underlying mechanism with quantum chemically calculated net atomic charges of the substrate Cl, H, and C atoms. Strain CBDB1 preferentially removed Cl doubly flanked by two Cl or by one Cl and NH 2 , whereas strain 14DCB1 preferentially dechlorinated Cl that has an ortho H. For the CBDB1-mediated dechlorination, comparative analysis with Hirshfeld charges shows that the least-negative Cl discriminates active from nonactive substrates in 14 out of 15 cases and may represent the preferred site of primary attack through cob(I)alamin. For the latter trend, three of seven active substrates provide strong evidence, with partial support from three of the remaining four substrates. Regarding strain 14DCB1, the most positive carbon-attached H atom discriminates active from nonactive chloroanilines in again 14 out of 15 cases. Here, regioselectivity is governed for 10 of the 11 active substrates by the most positive H attached to the highest-charge (most positive or least negative) aromatic C carrying the Cl to be removed. These findings suggest the aromatic ring H as primary site of attack through the supernucleophile Co(I), converting an initial H bond to a full electron transfer as start of the reductive dehalogenation. For both mechanisms, one- and two-electron transfer to Cl (strain CBDB1) or H (strain 14DCB1) are compatible with the presently available data. Computational chemistry research into reaction intermediates and pathways may further aid in understanding the bacterial reductive dehalogenation at the molecular level.

Genome-scale metabolic reconstructions and theoretical investigation of methane conversion in Methylomicrobium buryatense strain 5G(B1).

PubMed

de la Torre, Andrea; Metivier, Aisha; Chu, Frances; Laurens, Lieve M L; Beck, David A C; Pienkos, Philip T; Lidstrom, Mary E; Kalyuzhnaya, Marina G

2015-11-25

Methane-utilizing bacteria (methanotrophs) are capable of growth on methane and are attractive systems for bio-catalysis. However, the application of natural methanotrophic strains to large-scale production of value-added chemicals/biofuels requires a number of physiological and genetic alterations. An accurate metabolic model coupled with flux balance analysis can provide a solid interpretative framework for experimental data analyses and integration. A stoichiometric flux balance model of Methylomicrobium buryatense strain 5G(B1) was constructed and used for evaluating metabolic engineering strategies for biofuels and chemical production with a methanotrophic bacterium as the catalytic platform. The initial metabolic reconstruction was based on whole-genome predictions. Each metabolic step was manually verified, gapfilled, and modified in accordance with genome-wide expression data. The final model incorporates a total of 841 reactions (in 167 metabolic pathways). Of these, up to 400 reactions were recruited to produce 118 intracellular metabolites. The flux balance simulations suggest that only the transfer of electrons from methanol oxidation to methane oxidation steps can support measured growth and methane/oxygen consumption parameters, while the scenario employing NADH as a possible source of electrons for particulate methane monooxygenase cannot. Direct coupling between methane oxidation and methanol oxidation accounts for most of the membrane-associated methane monooxygenase activity. However the best fit to experimental results is achieved only after assuming that the efficiency of direct coupling depends on growth conditions and additional NADH input (about 0.1-0.2 mol of incremental NADH per one mol of methane oxidized). The additional input is proposed to cover loss of electrons through inefficiency and to sustain methane oxidation at perturbations or support uphill electron transfer. Finally, the model was used for testing the carbon conversion efficiency of different pathways for C1-utilization, including different variants of the ribulose monophosphate pathway and the serine cycle. We demonstrate that the metabolic model can provide an effective tool for predicting metabolic parameters for different nutrients and genetic perturbations, and as such, should be valuable for metabolic engineering of the central metabolism of M. buryatense strains.

Electrode architectures for efficient electronic and ionic transport pathways in high power lithium ion batteries

NASA Astrophysics Data System (ADS)

Faulkner, Ankita Shah

As the demand for clean energy sources increases, large investments have supported R&D programs aimed at developing high power lithium ion batteries for electric vehicles, military, grid storage and space applications. State of the art lithium ion technology cannot meet power demands for these applications due to high internal resistances in the cell. These resistances are mainly comprised of ionic and electronic resistance in the electrode and electrolyte. Recently, much attention has been focused on the use of nanoscale lithium ion active materials on the premise that these materials shorten the diffusion length of lithium ions and increase the surface area for electrochemical charge transfer. While, nanomaterials have allowed significant improvements in the power density of the cell, they are not a complete solution for commercial batteries. Due to their large surface area, they introduce new challenges such as a poor electrode packing densities, high electrolyte reactivity, and expensive synthesis procedures. Since greater than 70% of the cost of the electric vehicle is due to the cost of the battery, a cost-efficient battery design is most critical. To address the limitations of nanomaterials, efficient transport pathways must be engineered in the bulk electrode. As a part of nanomanufacturing research being conducted the Center for High-rate Nanomanufacturing at Northeastern University, the first aim of the proposed work is to develop electrode architectures that enhance electronic and ionic transport pathways in large and small area lithium ion electrodes. These architectures will utilize the unique electronic and mechanical properties of carbon nanotubes to create robust electrode scaffolding that improves electrochemical charge transfer. Using extensive physical and electrochemical characterization, the second aim is to investigate the effect of electrode parameters on electrochemical performance and evaluate the performance against standard commercial electrodes. These parameters include surface morphology, electrode composition, electrode density, and operating temperature. Finally, the third aim is to investigate commercial viability of the electrode architecture. This will be accomplished by developing pouch cell prototypes using a high-rate and low cost scale-up process. Through this work, we aim to realize a commercially viable high-power electrode technology.

Application of Bioelectrochemical Process (BES) for Electricity Generation and Sustainable Wastewater Treatment

NASA Astrophysics Data System (ADS)

Kim, Jung Rae

Bioelectrochemical system such as microbial fuel cells (MFCs) and microbial electrolysis cell are an emerging technology which converts biodegradable organic matter to electrical energy or hydrogen using a biofilm on the electrode as the biocatalyst. It has recently been shown that waste-to-energy technology based on MFC can treat organic contaminant in domestic or industrial wastewater and simultaneously produce electricity. The maximum power density increased up to 1kW/m3 based on reactor volume. Bioelectrochemical systems may reduce the energy consumption for wastewater treatment by replacing energy intensive aeration of present treatment systems, while generate electrical energy from waste. In addition, the biomass production in MFCs has been reported to be 10-50% of conventional wastewater treatment, leading to reduce environmental impact and disposal costs. Various electrochemically active bacteria metabolize biodegradable organic compounds then discharge electrons to an extracellular electron acceptor for bacterial respiration. These bacteria also transfer electrons to electrodes by direct electron transfer, electron mediators or shuttles, and electrically conductive nanowires. Investigation of bacterial electron transport mechanisms may improve understanding of the biomaterial involved and metabolic pathways as well as improving power from MFCs. Biofuel cell systems require interdisciplinary research ranging from electrochemistry, microbiology, material science and surface chemistry to engineering such as reactor design, operation and modelling. Collaboration within each study and integration of systems might increase the performance and feasibility of BES process for sustainable energy.

Two-Photon Antenna-Core Oxygen Probe with Enhanced Performance

PubMed Central

2015-01-01

Recent development of two-photon phosphorescence lifetime microscopy (2PLM) of oxygen enabled first noninvasive high-resolution measurements of tissue oxygenation in vivo in 3D, providing valuable physiological information. The so far developed two-photon-enhanced phosphorescent probes comprise antenna-core constructs, in which two-photon absorbing chromophores (antenna) capture and channel excitation energy to a phosphorescent core (metalloporphyrin) via intramolecular excitation energy transfer (EET). These probes allowed demonstration of the methods’ potential; however, they suffer from a number of limitations, such as partial loss of emissivity to competing triplet state deactivation pathways (e.g., electron transfer) and suboptimal sensitivity to oxygen, thereby limiting spatial and temporal resolution of the method. Here we present a new probe, PtTCHP-C307, designed to overcome these limitations. The key improvements include significant increase in the phosphorescence quantum yield, higher efficiency of the antenna-core energy transfer, minimized quenching of the phosphorescence by electron transfer and increased signal dynamic range. For the same excitation flux, the new probe is able to produce up to 6-fold higher signal output than previously reported molecules. Performance of PtTCHP-C307 was demonstrated in vivo in pO2 measurements through the intact mouse skull into the bone marrow, where all blood cells are made from hematopoietic stem cells. PMID:24848643

Control of electron transport routes through redox-regulated redistribution of respiratory complexes

PubMed Central

Liu, Lu-Ning; Bryan, Samantha J.; Huang, Fang; Yu, Jianfeng; Nixon, Peter J.; Rich, Peter R.; Mullineaux, Conrad W.

2012-01-01

In cyanobacteria, respiratory electron transport takes place in close proximity to photosynthetic electron transport, because the complexes required for both processes are located within the thylakoid membranes. The balance of electron transport routes is crucial for cell physiology, yet the factors that control the predominance of particular pathways are poorly understood. Here we use a combination of tagging with green fluorescent protein and confocal fluorescence microscopy in live cells of the cyanobacterium Synechococcus elongatus PCC 7942 to investigate the distribution on submicron scales of two key respiratory electron donors, type-I NAD(P)H dehydrogenase (NDH-1) and succinate dehydrogenase (SDH). When cells are grown under low light, both complexes are concentrated in discrete patches in the thylakoid membranes, about 100–300 nm in diameter and containing tens to hundreds of complexes. Exposure to moderate light leads to redistribution of both NDH-1 and SDH such that they become evenly distributed within the thylakoid membranes. The effects of electron transport inhibitors indicate that redistribution of respiratory complexes is triggered by changes in the redox state of an electron carrier close to plastoquinone. Redistribution does not depend on de novo protein synthesis, and it is accompanied by a major increase in the probability that respiratory electrons are transferred to photosystem I rather than to a terminal oxidase. These results indicate that the distribution of complexes on the scale of 100–300 nm controls the partitioning of reducing power and that redistribution of electron transport complexes on these scales is a physiological mechanism to regulate the pathways of electron flow. PMID:22733774

Pivotal Role of Iron in the Regulation of Cyanobacterial Electron Transport.

PubMed

González, A; Sevilla, E; Bes, M T; Peleato, M L; Fillat, M F

2016-01-01

Iron-containing metalloproteins are the main cornerstones for efficient electron transport in biological systems. The abundance and diversity of iron-dependent proteins in cyanobacteria makes those organisms highly dependent of this micronutrient. To cope with iron imbalance, cyanobacteria have developed a survey of adaptation strategies that are strongly related to the regulation of photosynthesis, nitrogen metabolism and other central electron transfer pathways. Furthermore, either in its ferrous form or as a component of the haem group, iron plays a crucial role as regulatory signalling molecule that directly or indirectly modulates the composition and efficiency of cyanobacterial redox reactions. We present here the major mechanism used by cyanobacteria to couple iron homeostasis to the regulation of electron transport, making special emphasis in processes specific in those organisms. © 2016 Elsevier Ltd. All rights reserved.

Analysis of Borderline Substitution/Electron Transfer Pathways from Direct ab initio MD Simulations

DOE Office of Scientific and Technical Information (OSTI.GOV)

Yamataka, H; Aida, M A.; Dupuis, Michel

Ab initio molecular dynamics simulations were carried out for the borderline reaction pathways in the reaction of CH2O?- with CH3Cl. The simulations reveal distinctive features of three types of mechanisms passing through the SN2-like transition state (TS): (i) a direct formation of SN2 products, (ii) a direct formation of ET products, and (iii) a 2-step formation of ET products via the SN2 valley. The direct formation of the ET product through the SN2-like TS appears to be more favorable at higher temperatures. The 2-step process depends on the amount of energy that goes into the C-C stretching mode.

Autophagy Deficiency Compromises Alternative Pathways of Respiration following Energy Deprivation in Arabidopsis thaliana.

PubMed

Barros, Jessica A S; Cavalcanti, João Henrique F; Medeiros, David B; Nunes-Nesi, Adriano; Avin-Wittenberg, Tamar; Fernie, Alisdair R; Araújo, Wagner L

2017-09-01

Under heterotrophic conditions, carbohydrate oxidation inside the mitochondrion is the primary energy source for cellular metabolism. However, during energy-limited conditions, alternative substrates are required to support respiration. Amino acid oxidation in plant cells plays a key role in this by generating electrons that can be transferred to the mitochondrial electron transport chain via the electron transfer flavoprotein/ubiquinone oxidoreductase system. Autophagy, a catabolic mechanism for macromolecule and protein recycling, allows the maintenance of amino acid pools and nutrient remobilization. Although the association between autophagy and alternative respiratory substrates has been suggested, the extent to which autophagy and primary metabolism interact to support plant respiration remains unclear. To investigate the metabolic importance of autophagy during development and under extended darkness, Arabidopsis ( Arabidopsis thaliana ) mutants with disruption of autophagy ( atg mutants) were used. Under normal growth conditions, atg mutants showed lower growth and seed production with no impact on photosynthesis. Following extended darkness, atg mutants were characterized by signatures of early senescence, including decreased chlorophyll content and maximum photochemical efficiency of photosystem II coupled with increases in dark respiration. Transcript levels of genes involved in alternative pathways of respiration and amino acid catabolism were up-regulated in atg mutants. The metabolite profiles of dark-treated leaves revealed an extensive metabolic reprogramming in which increases in amino acid levels were partially compromised in atg mutants. Although an enhanced respiration in atg mutants was observed during extended darkness, autophagy deficiency compromises protein degradation and the generation of amino acids used as alternative substrates to the respiration. © 2017 American Society of Plant Biologists. All Rights Reserved.

Excitation energy transfer from the bacteriochlorophyll Soret band to carotenoids in the LH2 light-harvesting complex from Ectothiorhodospira haloalkaliphila is negligible.

PubMed

Razjivin, A P; Lukashev, E P; Kompanets, V O; Kozlovsky, V S; Ashikhmin, A A; Chekalin, S V; Moskalenko, A A; Paschenko, V Z

2017-09-01

Pathways of intramolecular conversion and intermolecular electronic excitation energy transfer (EET) in the photosynthetic apparatus of purple bacteria remain subject to debate. Here we experimentally tested the possibility of EET from the bacteriochlorophyll (BChl) Soret band to the singlet S 2 level of carotenoids using femtosecond pump-probe measurements and steady-state fluorescence excitation and absorption measurements in the near-ultraviolet and visible spectral ranges. The efficiency of EET from the Soret band of BChl to S 2 of the carotenoids in light-harvesting complex LH2 from the purple bacterium Ectothiorhodospira haloalkaliphila appeared not to exceed a few percent.

Quantum coherence selective 2D Raman–2D electronic spectroscopy

PubMed Central

Spencer, Austin P.; Hutson, William O.; Harel, Elad

2017-01-01

Electronic and vibrational correlations report on the dynamics and structure of molecular species, yet revealing these correlations experimentally has proved extremely challenging. Here, we demonstrate a method that probes correlations between states within the vibrational and electronic manifold with quantum coherence selectivity. Specifically, we measure a fully coherent four-dimensional spectrum which simultaneously encodes vibrational–vibrational, electronic–vibrational and electronic–electronic interactions. By combining near-impulsive resonant and non-resonant excitation, the desired fifth-order signal of a complex organic molecule in solution is measured free of unwanted lower-order contamination. A critical feature of this method is electronic and vibrational frequency resolution, enabling isolation and assignment of individual quantum coherence pathways. The vibronic structure of the system is then revealed within an otherwise broad and featureless 2D electronic spectrum. This method is suited for studying elusive quantum effects in which electronic transitions strongly couple to phonons and vibrations, such as energy transfer in photosynthetic pigment–protein complexes. PMID:28281541

Exosomes play an important role in the process of psoralen reverse multidrug resistance of breast cancer.

PubMed

Wang, Xiaohong; Xu, Chengfeng; Hua, Yitong; Sun, Leitao; Cheng, Kai; Jia, Zhongming; Han, Yong; Dong, Jianli; Cui, Yuzhen; Yang, Zhenlin

2016-12-01

Release of exosomes have been shown to play critical roles in drug resistance by delivering cargo. Targeting the transfer of exosomes from resistant cells to sensitive cells may be an approach to overcome some cases of drug resistance. In this study, we investigated the potential role of exosomes in the process of psoralen reverse multidrug resistance of MCF-7/ADR cells. Exosomes were isolated by differential centrifugation of culture media from MCF-7/ADR cells (ADR/exo) and MCF-7 parental cells (S/exo). Exosomes were characterized by morphology, exosomal markers and size distribution. The ability of ADR/exo to transfer multidrug resistance was assessed by MTT and real-time quantitative PCR. The different formation and secretion of exosomes were detected by immunofluorescence and transmission electron microscopy. Then we performed comparative transcriptomic analysis using RNA-Seq technology and real-time quantitative PCR to better understand the gene expression regulation in exosmes formation and release after psoralen treatment. Our data showed that exosomes derived from MCF-7/ADR cells were able to promote active sequestration of drugs and could induce a drug resistance phenotype by transferring drug-resistance-related gene MDR-1 and P-glycoprotein protein. Psoralen could reduce the formation and secretion of exosomes to overcome drug resistance. There were 21 differentially expressed genes. Gene ontology (GO) pathway analysis and Kyoto Encyclopedia of Genes and Genomes (KEGG) pathway analysis showed that the most significantly expressed genes were linked to PPAR and P53 signaling pathways which were related to exosomes formation, secretion and cargo sorting. Psoralen can affect the exosomes and induce the reduction of resistance transmission via exosomes might through PPAR and P53 signaling pathways, which might provide a novel strategy for breast cancer resistance to chemotherapy in the future.

Involvement of cyclic electron flow in irradiance stress responding and its potential regulation of the mechanisms in Pyropia yezoensis

NASA Astrophysics Data System (ADS)

Niu, Jianfeng; Feng, Jianhua; Xie, Xiujun; Gao, Shan; Wang, Guangce

2016-07-01

Pyropia yezoensis, belongs to the genus of Porphyra before 2011, inhabit on intertidal zone rocks where irradiation changes dramatically, implying that the seaweed has gained certain mechanisms to survive a harsh environment. Based on the photosynthetic parameters with or without the inhibitors determined by a Dual-PAM-100 apparatus, we investigated the photosynthetic performance and the changes in electron flow that occurred during the algae were stressed with different light intensities previously. When the irradiation saturation was approaching, the CEF around PS I became crucial since the addition of inhibitors usually led to an increase in non-photochemical quenching. The inhibitor experiments showed that there were at least three different CEF pathways in Py. yezoensis and these pathways compensated each other. In addition to maintaining a proper ratio of ATP/NAD(P)H to support efficient photosynthesis, the potential roles of CEF might also include the regulation of different photoprotective mechanisms in Py. yezoensis. Under the regulation of CEF, chlororespiration is thought to transport electrons from the reduced plastoquinone (PQ) pool to oxygen in order to mitigate the reduction in the electron transfer chain. When irradiation was up to the high-grade stress conditions, the relative value of CEF began to decrease, which implied that the NADP+ pool or PQ+ pool was very small and that the electrons were transferred from reduced PS I to oxygen. The scavenging enzymes might be activated and the water-water cycle probably became an effective means of removing the active oxygen produced by the irradiation stressed Py. yezoensis. We believe that the different mechanisms could make up the photoprotective network to allow Py. yezoensis for survival in a highly variable light stress habitat, which may enlighten scientists in future studies on irradiance stress in other algae species.

Spectroscopic elucidation of energy transfer in hybrid inorganic–biological organisms for solar-to-chemical production

DOE PAGES

Kornienko, Nikolay; Sakimoto, Kelsey K.; Herlihy, David M.; ...

2016-10-03

We present that the rise of inorganic–biological hybrid organisms for solar-to-chemical production has spurred mechanistic investigations into the dynamics of the biotic–abiotic interface to drive the development of next-generation systems. The model system, Moorella thermoacetica–cadmium sulfide (CdS), combines an inorganic semiconductor nanoparticle light harvester with an acetogenic bacterium to drive the photosynthetic reduction of CO 2 to acetic acid with high efficiency. In this work, we report insights into this unique electrotrophic behavior and propose a charge-transfer mechanism from CdS to M. thermoacetica. Transient absorption (TA) spectroscopy revealed that photoexcited electron transfer rates increase with increasing hydrogenase (H 2ase) enzymemore » activity. On the same time scale as the TA spectroscopy, time-resolved infrared (TRIR) spectroscopy showed spectral changes in the 1,700–1,900-cm -1 spectral region. The quantum efficiency of this system for photosynthetic acetic acid generation also increased with increasing H 2ase activity and shorter carrier lifetimes when averaged over the first 24 h of photosynthesis. However, within the initial 3 h of photosynthesis, the rate followed an opposite trend: The bacteria with the lowest H 2ase activity photosynthesized acetic acid the fastest. These results suggest a two-pathway mechanism: a high quantum efficiency charge-transfer pathway to H 2ase generating H 2 as a molecular intermediate that dominates at long time scales (24 h), and a direct energy-transducing enzymatic pathway responsible for acetic acid production at short time scales (3 h). Lastly, this work represents a promising platform to utilize conventional spectroscopic methodology to extract insights from more complex biotic–abiotic hybrid systems.« less

Spectroscopic elucidation of energy transfer in hybrid inorganic-biological organisms for solar-to-chemical production.

PubMed

Kornienko, Nikolay; Sakimoto, Kelsey K; Herlihy, David M; Nguyen, Son C; Alivisatos, A Paul; Harris, Charles B; Schwartzberg, Adam; Yang, Peidong

2016-10-18

The rise of inorganic-biological hybrid organisms for solar-to-chemical production has spurred mechanistic investigations into the dynamics of the biotic-abiotic interface to drive the development of next-generation systems. The model system, Moorella thermoacetica-cadmium sulfide (CdS), combines an inorganic semiconductor nanoparticle light harvester with an acetogenic bacterium to drive the photosynthetic reduction of CO 2 to acetic acid with high efficiency. In this work, we report insights into this unique electrotrophic behavior and propose a charge-transfer mechanism from CdS to M. thermoacetica Transient absorption (TA) spectroscopy revealed that photoexcited electron transfer rates increase with increasing hydrogenase (H 2 ase) enzyme activity. On the same time scale as the TA spectroscopy, time-resolved infrared (TRIR) spectroscopy showed spectral changes in the 1,700-1,900-cm -1 spectral region. The quantum efficiency of this system for photosynthetic acetic acid generation also increased with increasing H 2 ase activity and shorter carrier lifetimes when averaged over the first 24 h of photosynthesis. However, within the initial 3 h of photosynthesis, the rate followed an opposite trend: The bacteria with the lowest H 2 ase activity photosynthesized acetic acid the fastest. These results suggest a two-pathway mechanism: a high quantum efficiency charge-transfer pathway to H 2 ase generating H 2 as a molecular intermediate that dominates at long time scales (24 h), and a direct energy-transducing enzymatic pathway responsible for acetic acid production at short time scales (3 h). This work represents a promising platform to utilize conventional spectroscopic methodology to extract insights from more complex biotic-abiotic hybrid systems.

Redox regulation of energy transfer efficiency in antennas of green photosynthetic bacteria

NASA Technical Reports Server (NTRS)

Blankenship, R. E.; Cheng, P.; Causgrove, T. P.; Brune, D. C.; Wang, J.

1993-01-01

The efficiency of energy transfer from the peripheral chlorosome antenna structure to the membrane-bound antenna in green sulfur bacteria depends strongly on the redox potential of the medium. The fluorescence spectra and lifetimes indicate that efficient quenching pathways are induced in the chlorosome at high redox potential. The midpoint redox potential for the induction of this effect in isolated chlorosomes from Chlorobium vibrioforme is -146 mV at pH 7 (vs the normal hydrogen electrode), and the observed midpoint potential (n = 1) decreases by 60 mV per pH unit over the pH range 7-10. Extraction of isolated chlorosomes with hexane has little effect on the redox-induced quenching, indicating that the component(s) responsible for this effect are bound and not readily extractable. We have purified and partially characterized the trimeric water-soluble bacteriochlorophyll a-containing protein from the thermophilic green sulfur bacterium Chlorobium tepidum. This protein is located between the chlorosome and the membrane. Fluorescence spectra of the purified protein indicate that it also contains groups that quench excitations at high redox potential. The results indicate that the energy transfer pathway in green sulfur bacteria is regulated by redox potential. This regulation appears to operate in at least two distinct places in the energy transfer pathway, the oligomeric pigments in the interior of the chlorosome and in the bacteriochlorophyll a protein. The regulatory effect may serve to protect the cell against superoxide-induced damage when oxygen is present. By quenching excitations before they reach the reaction center, reduction and subsequent autooxidation of the low potential electron acceptors found in these organisms is avoided.

Mechanistic Insights into the Oxidation of Substituted Phenols via Hydrogen Atom Abstraction by a Cupric–Superoxo Complex

PubMed Central

2015-01-01

To obtain mechanistic insights into the inherent reactivity patterns for copper(I)–O2 adducts, a new cupric–superoxo complex [(DMM-tmpa)CuII(O2•–)]+ (2) [DMM-tmpa = tris((4-methoxy-3,5-dimethylpyridin-2-yl)methyl)amine] has been synthesized and studied in phenol oxidation–oxygenation reactions. Compound 2 is characterized by UV–vis, resonance Raman, and EPR spectroscopies. Its reactions with a series of para-substituted 2,6-di-tert-butylphenols (p-X-DTBPs) afford 2,6-di-tert-butyl-1,4-benzoquinone (DTBQ) in up to 50% yields. Significant deuterium kinetic isotope effects and a positive correlation of second-order rate constants (k2) compared to rate constants for p-X-DTBPs plus cumylperoxyl radical reactions indicate a mechanism that involves rate-limiting hydrogen atom transfer (HAT). A weak correlation of (kBT/e) ln k2 versus Eox of p-X-DTBP indicates that the HAT reactions proceed via a partial transfer of charge rather than a complete transfer of charge in the electron transfer/proton transfer pathway. Product analyses, 18O-labeling experiments, and separate reactivity employing the 2,4,6-tri-tert-butylphenoxyl radical provide further mechanistic insights. After initial HAT, a second molar equiv of 2 couples to the phenoxyl radical initially formed, giving a CuII–OO–(ArO′) intermediate, which proceeds in the case of p-OR-DTBP substrates via a two-electron oxidation reaction involving hydrolysis steps which liberate H2O2 and the corresponding alcohol. By contrast, four-electron oxygenation (O–O cleavage) mainly occurs for p-R-DTBP which gives 18O-labeled DTBQ and elimination of the R group. PMID:24953129

Kinetics of interprotein electron transfer between cytochrome c6 and the soluble CuA domain of cyanobacterial cytochrome c oxidase.

PubMed

Paumann, Martina; Feichtinger, Markus; Bernroitner, Margit; Goldfuhs, Judith; Jakopitsch, Christa; Furtmüller, Paul G; Regelsberger, Günther; Peschek, Günter A; Obinger, Christian

2004-10-08

Cytochrome c6 is a soluble metalloprotein located in the periplasmic space and the thylakoid lumen of many cyanobacteria and is known to carry electrons from cytochrome b6f to photosystem I. The CuA domain of cytochrome c oxidase, the terminal enzyme which catalyzes the four-electron reduction of molecular oxygen in the respiratory chains of mitochondria and many bacteria, also has a periplasmic location. In order to test whether cytochrome c6 could also function as a donor for cytochrome c oxidase, we investigated the kinetics of the electron transfer between recombinant cytochrome c6 (produced in high yield in Escherichia coli by coexpressing the maturation proteins encoded by the ccmA-H gene cluster) and the recombinant soluble CuA domain (i.e., the donor binding and electron entry site) of subunit II of cytochrome c oxidase from Synechocystis PCC 6803. The forward and the reverse electron transfer reactions were studied by the stopped-flow technique and yielded apparent bimolecular rate constants of (3.3 +/- 0.3) x 10(5) M(-1) s(-1) and (3.9 +/- 0.1) x 10(6) M(-1) s(-1), respectively, in 5 mM potassium phosphate buffer, pH 7, containing 20 mM potassium chloride and 25 degrees C. This corresponds to an equilibrium constant Keq of 0.085 in the physiological direction (DeltarG'0 = 6.1 kJ/mol). The reduction of the CuA fragment by cytochrome c6 is almost independent on ionic strength, which is in contrast to the reaction of the CuA domain with horse heart cytochrome c, which decreases with increasing ionic strength. The findings are discussed with respect to the potential role of cytochrome c6 as mobile electron carrier in both cyanobacterial electron transport pathways. Copyright 2004 Federation of European Biochemical Societies

The dynamics of energy and charge transfer in low and hyperthermal energy ion-solid interactions

NASA Astrophysics Data System (ADS)

Ray, Matthew Preston

The energy and charge transfer dynamics for low and hyperthermal energy (10 eV to 2 keV) alkali and noble gas ions impacting noble metals as a function of incident energy, species and scattering geometry has been studied. The experiments were performed in an ultra-high vacuum scattering chamber attached to a low and hyperthermal energy beamline. The energy transfer was measured for K+ scattered from a Ag(001) surface along the [110] crystalline direction at a fixed laboratory angle of 90°. It was found that as the incident energy is reduced from 100 to 10 eV, the normalized scattered energy increased. Previous measurements have shown a decrease in the normalized energy as the incident ion energy is reduced due to an attractive image force. Trajectory analysis of the data using a classical scattering simulation revealed that instead of undergoing sequential binary collisions as in previous studies, the ion scatters from two surface atoms simultaneously leading to an increased normalized energy. Additionally, charge transfer measurements have been performed for Na + scattering from Ag(001) along the [110] crystalline direction at a fixed laboratory angle of 70°. It was found that over the range of energies used (10 eV to 2 keV), the neutralization probability of the scattered ions varied from ˜30% to ˜70% depending on the incident velocity, consistent with resonant charge transfer. A fully quantum mechanical model that treats electrons independently accurately reproduces the observed data. Measurements of electron-hole pair excitations were used to explore the pathways which a solid uses to dissipate the energy imparted by the incident ion beam. Ultrathin film (10 nm) metal-oxide-semiconductor (Au/SiO2/n-Si) devices were used to detect the electron-hole pairs for cases when the ion deposited all of its translational energy into the solid. The incident ions were incident at an angle normal to the surface of the device to maximize energy deposition and consequently electron-hole pair production. The rectifying metal-oxide-semiconductor device separates the electrons from the holes, allowing a current associated with electron-hole pair production to be measured. In these experiments a number of ion species (He+, Li+ , Ar+, K+) were made incident on multiple devices and the incident energy ranged from 100 eV to 2 keV. It was found that electron-hole pair production increased with incident ion velocity consistent with a kinetic electron excitation model where the electrons in the metal are partially confined to the surface.

Quadrupolar transfer pathways

NASA Astrophysics Data System (ADS)

Antonijevic, Sasa; Bodenhausen, Geoffrey

2006-06-01

A set of graphical conventions called quadrupolar transfer pathways is proposed to describe a wide range of experiments designed for the study of quadrupolar nuclei with spin quantum numbers I = 1, 3/2, 2, 5/2, etc. These pathways, which inter alea allow one to appreciate the distinction between quadrupolar and Zeeman echoes, represent a generalization of the well-known coherence transfer pathways. Quadrupolar transfer pathways not merely distinguish coherences with different orders -2 I ⩽ p ⩽ +2 I, but allow one to follow the fate of coherences associated with single transitions that have the same coherence orderp=mIr-mIs but can be distinguished by a satellite orderq=(mIr)2-(mIs)2.

Quadrupolar transfer pathways.

PubMed

Antonijevic, Sasa; Bodenhausen, Geoffrey

2006-06-01

A set of graphical conventions called quadrupolar transfer pathways is proposed to describe a wide range of experiments designed for the study of quadrupolar nuclei with spin quantum numbers I=1, 3/2, 2, 5/2, etc. These pathways, which inter alea allow one to appreciate the distinction between quadrupolar and Zeeman echoes, represent a generalization of the well-known coherence transfer pathways. Quadrupolar transfer pathways not merely distinguish coherences with different orders -2I < or = p< or = +2I, but allow one to follow the fate of coherences associated with single transitions that have the same coherence order p=m(I)(r)-m(I)(s) but can be distinguished by a satellite order q=(m(I)(r))(2)-(m(I)(s))(2).

Construction and direct electrochemistry of orientation controlled laccase electrode

DOE Office of Scientific and Technical Information (OSTI.GOV)

Li, Ying; Zhang, Jiwei; Huang, Xirong, E-mail: xrhuang@sdu.edu.cn

2014-03-28

Highlights: • A recombinant laccase with Cys-6×His tag at the N or C terminus was generated. • Orientation controlled laccase electrodes were constructed via self assembly. • The electrochemical behavior of laccase electrodes was orientation dependent. • The C terminus tagged laccase was better for bioelectrocatalytic reduction of O{sub 2}. - Abstract: A laccase has multiple redox centres. Chemisorption of laccases on a gold electrode through a polypeptide tag introduced at the protein surface provides an isotropic orientation of laccases on the Au surface, which allows the orientation dependent study of the direct electrochemistry of laccase. In this paper, usingmore » genetic engineering technology, two forms of recombinant laccase which has Cys-6×His tag at the N or C terminus were generated. Via the Au-S linkage, the recombinant laccase was assembled orientationally on gold electrode. A direct electron transfer and a bioelectrocatalytic activity toward oxygen reduction were observed on the two orientation controlled laccase electrodes, but their electrochemical behaviors were found to be quite different. The orientation of laccase on the gold electrode affects both the electron transfer pathway and the electron transfer efficiency of O{sub 2} reduction. The present study is helpful not only to the in-depth understanding of the direct electrochemistry of laccase, but also to the development of laccase-based biofuel cells.« less

Quantum Computational Studies of Electron Transfer in Respiratory Complex III and its Application for Designing New Mitocan Drugs

NASA Astrophysics Data System (ADS)

Hagras, Muhammad Ahmed

Electron transfer occurs in many biological systems which are imperative to sustain life; oxidative phosphorylation in prokaryotes and eukaryotes, and photophosphorylation in photosynthetic and plant cells are well-balanced and complementary processes. Investigating electron transfer in those natural systems provides detailed knowledge of the atomistic events that lead eventually to production of ATP, or harvesting light energy. Ubiquinol:cytochrome c oxidoreductase complex (also known as bc 1 complex, or respiratory complex III) is a middle player in the electron transport proton pumping orchestra, located in the inner-mitochondrial membrane in eukaryotes or plasma membrane in prokaryotes, which converts the free energy of redox reactions to electrochemical proton gradient across the membrane, following the fundamental chemiosmotic principle discovered by Peter Mitchell 1. In humans, the malfunctioned bc1 complex plays a major role in many neurodegenerative diseases, stress-induced aging, and cancer development, because it produces most of the reactive oxygen species, which are also involved in cellular signaling 2. The mitochondrial bc1 complex has an intertwined dimeric structure comprised of 11 subunits in each monomer, but only three of them have catalytic function, and those are the only domains found in bacterial bc1 complex. The core subunits include: Rieske domain, which incorporates iron-sulfur cluster [2Fe-2S]; trans-membrane cytochrome b domain, incorporating low-potential heme group (heme b L) and high-potential heme group (heme b H); and cytochrome c1 domain, containing heme c1 group and two separate binding sites, Qo (or QP) site where the hydrophobic electron carrier ubihydroquinol QH2 is oxidized, and Qi (or QN) site where ubiquinone molecule Q is reduced 3. Electrons and protons in the bc1 complex flow according to the proton-motive Q-cycle proposed by Mitchell, which includes a unique electron flow bifurcation at the Qo site. At this site, one electron of a bound QH2 molecule transfers to [2Fe-2S] cluster of the Rieske domain, docked at the proximal docking site, and another electron transfers to heme b L , which subsequently passes it to heme bH , and finally to Q or SQ molecule bound at the Qi-site 4. Rieske domain undergoes a domain movement 22 A to bind at the distal docking site, where [2Fe-2S] cluster passes its electron to heme c1, which in turn passes it to heme c of the water-soluble cytochrome c carrier 3c, 5 (which shuttles it to cytochrome c oxidase, complex IV). In the current compiled work presented in the subsequent chapters, we deployed a stacking tiers hierarchy where each chapter's work presents a foundation for the next one. In chapter 1, we first present different methods to calculate tunneling currents in proteins including a new derivation method for the inter-atomic tunneling current method. In addition, we show the results of the inter-atomic tunneling current theory on models based on heme bL-heme bH redox pair system in bc1 complex. Afterwards, in chapter 2, we examine the electron tunneling pathways 6 between different intra-monomeric and inter-monomeric redox centers of bc1 complex, including its electron carriers - ubiquinol, ubiquinone, and cytochrome c molecules, using the well-studied coarse-grained interatomic method of the tunneling current theory 7. Going through the different tunneling pathways in bc1 complex, we discovered a pair of internal switches that modulate the electron transfer rate which we discuss in full details in chapter 3. Motivated by the discovery of those internal switches, we discuss in chapter 4 the discovery of a new binding pocket (designated as NonQ-site or NQ-site for short) in bc 1 complex which is located at the opposite side of the enzyme with respect to Qo site. In contrast to Qo site, however, the NQ-site penetrates deeply in the cytochrome b domain and reaches very closely the LH region. Hence the NQ-site provides a suitable binding pocket for ligands that can influence the orientation of Phe90 residue, and hence modulate the corresponding ET rate between heme b L and heme bH. Finally we present in chapter 5 our unique integrated software package (called Electron Tunneling in Proteins Program or ETP) which provides an environment with different capabilities such as tunneling current calculation, semi-empirical quantum mechanical calculation and molecular modeling simulation for calculation and analysis of electron transfer reactions in proteins.

Effects of the Herbicide Imazethapyr on Photosynthesis in PGR5- and NDH-Deficient Arabidopsis thaliana at the Biochemical, Transcriptomic, and Proteomic Levels.

PubMed

Sun, Chongchong; Chen, Si; Jin, Yujian; Song, Hao; Ruan, Songlin; Fu, Zhengwei; Asad, Muhammad Asad Ullah; Qian, Haifeng

2016-06-08

Photosynthesis is a very important metabolic pathway for plant growth and crop yield. This report investigated the effect of the herbicide imazethapyr on photosynthesis in the Arabidopsis thaliana pnsB3 mutant (a defect in the NDH pathway) and pgr5 mutant (a defect in the PGR5 pathway) to determine which cyclic electron transport chain (CET) of the NDH and PGR5 pathways is more important for protecting the photosynthetic system under herbicide stress. The results showed that 20 μg/L imazethapyr markedly inhibited the growth of the three ecotypes of A. thaliana and produced more anthocyanins and reactive oxygen species (ROS), particularly in the pgr5 mutant. The chlorophyll fluorescence results showed that PSII was severely damaged in the pgr5 mutant. Additionally, the CET was significantly stimulated to protect the photosynthetic system from light damage in Wt and the pnsB3 mutant but not the pgr5 mutant. The real-time PCR analysis indicated that imazethapyr treatment considerably decreased the transcript levels of most photosynthesis-related genes in the three treated groups. Several genes in the PGR5 pathway were significantly induced in the pnsB3 mutant, but no genes in the NDH pathway were induced in the pgr5 mutant. The gene transcription analysis showed that the pgr5 mutant cannot compensate for the deficit in the PGR5 pathway by stimulating the NDH pathway, whereas the pnsB3 mutant can compensate for the deficit in the CET cycle by regulating the PGR5 pathway. The iTRAQ analyses also showed that the photosynthesis system, glycolysis, and TCA cycle suffered the most severe damage in the pgr5 mutant. All of these results showed that the PGR5 pathway is more critical for electron transfer around PSI than the NDH pathway to resist herbicide stress.

The Mg2+-containing Water Cluster of Mammalian Cytochrome c Oxidase Collects Four Pumping Proton Equivalents in Each Catalytic Cycle*

PubMed Central

Yano, Naomine; Muramoto, Kazumasa; Shimada, Atsuhiro; Takemura, Shuhei; Baba, Junpei; Fujisawa, Hidenori; Mochizuki, Masao; Shinzawa-Itoh, Kyoko; Yamashita, Eiki; Tsukihara, Tomitake; Yoshikawa, Shinya

2016-01-01

Bovine heart cytochrome c oxidase (CcO) pumps four proton equivalents per catalytic cycle through the H-pathway, a proton-conducting pathway, which includes a hydrogen bond network and a water channel operating in tandem. Protons are transferred by H3O+ through the water channel from the N-side into the hydrogen bond network, where they are pumped to the P-side by electrostatic repulsion between protons and net positive charges created at heme a as a result of electron donation to O2 bound to heme a3. To block backward proton movement, the water channel remains closed after O2 binding until the sequential four-proton pumping process is complete. Thus, the hydrogen bond network must collect four proton equivalents before O2 binding. However, a region with the capacity to accept four proton equivalents was not discernable in the x-ray structures of the hydrogen bond network. The present x-ray structures of oxidized/reduced bovine CcO are improved from 1.8/1.9 to 1.5/1.6 Å resolution, increasing the structural information by 1.7/1.6 times and revealing that a large water cluster, which includes a Mg2+ ion, is linked to the H-pathway. The cluster contains enough proton acceptor groups to retain four proton equivalents. The redox-coupled x-ray structural changes in Glu198, which bridges the Mg2+ and CuA (the initial electron acceptor from cytochrome c) sites, suggest that the CuA-Glu198-Mg2+ system drives redox-coupled transfer of protons pooled in the water cluster to the H-pathway. Thus, these x-ray structures indicate that the Mg2+-containing water cluster is the crucial structural element providing the effective proton pumping in bovine CcO. PMID:27605664

The Mg2+-containing Water Cluster of Mammalian Cytochrome c Oxidase Collects Four Pumping Proton Equivalents in Each Catalytic Cycle.

PubMed

Yano, Naomine; Muramoto, Kazumasa; Shimada, Atsuhiro; Takemura, Shuhei; Baba, Junpei; Fujisawa, Hidenori; Mochizuki, Masao; Shinzawa-Itoh, Kyoko; Yamashita, Eiki; Tsukihara, Tomitake; Yoshikawa, Shinya

2016-11-11

Bovine heart cytochrome c oxidase (CcO) pumps four proton equivalents per catalytic cycle through the H-pathway, a proton-conducting pathway, which includes a hydrogen bond network and a water channel operating in tandem. Protons are transferred by H 3 O + through the water channel from the N-side into the hydrogen bond network, where they are pumped to the P-side by electrostatic repulsion between protons and net positive charges created at heme a as a result of electron donation to O 2 bound to heme a 3 To block backward proton movement, the water channel remains closed after O 2 binding until the sequential four-proton pumping process is complete. Thus, the hydrogen bond network must collect four proton equivalents before O 2 binding. However, a region with the capacity to accept four proton equivalents was not discernable in the x-ray structures of the hydrogen bond network. The present x-ray structures of oxidized/reduced bovine CcO are improved from 1.8/1.9 to 1.5/1.6 Å resolution, increasing the structural information by 1.7/1.6 times and revealing that a large water cluster, which includes a Mg 2+ ion, is linked to the H-pathway. The cluster contains enough proton acceptor groups to retain four proton equivalents. The redox-coupled x-ray structural changes in Glu 198 , which bridges the Mg 2+ and Cu A (the initial electron acceptor from cytochrome c) sites, suggest that the Cu A -Glu 198 -Mg 2+ system drives redox-coupled transfer of protons pooled in the water cluster to the H-pathway. Thus, these x-ray structures indicate that the Mg 2+ -containing water cluster is the crucial structural element providing the effective proton pumping in bovine CcO. © 2016 by The American Society for Biochemistry and Molecular Biology, Inc.

Fine Tuning of Redox Networks on Multiheme Cytochromes from Geobacter sulfurreducens Drives Physiological Electron/Proton Energy Transduction

PubMed Central

Morgado, Leonor; Dantas, Joana M.; Bruix, Marta; Londer, Yuri Y.; Salgueiro, Carlos A.

2012-01-01

The bacterium Geobacter sulfurreducens (Gs) can grow in the presence of extracellular terminal acceptors, a property that is currently explored to harvest electricity from aquatic sediments and waste organic matter into microbial fuel cells. A family composed of five triheme cytochromes (PpcA-E) was identified in Gs. These cytochromes play a crucial role by bridging the electron transfer from oxidation of cytoplasmic donors to the cell exterior and assisting the reduction of extracellular terminal acceptors. The detailed thermodynamic characterization of such proteins showed that PpcA and PpcD have an important redox-Bohr effect that might implicate these proteins in the e−/H+ coupling mechanisms to sustain cellular growth. The physiological relevance of the redox-Bohr effect in these proteins was studied by determining the fractional contribution of each individual redox-microstate at different pH values. For both proteins, oxidation progresses from a particular protonated microstate to a particular deprotonated one, over specific pH ranges. The preferred e−/H+ transfer pathway established by the selected microstates indicates that both proteins are functionally designed to couple e−/H+ transfer at the physiological pH range for cellular growth. PMID:22899897

A lactate electrochemical biosensor with a titanate nanotube as direct electron transfer promoter

NASA Astrophysics Data System (ADS)

Yang, Mingli; Wang, Jin; Li, Huaqing; Zheng, Jian-Guo; Wu, Nianqiang Nick

2008-02-01

Hydrogen titanate (H2Ti3O7) nanotubes (TNTs) have been synthesized by a one-step hydrothermal processing. Lactate oxidase (LOx) enzyme has been immobilized on the three-dimensional porous TNT network to make an electrochemical biosensor for lactate detection. Cyclic voltammetry and amperometry tests reveal that the LOx enzyme, which is supported on TNTs, maintains their substrate-specific catalytic activity. The nanotubes offer the pathway for direct electron transfer between the electrode surface and the active redox centers of LOx, which enables the biosensor to operate at a low working potential and to avoid the influence of the presence of O2 on the amperometric current response. The biosensor exhibits a sensitivity of 0.24 µA cm-2 mM-1, a 90% response time of 5 s, and a linear response in the range from 0.5 to 14 mM and the redox center of enzyme obviates the need of redox mediators for electrochemical enzymatic sensors, which is attractive for the development of reagentless biosensors.

Polarized electrode enhances biological direct interspecies electron transfer for methane production in upflow anaerobic bioelectrochemical reactor.

PubMed

Feng, Qing; Song, Young-Chae; Yoo, Kyuseon; Kuppanan, Nanthakumar; Subudhi, Sanjukta; Lal, Banwari

2018-08-01

The influence of polarized electrodes on the methane production, which depends on the sludge concentration, was investigated in upflow anaerobic bioelectrochemical (UABE) reactor. When the polarized electrode was placed in the bottom zone with a high sludge concentration, the methane production was 5.34 L/L.d, which was 53% higher than upflow anaerobic sludge blanket (UASB) reactor. However, the methane production was reduced to 4.34 L/L.d by placing the electrode in the upper zone of the UABE reactor with lower sludge concentration. In the UABE reactor, the methane production was mainly improved by the enhanced biological direct interspecies electron transfer (bDIET) pathway, and the methane production via the electrode was a minor fraction of less than 4% of total methane production. The polarized electrodes that placed in the bottom zone with a high sludge concentration enhance the bDIET for methane production in the UABE reactor and greatly improve the methane production. Copyright © 2018. Published by Elsevier Ltd.

Resonance Raman spectra of organic molecules absorbed on inorganic semiconducting surfaces: Contribution from both localized intramolecular excitation and intermolecular charge transfer excitation

DOE Office of Scientific and Technical Information (OSTI.GOV)

Ye, ChuanXiang; Zhao, Yi, E-mail: yizhao@xmu.edu.cn, E-mail: liangwz@xmu.edu.cn; Liang, WanZhen, E-mail: yizhao@xmu.edu.cn, E-mail: liangwz@xmu.edu.cn

2015-10-21

The time-dependent correlation function approach for the calculations of absorption and resonance Raman spectra (RRS) of organic molecules absorbed on semiconductor surfaces [Y. Zhao and W. Z. Liang, J. Chem. Phys. 135, 044108 (2011)] is extended to include the contribution of the intermolecular charge transfer (CT) excitation from the absorbers to the semiconducting nanoparticles. The results demonstrate that the bidirectionally interfacial CT significantly modifies the spectral line shapes. Although the intermolecular CT excitation makes the absorption spectra red shift slightly, it essentially changes the relative intensities of mode-specific RRS and causes the oscillation behavior of surface enhanced Raman spectra withmore » respect to interfacial electronic couplings. Furthermore, the constructive and destructive interferences of RRS from the localized molecular excitation and CT excitation are observed with respect to the electronic coupling and the bottom position of conductor band. The interferences are determined by both excitation pathways and bidirectionally interfacial CT.« less

Quenching mechanism of Zn(salicylaldimine) by nitroaromatics.

PubMed

Germain, Meaghan E; Vargo, Thomas R; McClure, Beth Anne; Rack, Jeffrey J; Van Patten, P Gregory; Odoi, Michael; Knapp, Michael J

2008-07-21

Nitroaromatics and nitroalkanes quench the fluorescence of Zn(Salophen) (H2Salophen = N,N'-phenylene-bis-(3,5-di- tert-butylsalicylideneimine); ZnL(R)) complexes. A structurally related family of ZnL(R) complexes (R = OMe, di-tBu, tBu, Cl, NO2) were prepared, and the mechanisms of fluorescence quenching by nitroaromatics were studied by a combined kinetics and spectroscopic approach. The fluorescent quantum yields for ZnL(R) were generally high (Phi approximately 0.3) with sub-nanosecond fluorescence lifetimes. The fluorescence of ZnL(R) was quenched by nitroaromatic compounds by a mixture of static and dynamic pathways, reflecting the ZnL(R) ligand bulk and reduction potential. Steady-state Stern-Volmer plots were curved for ZnL(R) with less-bulky substituents (R = OMe, NO2), suggesting that both static and dynamic pathways were important for quenching. Transient Stern-Volmer data indicated that the dynamic pathway dominated quenching for ZnL(R) with bulky substituents (R = tBu, DtBu). The quenching rate constants with varied nitroaromatics (ArNO2) followed the driving force dependence predicted for bimolecular electron transfer: ZnL* + ArNO2 --> ZnL(+) + ArNO2(-). A treatment of the diffusion-corrected quenching rates with Marcus theory yielded a modest reorganization energy (lambda = 25 kcal/mol), and a small self-exchange reorganization energy for ZnL*/ZnL(+) (ca. 20 kcal/mol) was estimated from the Marcus cross-relation, suggesting that metal phenoxyls may be robust biological redox cofactors. Electronic structure calculations indicated very small changes in bond distances for the ZnL --> ZnL(+) oxidation, suggesting that solvation was the dominant contributor to the observed reorganization energy. These mechanistic insights provide information that will be helpful to further develop ZnL(R) as sensors, as well as for potential photoinduced charge transfer chemistry.

Metagenomic Analyses of the Autotrophic Fe(II)-Oxidizing, Nitrate-Reducing Enrichment Culture KS

PubMed Central

Tominski, Claudia; Kappler, Andreas; Behrens, Sebastian

2016-01-01

Nitrate-dependent ferrous iron [Fe(II)] oxidation (NDFO) is a well-recognized chemolithotrophic pathway in anoxic sediments. The neutrophilic chemolithoautotrophic enrichment culture KS originally obtained from a freshwater sediment (K. L. Straub, M. Benz, B. Schink, and F. Widdel, Appl Environ Microbiol 62:1458–1460, 1996) has been used as a model system to study NDFO. However, the primary Fe(II) oxidizer in this culture has not been isolated, despite extensive efforts to do so. Here, we present a metagenomic analysis of this enrichment culture in order to gain insight into electron transfer pathways and the roles of different bacteria in the culture. We obtained a near-complete genome of the primary Fe(II) oxidizer, a species in the family Gallionellaceae, and draft genomes from its flanking community members. A search of the putative extracellular electron transfer pathways in these genomes led to the identification of a homolog of the MtoAB complex [a porin-multiheme cytochrome c system identified in neutrophilic microaerobic Fe(II)-oxidizing Sideroxydans lithotrophicus ES-1] in a Gallionellaceae sp., and findings of other putative genes involving cytochrome c and multicopper oxidases, such as Cyc2 and OmpB. Genome-enabled metabolic reconstruction revealed that this Gallionellaceae sp. lacks nitric oxide and nitrous oxide reductase genes and may partner with flanking populations capable of complete denitrification to avoid toxic metabolite accumulation, which may explain its resistance to growth in pure culture. This and other revealed interspecies interactions and metabolic interdependencies in nitrogen and carbon metabolisms may allow these organisms to cooperate effectively to achieve robust chemolithoautotrophic NDFO. Overall, the results significantly expand our knowledge of NDFO and suggest a range of genetic targets for further exploration. PMID:26896135

Tracing Single Electrons in a Disordered Polymer Film at Room Temperature.

PubMed

Wilma, Kevin; Issac, Abey; Chen, Zhijian; Würthner, Frank; Hildner, Richard; Köhler, Jürgen

2016-04-21

The transport of charges lies at the heart of essentially all modern (opto-) electronic devices. Although inorganic semiconductors built the basis for current technologies, organic materials have become increasingly important in recent years. However, organic matter is often highly disordered, which directly impacts the charge carrier dynamics. To understand and optimize device performance, detailed knowledge of the transport mechanisms of charge carriers in disordered matter is therefore of crucial importance. Here we report on the observation of the motion of single electrons within a disordered polymer film at room temperature, using single organic chromophores as probe molecules. The migration of a single electron gives rise to a varying electric field in its vicinity, which is registered via a shift of the emission spectra (Stark shift) of a chromophore. The spectral shifts allow us to determine the electron mobility and reveal for each nanoenvironment a distinct number of different possible electron-transfer pathways within the rugged energy landscape of the disordered polymer matrix.

Electron transport and light-harvesting switches in cyanobacteria

PubMed Central

Mullineaux, Conrad W.

2014-01-01

Cyanobacteria possess multiple mechanisms for regulating the pathways of photosynthetic and respiratory electron transport. Electron transport may be regulated indirectly by controlling the transfer of excitation energy from the light-harvesting complexes, or it may be more directly regulated by controlling the stoichiometry, localization, and interactions of photosynthetic and respiratory electron transport complexes. Regulation of the extent of linear vs. cyclic electron transport is particularly important for controlling the redox balance of the cell. This review discusses what is known of the regulatory mechanisms and the timescales on which they occur, with particular regard to the structural reorganization needed and the constraints imposed by the limited mobility of membrane-integral proteins in the crowded thylakoid membrane. Switching mechanisms requiring substantial movement of integral thylakoid membrane proteins occur on slower timescales than those that require the movement only of cytoplasmic or extrinsic membrane proteins. This difference is probably due to the restricted diffusion of membrane-integral proteins. Multiple switching mechanisms may be needed to regulate electron transport on different timescales. PMID:24478787

Electricity-driven metabolic shift through direct electron uptake by electroactive heterotroph Clostridium pasteurianum

PubMed Central

Choi, Okkyoung; Kim, Taeyeon; Woo, Han Min; Um, Youngsoon

2014-01-01

Although microbes directly accepting electrons from a cathode have been applied for CO2 reduction to produce multicarbon-compounds, a high electron demand and low product concentration are critical limitations. Alternatively, the utilization of electrons as a co-reducing power during fermentation has been attempted, but there must be exogenous mediators due to the lack of an electroactive heterotroph. Here, we show that Clostridium pasteurianum DSM 525 simultaneously utilizes both cathode and substrate as electron donors through direct electron transfer. In a cathode compartment poised at +0.045 V vs. SHE, a metabolic shift in C. pasteurianum occurs toward NADH-consuming metabolite production such as butanol from glucose (20% shift in terms of NADH consumption) and 1,3-propandiol from glycerol (21% shift in terms of NADH consumption). Notably, a small amount of electron uptake significantly induces NADH-consuming pathways over the stoichiometric contribution of the electrons as reducing equivalents. Our results demonstrate a previously unknown electroactivity and metabolic shift in the biochemical-producing heterotroph, opening up the possibility of efficient and enhanced production of electron-dense metabolites using electricity. PMID:25376371

Abundant Type III Lipid Transfer Proteins in Arabidopsis Tapetum Are Secreted to the Locule and Become a Constituent of the Pollen Exine1[W][OPEN

PubMed Central

Huang, Ming-Der; Chen, Tung-Ling L.; Huang, Anthony H.C.

2013-01-01

Lipid transfer proteins (LTPs) are small secretory proteins in plants with defined lipid-binding structures for possible lipid exocytosis. Special groups of LTPs unique to the anther tapetum are abundant, but their functions are unclear. We studied a special group of LTPs, type III LTPs, in Arabidopsis (Arabidopsis thaliana). Their transcripts were restricted to the anther tapetum, with levels peaking at the developmental stage of maximal pollen-wall exine synthesis. We constructed an LTP-Green Fluorescent Protein (LTP-GFP) plasmid, transformed it into wild-type plants, and monitored LTP-GFP in developing anthers with confocal laser scanning microscopy. LTP-GFP appeared in the tapetum and was secreted via the endoplasmic reticulum-trans-Golgi network machinery into the locule. It then moved to the microspore surface and remained as a component of exine. Immuno-transmission electron microscopy of native LTP in anthers confirmed the LTP-GFP observations. The in vivo association of LTP-GFP and exine in anthers was not observed with non-type III or structurally modified type III LTPs or in transformed exine-defective mutant plants. RNA interference knockdown of individual type III LTPs produced no observable mutant phenotypes. RNA interference knockdown of two type III LTPs produced microscopy-observable morphologic changes in the intine underneath the exine (presumably as a consequence of changes in the exine not observed by transmission electron microscopy) and pollen susceptible to dehydration damage. Overall, we reveal a novel transfer pathway of LTPs in which LTPs bound or nonbound to exine precursors are secreted from the tapetum to become microspore exine constituents; this pathway explains the need for plentiful LTPs to incorporate into the abundant exine. PMID:24096413

Unveiling the Structural Basis That Regulates the Energy Transduction Properties within a Family of Triheme Cytochromes from Geobacter sulfurreducens

DOE Office of Scientific and Technical Information (OSTI.GOV)

Dantas, Joana M.; Simões, Telma; Morgado, Leonor

A family of triheme cytochromes from Geobacter sulfurreducens plays an important role in extracellular electron transfer. In addition to their role in electron transfer pathways, two members of this family (PpcA and PpcD) were also found to be able to couple e(-)/H+ transfer through the redox Bohr effect observed in the physiological pH range, a feature not observed for cytochromes PpcB and PpcE. In attempting to understand the molecular control of the redox Bohr effect in this family of cytochromes, which is highly homologous both in amino acid sequence and structures, it was observed that residue 6 is a conservedmore » leucine in PpcA and PpcD, whereas in the other two characterized members (PpcB and PpcE) the equivalent residue is a phenylalanine. To determine the role of this residue located close to the redox Bohr center, we replaced Leu(6) in PpcA with Phe and determined the redox properties of the mutant, as well as its solution structure in the fully reduced state. In contrast with the native form, the mutant PpcAL6F is not able to couple the e(-)/H+ pathway. We carried out the reverse mutation in PpcB and PpcE (i.e., replacing Phe(6) in these two proteins by leucine) and the mutated proteins showed an increased redox Bohr effect. The results clearly establish the role of residue 6 in the control of the redox Bohr effect in this family of cytochromes, a feature that could enable the rational design of G. sulfurreducens strains that carry mutant cytochromes with an optimal redox Bohr effect that would be suitable for various biotechnological applications.« less

The Cytochrome b 6 f Complex: Biophysical Aspects of Its Functioning in Chloroplasts.

PubMed

Tikhonov, Alexander N

2018-01-01

This chapter presents an overview of structural properties of the cytochrome (Cyt) b 6 f complex and its functioning in chloroplasts. The Cyt b 6 f complex stands at the crossroad of photosynthetic electron transport pathways, providing connectivity between Photosystem (PSI) and Photosysten II (PSII) and pumping protons across the membrane into the thylakoid lumen. After a brief review of the chloroplast electron transport chain, the consideration is focused on the structural organization of the Cyt b 6 f complex and its interaction with plastoquinol (PQH 2 , reduced form of plastoquinone), a mediator of electron transfer from PSII to the Cyt b 6 f complex. The processes of PQH 2 oxidation by the Cyt b 6 f complex have been considered within the framework of the Mitchell's Q-cycle. The overall rate of the intersystem electron transport is determined by PQH 2 turnover at the quinone-binding site Q o of the Cyt b 6 f complex. The rate of PQH 2 oxidation is controlled by the intrathylakoid pH in , which value determines the protonation/deprotonation events in the Q o -center. Two other regulatory mechanisms associated with the Cyt b 6 f complex are briefly overviewed: (i) redistribution of electron fluxes between alternative (linear and cyclic) pathways, and (ii) "state transitions" related to redistribution of solar energy between PSI and PSII.

Reduced graphene oxide-mediated Z-scheme BiVO4/CdS nanocomposites for boosted photocatalytic decomposition of harmful organic pollutants.

PubMed

Clament Sagaya Selvam, N; Kim, Yeong Gyeong; Kim, Dong Jin; Hong, Won-Hwa; Kim, Woong; Park, Sung Hyuk; Jo, Wan-Kuen

2018-09-01

The efficient photocatalytic degradation of harmful organic pollutants (isoniazid (ISN) and 1,4-dioxane (DX)) via the Z-scheme electron transfer mechanism was accomplished using a photostable composite photocatalyst consisting of BiVO 4 , CdS, and reduced graphene oxide (RGO). Compared to their pristine counterparts, the RGO-mediated Z-scheme CdS/BiVO 4 (CdS/RGO-BiVO 4 ) nanocomposites exhibited superior degradation activities, mainly attributed to the prolonged charge separation. RGO was found to be involved in visible-light harvesting and acted as a solid-state electron mediator at the CdS/BiVO 4 interface to realize an effective Z-scheme electron transfer pathway, avoid photocatalyst self-oxidation, and lengthen the life span of charge carriers. The results of reactive species scavenging experiments, photoluminescence measurements, and transient photocurrent measurements, as well as the calculated band potentials of the synthesized photocatalysts, supported the Z-scheme electron/hole pair separation mechanism. Additionally, the intermediates formed during the degradation of ISN and DX were identified, and a possible fragmentation pattern was proposed. This systematic work aims to develop photostable Z-scheme composites as unique photocatalytic systems for the efficient removal of harmful organic pollutants. Copyright © 2018 Elsevier B.V. All rights reserved.

Exciton Relaxation and Electron Transfer Dynamics of Semiconductor Quantum Dots

NASA Astrophysics Data System (ADS)

Liu, Cunming

Quantum dots (QDs), also referred to as colloidal semiconductor nanocrystals, exhibit unique electronic and optical properties arising from their three-dimensional confinement and strongly enhanced coulomb interactions. Developing a detailed understanding of the exciton relaxation dynamics within QDs is important not only for sake of exploring the fundamental physics of quantum confinement processes, but also for their applications. Ultrafast transient absorption (TA) spectroscopy, as a powerful tool to explore the relaxation dynamics of excitons, was employed to characterize the hot single/multiexciton relaxation dynamics at the first four exciton states of CdSe/CdZnS QDs. We observed for the first time that the hot hole can relax through two possible pathways: Intraband multiple phonon coupling and intrinsic defect trapping, with a lifetime of ˜7 ps. Additionally, an ultra-short component of ˜ 8 ps, directly associated with the Auger recombination of highly energetic exciton states, was discovered. After exploring the exciton relaxation inside QDs, ultrafast TA spectroscopy was further applied to study the electron transferring outside from QDs. By using a brand-new photocatalytic system consisting of CdSe QDs and Ni-dihydrolipoic acid (Ni-DHLA) catalyst, which has represented a robust photocatalysis of H2 from water, the photoinduced electron transfer (ET) dynamics between QD and the catalyst, one of most important steps during H2 generation, was studied. We found smaller bare CdSe QDs exhibit a better ET performance and CdS shelling on the bare QDs leads to worsen the ET. The calculations of effective mass approximation (EMA) and Marcus theory show the ET process is mainly dominated by driving force, electronic coupling strength and reorganization energy between QD and the catalyst.

Oxidations of N-(3-indoleethyl) cyclic aliphatic amines by horseradish peroxidase: the indole ring binds to the enzyme and mediates electron-transfer amine oxidation.

PubMed

Ling, Ke-Qing; Li, Wen-Shan; Sayre, Lawrence M

2008-01-23

Although oxidations of aromatic amines by horseradish peroxidase (HRP) are well-known, typical aliphatic amines are not substrates of HRP. In this study, the reactions of N-benzyl and N-methyl cyclic amines with HRP were found to be slow, but reactions of N-(3-indoleethyl) cyclic amines were 2-3 orders of magnitude faster. Analyses of pH-rate profiles revealed a dominant contribution to reaction by the amine-free base forms, the only species found to bind to the enzyme. A metabolic study on a family of congeneric N-(3-indoleethyl) cyclic amines indicated competition between amine and indole oxidation pathways. Amine oxidation dominated for the seven- and eight-membered azacycles, where ring size supports the change in hybridization from sp3 to sp2 that occurs upon one-electron amine nitrogen oxidation, whereas only indole oxidation was observed for the six-membered ring congener. Optical difference spectroscopic binding data and computational docking simulations suggest that all the arylalkylamine substrates bind to the enzyme through their aromatic termini with similar binding modes and binding affinities. Kinetic saturation was observed for a particularly soluble substrate, consistent with an obligatory role of an enzyme-substrate complexation preceding electron transfer. The significant rate enhancements seen for the indoleethylamine substrates suggest the ability of the bound indole ring to mediate what amounts to medium long-range electron-transfer oxidation of the tertiary amine center by the HRP oxidants. This is the first systematic investigation to document aliphatic amine oxidation by HRP at rates consistent with normal metabolic turnover, and the demonstration that this is facilitated by an auxiliary electron-rich aromatic ring.

Probing energy transfer events in the light harvesting complex 2 (LH2) of Rhodobacter sphaeroides with two-dimensional spectroscopy.

PubMed

Fidler, Andrew F; Singh, Ved P; Long, Phillip D; Dahlberg, Peter D; Engel, Gregory S

2013-10-21

Excitation energy transfer events in the photosynthetic light harvesting complex 2 (LH2) of Rhodobacter sphaeroides are investigated with polarization controlled two-dimensional electronic spectroscopy. A spectrally broadened pulse allows simultaneous measurement of the energy transfer within and between the two absorption bands at 800 nm and 850 nm. The phased all-parallel polarization two-dimensional spectra resolve the initial events of energy transfer by separating the intra-band and inter-band relaxation processes across the two-dimensional map. The internal dynamics of the 800 nm region of the spectra are resolved as a cross peak that grows in on an ultrafast time scale, reflecting energy transfer between higher lying excitations of the B850 chromophores into the B800 states. We utilize a polarization sequence designed to highlight the initial excited state dynamics which uncovers an ultrafast transfer component between the two bands that was not observed in the all-parallel polarization data. We attribute the ultrafast transfer component to energy transfer from higher energy exciton states to lower energy states of the strongly coupled B850 chromophores. Connecting the spectroscopic signature to the molecular structure, we reveal multiple relaxation pathways including a cyclic transfer of energy between the two rings of the complex.

Electron and hole relaxation pathways in semiconductor quantum dots

DOE Office of Scientific and Technical Information (OSTI.GOV)

Klimov, V.I.; McBranch, D.W.; Leatherdale, C.A.

1999-11-01

Femtosecond (fs) broad-band transient absorption (TA) is used to study the intraband relaxation and depopulation dynamics of electron and hole quantized states in CdSe nanocrystals (NC{close_quote}s) with a range of surface properties. Instead of the drastic reduction in the energy relaxation rate expected due to a {open_quotes}phonon bottleneck,{close_quotes} we observe a fast subpicosecond 1P-to-1S electron relaxation, with the rate exceeding that due to phonon emission in bulk semiconductors. The energy relaxation is enhanced with reducing the NC{close_quote}s radius, and does not show any dependence on the NC surface properties (quality of the surface passivation). These data indicate that electron energymore » relaxation occurs by neither multiphonon emission nor by coupling to surface defects, but is likely meditated by Auger-type electron-hole energy transfer. We use fs infrared TA to probe electron and hole intraband transitions, which allows us to distinguish between electron and hole relaxation pathways leading to the depopulation of NC quantized states. In contrast to the electron relaxation, which is controlled by NC surface passivation, the depopulation of hole quantized states is extremely fast (sub-ps-to-ps time scales) in all types of samples, independent of NC surface treatment (including NC{close_quote}s overcoated with a ZnS layer). Our results indicate that ultrafast hole dynamics are not due to trapping at localized surface defects such as a vacancy, but rather arise from relaxation into intrinsic NC states or intrinsically unpassivated interface states. {copyright} {ital 1999} {ital The American Physical Society}« less

Cytosolic thioredoxin reductase 1 is required for correct disulfide formation in the ER.

PubMed

Poet, Greg J; Oka, Ojore Bv; van Lith, Marcel; Cao, Zhenbo; Robinson, Philip J; Pringle, Marie Anne; Arnér, Elias Sj; Bulleid, Neil J

2017-03-01

Folding of proteins entering the secretory pathway in mammalian cells frequently requires the insertion of disulfide bonds. Disulfide insertion can result in covalent linkages found in the native structure as well as those that are not, so-called non-native disulfides. The pathways for disulfide formation are well characterized, but our understanding of how non-native disulfides are reduced so that the correct or native disulfides can form is poor. Here, we use a novel assay to demonstrate that the reduction in non-native disulfides requires NADPH as the ultimate electron donor, and a robust cytosolic thioredoxin system, driven by thioredoxin reductase 1 (TrxR1 or TXNRD1). Inhibition of this reductive pathway prevents the correct folding and secretion of proteins that are known to form non-native disulfides during their folding. Hence, we have shown for the first time that mammalian cells have a pathway for transferring reducing equivalents from the cytosol to the ER, which is required to ensure correct disulfide formation in proteins entering the secretory pathway. © 2017 The Authors. Published under the terms of the CC BY 4.0 license.

Metabolic control of respiratory levels in coenzyme Q biosynthesis-deficient Escherichia coli strains leading to fine-tune aerobic lactate fermentation.

PubMed

Wu, Hui; Bennett, George N; San, Ka-Yiu

2015-08-01

A novel strategy to finely control the electron transfer chain (ETC) activity of Escherichia coli was established. In this study, the fine-tuning of the ubiquinone biosynthesis pathway was applied to further controlling ETC function in coenzyme Q8 biosynthesis-deficient E. coli strains, HW108 and HW109, which contain mutations in ubiE and ubiG, respectively. A competing pathway on the intermediate substrates of the Q8 synthesis pathway, catalyzed by diphosphate:4-hydroxybenzoate geranyltransferase (PGT-1) of Lithospermum erythrorhizon, was introduced into these mutant strains. A nearly theoretical yield of lactate production can be achieved under fully aerobic conditions via an in vivo, genetically fine-tunable means to further control the activity of the ETC of the Q8 biosynthesis-deficient E. coli strains. © 2015 Wiley Periodicals, Inc.

Modular Homogeneous Chromophore–Catalyst Assemblies

DOE Office of Scientific and Technical Information (OSTI.GOV)

Mulfort, Karen L.; Utschig, Lisa M.

2016-05-17

Photosynthetic reaction center (RC) proteins convert incident solar energy to chemical energy through a network of molecular cofactors which have been evolutionarily tuned to couple efficient light-harvesting, directional electron transfer, and long-lived charge separation with secondary reaction sequences. These molecular cofactors are embedded within a complex protein environment which precisely positions each cofactor in optimal geometries along efficient electron transfer pathways with localized protein environments facilitating sequential and accumulative charge transfer. By contrast, it is difficult to approach a similar level of structural complexity in synthetic architectures for solar energy conversion. However, by using appropriate self-assembly strategies, we anticipate thatmore » molecular modules, which are independently synthesized and optimized for either light-harvesting or redox catalysis, can be organized into spatial arrangements that functionally mimic natural photosynthesis. In this Account, we describe a modular approach to new structural designs for artificial photosynthesis which is largely inspired by photosynthetic RC proteins. We focus on recent work from our lab which uses molecular modules for light-harvesting or proton reduction catalysis in different coordination geometries and different platforms, spanning from discrete supramolecular assemblies to molecule–nanoparticle hybrids to protein-based biohybrids. Molecular modules are particularly amenable to high-resolution characterization of the ground and excited state of each module using a variety of physical techniques; such spectroscopic interrogation helps our understanding of primary artificial photosynthetic mechanisms. In particular, we discuss the use of transient optical spectroscopy, EPR, and X-ray scattering techniques to elucidate dynamic structural behavior and light-induced kinetics and the impact on photocatalytic mechanism. Two different coordination geometries of supramolecular photocatalyst based on the [Ru(bpy)3]2+ (bpy = 2,2'-bipyridine) light-harvesting module with cobaloxime-based catalyst module are compared, with progress in stabilizing photoinduced charge separation identified. These same modules embedded in the small electron transfer protein ferredoxin exhibit much longer charge-separation, enabled by stepwise electron transfer through the native [2Fe-2S] cofactor. We anticipate that the use of interchangeable, molecular modules which can interact in different coordination geometries or within entirely different structural platforms will provide important fundamental insights into the effect of environment on parameters such as electron transfer and charge separation, and ultimately drive more efficient designs for artificial photosynthesis.« less

The Perchlorate Reduction Genomic Island: Mechanisms and Pathways of Evolution by Horizontal Gene Transfer.

PubMed

Melnyk, Ryan A; Coates, John D

2015-10-26

Perchlorate is a widely distributed anion that is toxic to humans, but serves as a valuable electron acceptor for several lineages of bacteria. The ability to utilize perchlorate is conferred by a horizontally transferred piece of DNA called the perchlorate reduction genomic island (PRI). We compared genomes of perchlorate reducers using phylogenomics, SNP mapping, and differences in genomic architecture to interrogate the evolutionary history of perchlorate respiration. Here we report on the PRI of 13 genomes of perchlorate-reducing bacteria from four different classes of Phylum Proteobacteria (the Alpha-, Beta-, Gamma- and Epsilonproteobacteria). Among the different phylogenetic classes, the island varies considerably in genetic content as well as in its putative mechanism and location of integration. However, the islands of the densely sampled genera Azospira and Magnetospirillum have striking nucleotide identity despite divergent genomes, implying horizontal transfer and positive selection within narrow phylogenetic taxa. We also assess the phylogenetic origin of accessory genes in the various incarnations of the island, which can be traced to chromosomal paralogs from phylogenetically similar organisms. These observations suggest a complex phylogenetic history where the island is rarely transferred at the class level but undergoes frequent and continuous transfer within narrow phylogenetic groups. This restricted transfer is seen directly by the independent integration of near-identical islands within a genus and indirectly due to the acquisition of lineage-specific accessory genes. The genomic reversibility of perchlorate reduction may present a unique equilibrium for a metabolism that confers a competitive advantage only in the presence of an electron acceptor, which although widely distributed, is generally present at low concentrations in nature.

The glyoxylate pathway contributes to enhanced extracellular electron transfer in yeast-based biofuel cell.

PubMed

Hubenova, Yolina; Hubenova, Eleonora; Slavcheva, Evelina; Mitov, Mario

2017-08-01

This study provides a new insight into our understanding of yeast response to starvation conditions (sole acetate as carbon source) and applied polarization and offers important information about the role of the glyoxylate cycle in the carbohydrate synthesis and extracellular charge transfer processes in biofuel cells. The biosynthetic capabilities of yeast C. melibiosica 2491 and the up/down-regulation of the glyoxylate cycle are evaluated by modifying the cellular metabolism by feedback inhibition or carbohydrate presence and establishing the malate dehydrogenase activity and carbohydrate content together with the electric charge passed through bioelectrochemical system. 10mM malate leads to a decrease of the produced quantity of electricity with ca. 55%. At the same time, 24-times lower intracellular malate dehydrogenase activity is established. At polarization conditions the glyoxylate pathway is up-regulated and huge amount of malate is intra-converted into oxaloacetate. The yeasts are able to synthesize carbohydrates from acetate and a part of them is used for the electricity generation. It is recognized that the enhanced charge transfer in acetate fed yeast-based biofuel cell is implemented by secreted endogenous mediator and changes in the cellular surface redox activity depending on the addition of carbohydrate in the medium. Copyright © 2017 Elsevier B.V. All rights reserved.

Factors that control catalytic two- versus four-electron reduction of dioxygen by copper complexes.

PubMed

Fukuzumi, Shunichi; Tahsini, Laleh; Lee, Yong-Min; Ohkubo, Kei; Nam, Wonwoo; Karlin, Kenneth D

2012-04-25

The selective two-electron reduction of O(2) by one-electron reductants such as decamethylferrocene (Fc*) and octamethylferrocene (Me(8)Fc) is efficiently catalyzed by a binuclear Cu(II) complex [Cu(II)(2)(LO)(OH)](2+) (D1) {LO is a binucleating ligand with copper-bridging phenolate moiety} in the presence of trifluoroacetic acid (HOTF) in acetone. The protonation of the hydroxide group of [Cu(II)(2)(LO)(OH)](2+) with HOTF to produce [Cu(II)(2)(LO)(OTF)](2+) (D1-OTF) makes it possible for this to be reduced by 2 equiv of Fc* via a two-step electron-transfer sequence. Reactions of the fully reduced complex [Cu(I)(2)(LO)](+) (D3) with O(2) in the presence of HOTF led to the low-temperature detection of the absorption spectra due to the peroxo complex [Cu(II)(2)(LO)(OO)] (D) and the protonated hydroperoxo complex [Cu(II)(2)(LO)(OOH)](2+) (D4). No further Fc* reduction of D4 occurs, and it is instead further protonated by HOTF to yield H(2)O(2) accompanied by regeneration of [Cu(II)(2)(LO)(OTF)](2+) (D1-OTF), thus completing the catalytic cycle for the two-electron reduction of O(2) by Fc*. Kinetic studies on the formation of Fc*(+) under catalytic conditions as well as for separate examination of the electron transfer from Fc* to D1-OTF reveal there are two important reaction pathways operating. One is a rate-determining second reduction of D1-OTF, thus electron transfer from Fc* to a mixed-valent intermediate [Cu(II)Cu(I)(LO)](2+) (D2), which leads to [Cu(I)(2)(LO)](+) that is coupled with O(2) binding to produce [Cu(II)(2)(LO)(OO)](+) (D). The other involves direct reaction of O(2) with the mixed-valent compound D2 followed by rapid Fc* reduction of a putative superoxo-dicopper(II) species thus formed, producing D.

Intra- versus intermolecular electron transfer in radical nucleophilic aromatic substitution of dihalo(hetero)arenes – a tool for estimating π-conjugation in aromatic systems† †Electronic supplementary information (ESI) available: Experimental details and procedures, 1H and 13C NMR data, GC traces and mass spectra. CCDC 1526301 and 1526302. For ESI and crystallographic data in CIF or other electronic format see DOI: 10.1039/c7sc00100b Click here for additional data file. Click here for additional data file.

PubMed Central

Janhsen, B.; Daniliuc, C. G.

2017-01-01

In this paper, the application of the double radical nucleophilic aromatic substitution (SRN1) in various dihalogenated, mostly diiodinated, π-conjugated systems as a tool for qualitatively estimating their π-conjugation is described. This approach uses electron delocalisation as a measure of π-conjugation. Electron injection into the π-system is achieved via reaction of an intermediate aryl radical, itself generated from a dihalogenated π-system via SET-reduction of the C–I bond and subsequent reaction with a thiolate anion. The generated arene radical anion can then further react with the second aryl-halogen moiety within the π-system via an intramolecular electron transfer process. The efficiency of this intramolecular electron transfer is related to the π-conjugation of the radical anion. If the π-conjugation within the aromatic unit is weak, the arene radical anion reacts via an intermolecular ET with the starting dihalide. The intramolecular ET process delivers a product of a double SRN1 substitution whereas the intermolecular ET pathway provides a product of a mono- SRN1 substitution. By simple product analysis of mono- versus double substitution, π-conjugation can be qualitatively evaluated. This mechanistic tool is applied to various dihalogenated π-conjugated systems and the results are discussed within the context of π-conjugation. The conjugation mode within the π-system and the length of the aromatic system are varied, and the effect of relative positioning of the two halides within small π-systems is also addressed. PMID:28580099

Tight-binding model of the photosystem II reaction center: application to two-dimensional electronic spectroscopy

NASA Astrophysics Data System (ADS)

Gelzinis, Andrius; Valkunas, Leonas; Fuller, Franklin D.; Ogilvie, Jennifer P.; Mukamel, Shaul; Abramavicius, Darius

2013-07-01

We propose an optimized tight-binding electron-hole model of the photosystem II (PSII) reaction center (RC). Our model incorporates two charge separation pathways and spatial correlations of both static disorder and fast fluctuations of energy levels. It captures the main experimental features observed in time-resolved two-dimensional (2D) optical spectra at 77 K: peak pattern, lineshapes and time traces. Analysis of 2D spectra kinetics reveals that specific regions of the 2D spectra of the PSII RC are sensitive to the charge transfer states. We find that the energy disorder of two peripheral chlorophylls is four times larger than the other RC pigments.

Electron transfer driven decomposition of adenine and selected analogs as probed by experimental and theoretical methods

NASA Astrophysics Data System (ADS)

Cunha, T.; Mendes, M.; Ferreira da Silva, F.; Eden, S.; García, G.; Bacchus-Montabonel, M.-C.; Limão-Vieira, P.

2018-04-01

We report on a combined experimental and theoretical study of electron-transfer-induced decomposition of adenine (Ad) and a selection of analog molecules in collisions with potassium (K) atoms. Time-of-flight negative ion mass spectra have been obtained in a wide collision energy range (6-68 eV in the centre-of-mass frame), providing a comprehensive investigation of the fragmentation patterns of purine (Pu), adenine (Ad), 9-methyl adenine (9-mAd), 6-dimethyl adenine (6-dimAd), and 2-D adenine (2-DAd). Following our recent communication about selective hydrogen loss from the transient negative ions (TNIs) produced in these collisions [T. Cunha et al., J. Chem. Phys. 148, 021101 (2018)], this work focuses on the production of smaller fragment anions. In the low-energy part of the present range, several dissociation channels that are accessible in free electron attachment experiments are absent from the present mass spectra, notably NH2 loss from adenine and 9-methyl adenine. This can be understood in terms of a relatively long transit time of the K+ cation in the vicinity of the TNI tending to enhance the likelihood of intramolecular electron transfer. In this case, the excess energy can be redistributed through the available degrees of freedom inhibiting fragmentation pathways. Ab initio theoretical calculations were performed for 9-methyl adenine (9-mAd) and adenine (Ad) in the presence of a potassium atom and provided a strong basis for the assignment of the lowest unoccupied molecular orbitals accessed in the collision process.

Tryptophan and ATTO 590: mutual fluorescence quenching and exciplex formation.

PubMed

Bhattacharjee, Ujjal; Beck, Christie; Winter, Arthur; Wells, Carson; Petrich, Jacob W

2014-07-24

Investigation of fluorescence quenching of probes, such as ATTO dyes, is becoming an increasingly important topic owing to the use of these dyes in super-resolution microscopies and in single-molecule studies. Photoinduced electron transfer is their most important nonradiative pathway. Because of the increasing frequency of the use of ATTO and related dyes to investigate biological systems, studies are presented for inter- and intramolecular quenching of ATTO 590 with tryptophan. In order to examine intramolecular quenching, an ATTO 590-tryptophan conjugate was synthesized. It was determined that tryptophan is efficiently quenching ATTO 590 fluorescence by excited-state charge transfer and two charge transfer complexes are forming. In addition, it was discovered that an exciplex (whose lifetime is 5.6 ns) can be formed between tryptophan and ATTO 590, and it is suggested that the possibility of such exciplex formation should be taken into account when protein fluorescence is monitored in a system tagged with ATTO dyes.

The role of electron transfer in DNA building blocks: Evaluation of strand breaks and their implications

NASA Astrophysics Data System (ADS)

Almeida, Diogo Alexandre Fialho de

Radiation-induced damage to biological systems, both direct and indirect processes, has increasingly come under scrutiny by the international scientific community due to recent findings that electrons are a very effective agent in damaging DNA/RNA. Indeed, much remains to be discovered regarding the exact physico-chemical processes that occur in the nascent stages of DNA/RNA damage by incident radiation. However, it is also known that electrons do not exist freely in the physiological medium, but rather solvated and/or pre-solvated states. This leads to the need for new techniques that can better explore the damaging role of "bound" electrons to DNA/RNA. The work presented in this thesis consists on the study of electron transfer in collisions of atomic species with molecules of biological relevance. In order to study these processes, two experimental setups were used. One setup consists of a crossed beam experiment where a neutral potassium beam is created and made to collide with an effusive molecular target beam. The anionic products that stem from electron transfer in potassium atom to the molecular target collisions are then extracted and time-of-flight (TOF) mass analysed. In the second setup a beam of anionic species is formed and made to collide with a molecular target. Collisions with three different anionic beams were performed (H-, O- and OH-), as well as with different simple organic molecules, by measuring the positive and negative ion fragmentation patterns with a quadrupole mass spectrometer (QMS). A comparison between these two collisional systems can greatly help to understand the underlying mechanisms of the electron transfer processes. Finally, studies of potassium collisions with sugar surrogates D-Ribose and THF were performed. These studies show very different fragmentation patterns from DEA, although in the case of THF, it is suggested that the initially accessed states are the same as in DEA. With these studies was also possible to show for the first time collision induced site and bond selectivity breaking, where the electron is transferred into a given state of the acceptor molecule and the resulting fragmentation pathways are exclusive to the initial anionic state. Furthermore, the role of the potassium cation post collisionwas explored and indeed its presence is suggested to induce at least partial suppression of auto-detachment. The implications that ensue from this degradation are analysed in the light of the obtained fragmentation patterns.

Analysis of borderline substitution/electron transfer pathways from direct ab initio MD simulations

NASA Astrophysics Data System (ADS)

Yamataka, Hiroshi; Aida, Misako; Dupuis, Michel

2002-02-01

Ab initio molecular dynamics simulations were carried out for the borderline reaction pathways in the reaction of CH 2O rad - with CH 3Cl. The simulations reveal distinctive features of three types of mechanisms passing through the S N2-like transition state (TS): (i) a direct formation of S N2 products, (ii) a direct formation of ET products, and (iii) a two-step formation of ET products via the S N2 valley. The direct formation of the ET product through the S N2-like TS appears to be more favorable at higher temperatures. The two-step process depends on the amount of energy that goes into the C-C stretching mode.

Picolinoxy group, a new leaving group for anti SN2' selective allylic substitution with aryl anions based on Grignard reagents.

PubMed

Kiyotsuka, Yohei; Acharya, Hukum P; Katayama, Yuji; Hyodo, Tomonori; Kobayashi, Yuichi

2008-05-01

The picolinoxy group was found to be an extremely powerful leaving group for allylic substitution with aryl nucleophiles derived from ArMgBr and CuBr*Me2S. The substitution proceeds with anti SN2' pathway and with high chirality transfer. The electron-withdrawing effect of the pyridyl group and chelation to MgBr2 are likely the origin of success. Results suggesting these effects were obtained.

Visible-light-promoted redox neutral C-H amidation of heteroarenes with hydroxylamine derivatives.

PubMed

Qin, Qixue; Yu, Shouyun

2014-07-03

A room temperature redox neutral direct C-H amidation of heteroarenes has been achieved. Hydroxylamine derivatives, which are easily accessed, have been employed as tunable nitrogen sources. These reactions were enabled by a visible-light-promoted single-electron transfer pathway without a directing group. A variety of heteroarenes, such as indoles, pyrroles, and furans, could go through this amidation with high yields (up to 98%). These reactions are highly regioselective, and all the products were isolated as a single regioisomer.

High-level ab initio potential energy surface and dynamics of the F- + CH3I SN2 and proton-transfer reactions.

PubMed

Olasz, Balázs; Szabó, István; Czakó, Gábor

2017-04-01

Bimolecular nucleophilic substitution (S N 2) and proton transfer are fundamental processes in chemistry and F - + CH 3 I is an important prototype of these reactions. Here we develop the first full-dimensional ab initio analytical potential energy surface (PES) for the F - + CH 3 I system using a permutationally invariant fit of high-level composite energies obtained with the combination of the explicitly-correlated CCSD(T)-F12b method, the aug-cc-pVTZ basis, core electron correlation effects, and a relativistic effective core potential for iodine. The PES accurately describes the S N 2 channel producing I - + CH 3 F via Walden-inversion, front-side attack, and double-inversion pathways as well as the proton-transfer channel leading to HF + CH 2 I - . The relative energies of the stationary points on the PES agree well with the new explicitly-correlated all-electron CCSD(T)-F12b/QZ-quality benchmark values. Quasiclassical trajectory computations on the PES show that the proton transfer becomes significant at high collision energies and double-inversion as well as front-side attack trajectories can occur. The computed broad angular distributions and hot internal energy distributions indicate the dominance of indirect mechanisms at lower collision energies, which is confirmed by analyzing the integration time and leaving group velocity distributions. Comparison with available crossed-beam experiments shows usually good agreement.

The Role of Oxygen in the Formation of TNT Product Ions in Ion Mobility Spectrometry

DOE Office of Scientific and Technical Information (OSTI.GOV)

Daum, Keith Alvin; Atkinson, David Alan; Ewing, Robert Gordon

2002-03-01

The atmospheric pressure ionization of 2,4,6-trinitrotoluene (TNT) in air yields the (TNT-H)- product ion. It is generally accepted that this product ion is formed by the direct proton abstraction of neutral TNT by O2- reactant ions. Data presented here demonstrate the reaction involves the formation of an intermediate (TNT·O2)-, from the association of either TNT+O2- or TNT-+O2. This intermediate has two subsequent reaction branches. One of these branches involves simple dissociation of the intermediate to TNT-; the other branch is a terminal reaction that forms the typically observed (TNT-H)- ion via proton abstraction. The dissociation reaction involving electron transfer tomore » TNT- appeared to be kinetically favored and prevailed at low concentrations of oxygen (less than 2%). The presence of significant amounts of oxygen, however, resulted in the predominant formation of the (TNT-H)- ion by the terminal reaction branch. With TNT- in the system, either from direct electron attachment or by simple dissociation of the intermediate, increasing levels of oxygen in the system will continue to reform the intermediate, allowing the cycle to continue until proton abstraction occurs. Key to understanding this complex reaction pathway is that O2- was observed to transfer an electron directly to neutral TNT to form the TNT-. At oxygen levels of less than 2%, the TNT- ion intensity increased with increasing levels of oxygen (and O2-) and was larger than the (TNT-H)- ion intensity. As the oxygen level increased from 2 to 10%, the (TNT-H)- product ion became predominant. The potential reaction mechanisms were investigated with an ion mobility spectrometer, which was configured to independently evaluate the ionization pathways.« less

Mechanistic Probes of Zeolitic Imidazolate Framework for Photocatalytic Application

DOE Office of Scientific and Technical Information (OSTI.GOV)

Pattengale, Brian; Yang, Sizhuo; Lee, Sungsik

2017-11-07

In this work, we report a zeolitic imidazolate framework (ZIF-67) with remarkable activity for hydrogen evolution reaction (HER) of 40,500 μmol H2/g MOF, which is, to the best of our knowledge, the highest activity achieved by any MOF system. This result necessitated assessment of its atomic-scale mechanistic function for HER using advanced spectroscopy techniques including time-resolved optical (OTA) and in situ X-ray absorption (XAS) spectroscopy. Through the correlation of OTA results with catalytic performance, we demonstrated that the electron transfer (ET) rather than energy transfer (ENT) pathway between photosensitizer and ZIF-67 is the key factor that controls the efficiency ofmore » HER activity, as HER activity that undergoes ET pathway is 3 orders of magnitude higher than that of ENT process. Using in situ XAS, we unraveled the spectral features for key intermediate species which are likely responsible for the rate determining process under turn over conditions. This work represents an original approach to study porous ZIF materials at the molecular level using advanced spectroscopic techniques, providing unprecedented insights into the photoactive nature of ZIF frameworks.« less

Probing interfacial energetics and charge transfer kinetics in semiconductor nanocomposites: New insights into heterostructured TiO 2/BiVO 4 photoanodes

DOE PAGES

Hess, Lucas H.; Cooper, Jason K.; Loiudice, Anna; ...

2017-02-28

Heterostructured nanocomposites offer promise for creating systems exhibiting functional properties that exceed those of the isolated components. For solar energy conversion, such combinations of semiconducting nanomaterials can be used to direct charge transfer along pathways that reduce recombination and promote efficient charge extraction. However, interfacial energetics and associated kinetic pathways often differ significantly from predictions derived from the characteristics of pure component materials, particularly at the nanoscale. Here, the emergent properties of TiO 2/BiVO 4 nanocomposite photoanodes are explored using a combination of X-ray and optical spectroscopies, together with photoelectrochemical (PEC) characterization. Application of these methods to both the puremore » components and the fully assembled nanocomposites reveals unpredicted interfacial energetic alignment, which promotes ultrafast injection of electrons from BiVO 4 into TiO 2. Physical charge separation yields extremely long-lived photoexcited states and correspondingly enhanced photoelectrochemical functionality. This work highlights the importance of probing emergent interfacial energetic alignment and kinetic processes for understanding mechanisms of solar energy conversion in complex nanocomposites.« less

Linking Chemical Electron–Proton Transfer to Proton Pumping in Cytochrome c Oxidase: Broken-Symmetry DFT Exploration of Intermediates along the Catalytic Reaction Pathway of the Iron–Copper Dinuclear Complex

PubMed Central

2015-01-01

After a summary of the problem of coupling electron and proton transfer to proton pumping in cytochrome c oxidase, we present the results of our earlier and recent density functional theory calculations for the dinuclear Fe-a3–CuB reaction center in this enzyme. A specific catalytic reaction wheel diagram is constructed from the calculations, based on the structures and relative energies of the intermediate states of the reaction cycle. A larger family of tautomers/protonation states is generated compared to our earlier work, and a new lowest-energy pathway is proposed. The entire reaction cycle is calculated for the new smaller model (about 185–190 atoms), and two selected arcs of the wheel are chosen for calculations using a larger model (about 205 atoms). We compare the structural and redox energetics and protonation calculations with available experimental data. The reaction cycle map that we have built is positioned for further improvement and testing against experiment. PMID:24960612

Oxygen Reduction on Gold Nanocrystal Surfaces in Alkaline Electrolyte: Evidence for Surface Proton Transfer Effects

DOE Office of Scientific and Technical Information (OSTI.GOV)

Zhang, Yu; Lu, Fang; Liu, Shizhong

Four-electron oxygen reduction reaction (4e-ORR) pathway, as a key high-performance reaction pathway in energy conversion, has been sought after in numerous investigations on metal surfaces over the last decades. Although the surfaces of the most noble metals, including platinum and palladium, demonstrate the fullpotential- range 4e-ORR, this is not the case, for gold (Au) surfaces. The 4e-ORR is only operative on Au surfaces with {100} subfacets, e.g. Au(100), in alkaline solution, however restricted to a certain potential region at low overpotentials, while reverting to a 2e-ORR at high overpotentials. This ORR on Au(100) has been a long-standing puzzle of electrocatalysis.more » Hereby we review the ORR studies on Au, along with the studies of water effects on Au catalysts, and present our electrochemical results with monofacet Au nanocrystals. Finally, combining with theoretical calculations we demonstrate that surface proton transfer from co-adsorbed water plays the key role in determining the ORR mechanism on Au surfaces in base.« less

Oxygen Reduction on Gold Nanocrystal Surfaces in Alkaline Electrolyte: Evidence for Surface Proton Transfer Effects

DOE PAGES

Zhang, Yu; Lu, Fang; Liu, Shizhong; ...

2018-04-01

Four-electron oxygen reduction reaction (4e-ORR) pathway, as a key high-performance reaction pathway in energy conversion, has been sought after in numerous investigations on metal surfaces over the last decades. Although the surfaces of the most noble metals, including platinum and palladium, demonstrate the fullpotential- range 4e-ORR, this is not the case, for gold (Au) surfaces. The 4e-ORR is only operative on Au surfaces with {100} subfacets, e.g. Au(100), in alkaline solution, however restricted to a certain potential region at low overpotentials, while reverting to a 2e-ORR at high overpotentials. This ORR on Au(100) has been a long-standing puzzle of electrocatalysis.more » Hereby we review the ORR studies on Au, along with the studies of water effects on Au catalysts, and present our electrochemical results with monofacet Au nanocrystals. Finally, combining with theoretical calculations we demonstrate that surface proton transfer from co-adsorbed water plays the key role in determining the ORR mechanism on Au surfaces in base.« less

Excitonic pathway to photoinduced magnetism in colloidal nanocrystals with nonmagnetic dopants

NASA Astrophysics Data System (ADS)

Pinchetti, Valerio; Di, Qiumei; Lorenzon, Monica; Camellini, Andrea; Fasoli, Mauro; Zavelani-Rossi, Margherita; Meinardi, Francesco; Zhang, Jiatao; Crooker, Scott A.; Brovelli, Sergio

2018-02-01

Electronic doping of colloidal semiconductor nanostructures holds promise for future device concepts in optoelectronic and spin-based technologies. Ag+ is an emerging electronic dopant in iii-v and ii-vi nanostructures, introducing intragap electronic states optically coupled to the host conduction band. With its full 4d shell Ag+ is nonmagnetic, and the dopant-related luminescence is ascribed to decay of the conduction-band electron following transfer of the photoexcited hole to Ag+. This optical activation process and the associated modification of the electronic configuration of Ag+ remain unclear. Here, we trace a comprehensive picture of the excitonic process in Ag-doped CdSe nanocrystals and demonstrate that, in contrast to expectations, capture of the photohole leads to conversion of Ag+ to paramagnetic Ag2+. The process of exciton recombination is thus inextricably tied to photoinduced magnetism. Accordingly, we observe strong optically activated magnetism and diluted magnetic semiconductor behaviour, demonstrating that optically switchable magnetic nanomaterials can be obtained by exploiting excitonic processes involving nonmagnetic impurities.

A Structural Model of a P450-Ferredoxin Complex from Orientation-Selective Double Electron-Electron Resonance Spectroscopy.

PubMed

Bowen, Alice M; Johnson, Eachan O D; Mercuri, Francesco; Hoskins, Nicola J; Qiao, Ruihong; McCullagh, James S O; Lovett, Janet E; Bell, Stephen G; Zhou, Weihong; Timmel, Christiane R; Wong, Luet Lok; Harmer, Jeffrey R

2018-02-21

Cytochrome P450 (CYP) monooxygenases catalyze the oxidation of chemically inert carbon-hydrogen bonds in diverse endogenous and exogenous organic compounds by atmospheric oxygen. This C-H bond oxy-functionalization activity has huge potential in biotechnological applications. Class I CYPs receive the two electrons required for oxygen activation from NAD(P)H via a ferredoxin reductase and ferredoxin. The interaction of Class I CYPs with their cognate ferredoxin is specific. In order to reconstitute the activity of diverse CYPs, structural characterization of CYP-ferredoxin complexes is necessary, but little structural information is available. Here we report a structural model of such a complex (CYP199A2-HaPux) in frozen solution derived from distance and orientation restraints gathered by the EPR technique of orientation-selective double electron-electron resonance (os-DEER). The long-lived oscillations in the os-DEER spectra were well modeled by a single orientation of the CYP199A2-HaPux complex. The structure is different from the two known Class I CYP-Fdx structures: CYP11A1-Adx and CYP101A1-Pdx. At the protein interface, HaPux residues in the [Fe 2 S 2 ] cluster-binding loop and the α3 helix and the C-terminus residue interact with CYP199A2 residues in the proximal loop and the C helix. These residue contacts are consistent with biochemical data on CYP199A2-ferredoxin binding and electron transfer. Electron-tunneling calculations indicate an efficient electron-transfer pathway from the [Fe 2 S 2 ] cluster to the heme. This new structural model of a CYP-Fdx complex provides the basis for tailoring CYP enzymes for which the cognate ferredoxin is not known, to accept electrons from HaPux and display monooxygenase activity.

Electronic connection between the quinone and cytochrome C redox pools and its role in regulation of mitochondrial electron transport and redox signaling.

PubMed

Sarewicz, Marcin; Osyczka, Artur

2015-01-01

Mitochondrial respiration, an important bioenergetic process, relies on operation of four membranous enzymatic complexes linked functionally by mobile, freely diffusible elements: quinone molecules in the membrane and water-soluble cytochromes c in the intermembrane space. One of the mitochondrial complexes, complex III (cytochrome bc1 or ubiquinol:cytochrome c oxidoreductase), provides an electronic connection between these two diffusible redox pools linking in a fully reversible manner two-electron quinone oxidation/reduction with one-electron cytochrome c reduction/oxidation. Several features of this homodimeric enzyme implicate that in addition to its well-defined function of contributing to generation of proton-motive force, cytochrome bc1 may be a physiologically important point of regulation of electron flow acting as a sensor of the redox state of mitochondria that actively responds to changes in bioenergetic conditions. These features include the following: the opposing redox reactions at quinone catalytic sites located on the opposite sides of the membrane, the inter-monomer electronic connection that functionally links four quinone binding sites of a dimer into an H-shaped electron transfer system, as well as the potential to generate superoxide and release it to the intermembrane space where it can be engaged in redox signaling pathways. Here we highlight recent advances in understanding how cytochrome bc1 may accomplish this regulatory physiological function, what is known and remains unknown about catalytic and side reactions within the quinone binding sites and electron transfers through the cofactor chains connecting those sites with the substrate redox pools. We also discuss the developed molecular mechanisms in the context of physiology of mitochondria. Copyright © 2015 the American Physiological Society.

Electronic Connection Between the Quinone and Cytochrome c Redox Pools and Its Role in Regulation of Mitochondrial Electron Transport and Redox Signaling

PubMed Central

Sarewicz, Marcin; Osyczka, Artur

2015-01-01

Mitochondrial respiration, an important bioenergetic process, relies on operation of four membranous enzymatic complexes linked functionally by mobile, freely diffusible elements: quinone molecules in the membrane and water-soluble cytochromes c in the intermembrane space. One of the mitochondrial complexes, complex III (cytochrome bc1 or ubiquinol:cytochrome c oxidoreductase), provides an electronic connection between these two diffusible redox pools linking in a fully reversible manner two-electron quinone oxidation/reduction with one-electron cytochrome c reduction/oxidation. Several features of this homodimeric enzyme implicate that in addition to its well-defined function of contributing to generation of proton-motive force, cytochrome bc1 may be a physiologically important point of regulation of electron flow acting as a sensor of the redox state of mitochondria that actively responds to changes in bioenergetic conditions. These features include the following: the opposing redox reactions at quinone catalytic sites located on the opposite sides of the membrane, the inter-monomer electronic connection that functionally links four quinone binding sites of a dimer into an H-shaped electron transfer system, as well as the potential to generate superoxide and release it to the intermembrane space where it can be engaged in redox signaling pathways. Here we highlight recent advances in understanding how cytochrome bc1 may accomplish this regulatory physiological function, what is known and remains unknown about catalytic and side reactions within the quinone binding sites and electron transfers through the cofactor chains connecting those sites with the substrate redox pools. We also discuss the developed molecular mechanisms in the context of physiology of mitochondria. PMID:25540143

The End of the Line: Can Ferredoxin and Ferredoxin NADP(H) Oxidoreductase Determine the Fate of Photosynthetic Electrons?

PubMed Central

Goss, Tatjana; Hanke, Guy

2014-01-01

At the end of the linear photosynthetic electron transfer (PET) chain, the small soluble protein ferredoxin (Fd) transfers electrons to Fd:NADP(H) oxidoreductase (FNR), which can then reduce NADP+ to support C assimilation. In addition to this linear electron flow (LEF), Fd is also thought to mediate electron flow back to the membrane complexes by different cyclic electron flow (CEF) pathways: either antimycin A sensitive, NAD(P)H complex dependent, or through FNR located at the cytochrome b6f complex. Both Fd and FNR are present in higher plant genomes as multiple gene copies, and it is now known that specific Fd iso-proteins can promote CEF. In addition, FNR iso-proteins vary in their ability to dynamically interact with thylakoid membrane complexes, and it has been suggested that this may also play a role in CEF. We will highlight work on the different Fd-isoproteins and FNR-membrane association found in the bundle sheath (BSC) and mesophyll (MC) cell chloroplasts of the C4 plant maize. These two cell types perform predominantly CEF and LEF, and the properties and activities of Fd and FNR in the BSC and MC are therefore specialized for CEF and LEF respectively. A diversity of Fd isoproteins and dynamic FNR location has also been recorded in C3 plants, algae and cyanobacteria. This indicates that the principles learned from the extreme electron transport situations in the BSC and MC of maize might be usefully applied to understanding the dynamic transition between these states in other systems. PMID:24678667

Introduction to the Thematic Minireview Series: Redox metabolism and signaling.

PubMed

Banerjee, Ruma

2017-10-13

Life on oxygen predisposes cells to reactive oxygen species (ROS) generation by electron slippage in the electron transfer chain. Aerobic metabolism also generates superoxide (O 2 ̇̄ ) and hydrogen peroxide (H 2 O 2 ) as bona fide products in reactions involving 1- or 2-electron reduction of O 2 Although often viewed as dangerous, ROS are now recognized as important messengers in redox signaling pathways. A delicate balance between needed versus excessive ROS production distinguishes health from an array of disease states. A collection of provocative reviews in this thematic series discusses the relative importance of mitochondrial sites for ROS production, ROS signaling-mediated regulation of cellular stress responses and thermogenesis, and how O 2 deficiency leads to metabolic reprograming in cancer. © 2017 by The American Society for Biochemistry and Molecular Biology, Inc.

Unravelling electronic and structural requisites of triplet-triplet energy transfer by advanced electron paramagnetic resonance and density functional theory

NASA Astrophysics Data System (ADS)

Di Valentin, M.; Salvadori, E.; Barone, V.; Carbonera, D.

2013-10-01

Advanced electron paramagnetic resonance (EPR) techniques, in combination with Density Functional theory (DFT), have been applied to the comparative study of carotenoid triplet states in two major photosynthetic antenna complexes, the Peridinin-chlorophyll a-protein of dinoflagellates and the light-harvesting complex II of higher plants. Carotenoid triplet states are populated by triplet-triplet energy transfer (TTET) from chlorophyll molecules to photoprotect the system from singlet oxygen formation under light-stress conditions. The TTET process is strongly dependent on the relative arrangement and on the electronic properties of the triplet states involved. The proposed spectroscopic approach exploits the concept of spin conservation during TTET, which leads to recognisable spin polarisation effects in the time-resolved and field-swept echo-detected EPR spectra. The electron spin polarisation produced at the carotenoid acceptor site depends on the initial polarisation of the chlorophyll donor and on the relative geometrical arrangement of the donor-acceptor zero-field splitting axes. We have demonstrated that a proper analysis of the spectra in the framework of spin angular momentum conservation allows to derive the pathways of TTET and to gain insight into the structural requirements of this mechanism for those antenna complexes, whose X-ray structure is available. We have further proved that this method, developed for natural antenna complexes of known X-ray structure, can be extended to systems lacking structural information in order to derive the relative arrangement of the partners in the energy transfer process. The structural requirements for efficient TTET, obtained from time-resolved and pulse EPR, have been complemented by a detailed description of the electronic structure of the carotenoid triplet state, provided by pulse Electron-Nuclear DOuble Resonance (ENDOR) experiments. Triplet-state hyperfine couplings of the α- and β-protons of the carotenoid conjugated chain have been assigned with the aid of quantum chemical calculation. DFT predictions of the electronic structure of the carotenoid triplet state, in terms of spin density distribution, frontier orbital description and orbital excitation represent suitable building blocks toward a deeper understanding of electronic requirements for efficient TTET.

Chemistry at molecular junctions: Rotation and dissociation of O2 on the Ag(110) surface induced by a scanning tunneling microscope.

PubMed

Roy, Sharani; Mujica, Vladimiro; Ratner, Mark A

2013-08-21

The scanning tunneling microscope (STM) is a fascinating tool used to perform chemical processes at the single-molecule level, including bond formation, bond breaking, and even chemical reactions. Hahn and Ho [J. Chem. Phys. 123, 214702 (2005)] performed controlled rotations and dissociations of single O2 molecules chemisorbed on the Ag(110) surface at precise bias voltages using STM. These threshold voltages were dependent on the direction of the bias voltage and the initial orientation of the chemisorbed molecule. They also observed an interesting voltage-direction-dependent and orientation-dependent pathway selectivity suggestive of mode-selective chemistry at molecular junctions, such that in one case the molecule underwent direct dissociation, whereas in the other case it underwent rotation-mediated dissociation. We present a detailed, first-principles-based theoretical study to investigate the mechanism of the tunneling-induced O2 dynamics, including the origin of the observed threshold voltages, the pathway dependence, and the rate of O2 dissociation. Results show a direct correspondence between the observed threshold voltage for a process and the activation energy for that process. The pathway selectivity arises from a competition between the voltage-modified barrier heights for rotation and dissociation, and the coupling strength of the tunneling electrons to the rotational and vibrational modes of the adsorbed molecule. Finally, we explore the "dipole" and "resonance" mechanisms of inelastic electron tunneling to elucidate the energy transfer between the tunneling electrons and chemisorbed O2.

12 CFR 1005.14 - Electronic fund transfer service provider not holding consumer's account.

Code of Federal Regulations, 2012 CFR

2012-01-01

... 12 Banks and Banking 8 2012-01-01 2012-01-01 false Electronic fund transfer service provider not... PROTECTION ELECTRONIC FUND TRANSFERS (REGULATION E) § 1005.14 Electronic fund transfer service provider not holding consumer's account. (a) Provider of electronic fund transfer service. A person that provides an...

12 CFR 1005.14 - Electronic fund transfer service provider not holding consumer's account.

Code of Federal Regulations, 2013 CFR

2013-01-01

... 12 Banks and Banking 8 2013-01-01 2013-01-01 false Electronic fund transfer service provider not... PROTECTION ELECTRONIC FUND TRANSFERS (REGULATION E) General § 1005.14 Electronic fund transfer service provider not holding consumer's account. (a) Provider of electronic fund transfer service. A person that...

12 CFR 1005.14 - Electronic fund transfer service provider not holding consumer's account.

Code of Federal Regulations, 2014 CFR

2014-01-01

... 12 Banks and Banking 8 2014-01-01 2014-01-01 false Electronic fund transfer service provider not... PROTECTION ELECTRONIC FUND TRANSFERS (REGULATION E) General § 1005.14 Electronic fund transfer service provider not holding consumer's account. (a) Provider of electronic fund transfer service. A person that...

Expression and characterization of truncated human heme oxygenase (hHO-1) and a fusion protein of hHO-1 with human cytochrome P450 reductase.

PubMed

Wilks, A; Black, S M; Miller, W L; Ortiz de Montellano, P R

1995-04-04

A human heme oxygenase (hHO-1) gene without the sequence coding for the last 23 amino acids has been expressed in Escherichia coli behind the pho A promoter. The truncated enzyme is obtained in high yields as a soluble, catalytically-active protein, making it available for the first time for detailed mechanistic studies. The purified, truncated hHO-1/heme complex is spectroscopically indistinguishable from that of the rat enzyme and converts heme to biliverdin when reconstituted with rat liver cytochrome P450 reductase. A self-sufficient heme oxygenase system has been obtained by fusing the truncated hHO-1 gene to the gene for human cytochrome P450 reductase without the sequence coding for the 20 amino acid membrane binding domain. Expression of the fusion protein in pCWori+ yields a protein that only requires NADPH for catalytic turnover. The failure of exogenous cytochrome P450 reductase to stimulate turnover and the insensitivity of the catalytic rate toward changes in ionic strength establish that electrons are transferred intramolecularly between the reductase and heme oxygenase domains of the fusion protein. The Vmax for the fusion protein is 2.5 times higher than that for the reconstituted system. Therefore, either the covalent tether does not interfere with normal docking and electron transfer between the flavin and heme domains or alternative but equally efficient electron transfer pathways are available that do not require specific docking.

DOE Office of Scientific and Technical Information (OSTI.GOV)

Tiede, D.M.; Kellogg, E.C.; Kolaczkowski, S.

We have carried out a more stringent test for electron transfer along the M-pathway at low temperature. This has been done by directly detecting transient states generated from the trapped PH{sub L}{sup {minus}}H{sub M} state in Rps viridis reaction centers. Under these conditions the normal forward electron transfer to H{sub L} is blocked, and the yield of transient P{sup +}H{sub M}{sup {minus}} is determined with respect to the lifetime of P*. Others have measured this lifetime to be 20 ps at room temperature. This enhances the opportunity for detecting a reaction between P* and H{sub M} by 20-fold. These experimentsmore » find that transient bleaching of the P990 nm band occurs from the trapped PH{sub L}{sup {minus}}H{sub M} state on the ns time scale, with a quantum yield of 0.09 {plus minus} 0.06 compared to normal photochemistry. This measurement places an upper limit on the yield of a transient P{sup +}H{sub M}{sup {minus}} state. The measured yield and estimated lifetime of P* suggest that the maximum electron transfer rate P* {yields} H{sub M} is about 5 {times} 10{sup 9} sec{sup {minus}1} ({tau}{sub M} = 200 ps). This corresponds to a k{sub L}/k{sub M} ratio of at least 200. This large value of the branching ratio is remarkable in view of the structural symmetry of the reaction center. 13 refs., 2 figs.« less

Supramolecular organization of cytochrome c oxidase- and alternative oxidase-dependent respiratory chains in the filamentous fungus Podospora anserina.

PubMed

Krause, Frank; Scheckhuber, Christian Q; Werner, Alexandra; Rexroth, Sascha; Reifschneider, Nicole H; Dencher, Norbert A; Osiewacz, Heinz D

2004-06-18

To elucidate the molecular basis of the link between respiration and longevity, we have studied the organization of the respiratory chain of a wild-type strain and of two long-lived mutants of the filamentous fungus Podospora anserina. This established aging model is able to respire by either the standard or the alternative pathway. In the latter pathway, electrons are directly transferred from ubiquinol to the alternative oxidase and thus bypass complexes III and IV. We show that the cytochrome c oxidase pathway is organized according to the mammalian "respirasome" model (Schägger, H., and Pfeiffer, K. (2000) EMBO J. 19, 1777-1783). In contrast, the alternative pathway is composed of distinct supercomplexes of complexes I and III (i.e. I(2) and I(2)III(2)), which have not been described so far. Enzymatic analysis reveals distinct functional properties of complexes I and III belonging to either cytochrome c oxidase- or alternative oxidase-dependent pathways. By a gentle colorless-native PAGE, almost all of the ATP synthases from mitochondria respiring by either pathway were preserved in the dimeric state. Our data are of significance for the understanding of both respiratory pathways as well as lifespan control and aging.

Gas phase reactions of doubly charged alkaline earth and transition metal(II)-ligand complexes generated by electrospray ionization

NASA Astrophysics Data System (ADS)

Kohler, Martin; Leary, Julie A.

1997-03-01

Doubly charged metal(II)-complexes of [alpha] 1-3, [alpha] 1-6 mannotriose and the conserved trimannosyl core pentasaccharide as well as doubly charged complexes of Co(II), Mn(II), Ca(II) and Sr(II) with acetonitrile generated by electrospray ionization were studied by low energy collision induced dissociation (CID). Two main fragmentation pathways were observed for the metal(II)-oligosaccharide complexes. Regardless of the coordinating metal, loss of a neutral dehydrohexose residue (162 Da) from the doubly charged precursor ion is observed, forming a doubly charged product ion. However, if the oligosaccharide is coordinated to Co(II) or Mn(II), loss of a dehydroxyhexose cation is also observed. Investigation of the low mass region of the mass spectra of the metal coordinated oligosaccharides revealed intense signals corresponding to [metal(II) + (CH3CN)n2+ (where n = 1-6) species which were being formed by the metal(II) ions and the acetonitrile present in the sample. Analysis of these metal(II)-acetonitrile complexes provided further insight into the processes occurring upon low energy CID of doubly charged metal complexes. The metal(II)-acetonitrile system showed neutral loss and ligand cleavage as observed with the oligosaccharide complexes, as well as a series of six different dissociation mechanisms, most notable among them reduction from [metal(II) + (CH3CN)n2+ to the bare [metal(I)]+ species by electron transfer. Depending on the metal and collision gas chosen, one observes electron transfer from the ligand to the metal, electron transfer from the collision gas to the metal, proton transfer between ligands, heterolytic cleavage of the ligands, reactive collisions and loss of neutral ligands.

A Proteomic View at the Biochemistry of Syntrophic Butyrate Oxidation in Syntrophomonas wolfei

PubMed Central

Schmidt, Alexander; Müller, Nicolai; Schink, Bernhard; Schleheck, David

2013-01-01

In syntrophic conversion of butyrate to methane and CO2, butyrate is oxidized to acetate by secondary fermenting bacteria such as Syntrophomonas wolfei in close cooperation with methanogenic partner organisms, e.g., Methanospirillum hungatei. This process involves an energetically unfavourable shift of electrons from the level of butyryl-CoA oxidation to the substantially lower redox potential of proton and/or CO2 reduction, in order to transfer these electrons to the methanogenic partner via hydrogen and/or formate. In the present study, all prominent membrane-bound and soluble proteins expressed in S. wolfei specifically during syntrophic growth with butyrate, in comparison to pure-culture growth with crotonate, were examined by one- and two-dimensional gel electrophoresis, and identified by peptide fingerprinting-mass spectrometry. A membrane-bound, externally oriented, quinone-linked formate dehydrogenase complex was expressed at high level specifically during syntrophic butyrate oxidation, comprising a selenocystein-linked catalytic subunit with a membrane-translocation pathway signal (TAT), a membrane-bound iron-sulfur subunit, and a membrane-bound cytochrome. Soluble hydrogenases were expressed at high levels specifically during growth with crotonate. The results were confirmed by native protein gel electrophoresis, by formate dehydrogenase and hydrogenase-activity staining, and by analysis of formate dehydrogenase and hydrogenase activities in intact cells and cell extracts. Furthermore, constitutive expression of a membrane-bound, internally oriented iron-sulfur oxidoreductase (DUF224) was confirmed, together with expression of soluble electron-transfer flavoproteins (EtfAB) and two previously identified butyryl-CoA dehydrogenases. Our findings allow to depict an electron flow scheme for syntrophic butyrate oxidation in S. wolfei. Electrons derived from butyryl-CoA are transferred through a membrane-bound EtfAB:quinone oxidoreductase (DUF224) to a menaquinone cycle and further via a b-type cytochrome to an externally oriented formate dehydrogenase. Hence, an ATP hydrolysis-driven proton-motive force across the cytoplasmatic membrane would provide the energy input for the electron potential shift necessary for formate formation. PMID:23468890

Stabilization of very rare tautomers of uracil by an excess electron.

PubMed

Bachorz, Rafał A; Rak, Janusz; Gutowski, Maciej

2005-05-21

We characterized valence-type and dipole-bound anionic states of uracil using various electronic structure methods. We found that the most stable anion is related to neither the canonical 2,4-dioxo nor a rare imino-hydroxy tautomer. Instead, it is related to an imino-oxo tautomer, in which the N1H proton is transferred to the C5 atom. This valence anion is characterized by an electron vertical detachment energy (VDE) of 1267 meV and it is adiabatically stable with respect to the canonical neutral by 3.93 kcal mol(-1). It is also more stable by 2.32 and 5.10 kcal mol(-1) than the dipole-bound and valence anion, respectively, of the canonical tautomer. The VDE values for the former and the latter are 73 and 506 meV, respectively. Another, anionic, low-lying imino-oxo tautomer with a VDE of 2499 meV has a proton transferred from N3H to C5. It is less stable than the neutral canonical tautomer by 1.38 kcal mol(-1). The mechanism of formation of anionic tautomers with the carbon C5 protonated may involve intermolecular proton transfer or dissociative electron attachment to the canonical neutral tautomer followed by a barrier-free attachment of a hydrogen atom to C5. The six-member ring structure of anionic tautomers with carbon atoms protonated might be unstable upon an excess electron detachment. Indeed, the neutral systems resulting from electron detachment from anionic tautomers with carbon atoms protonated evolve along barrier-free decomposition pathways to a linear or a bicyclo structure, which might be viewed as lesions to RNA. Within the PCM hydration model, the low-lying valence anions become adiabatically bound with respect to the canonical neutral and the two most stable tautomers have carbon atoms protonated.

Proton pumping in the bc1 complex: a new gating mechanism that prevents short circuits.

PubMed

Crofts, Antony R; Lhee, Sangmoon; Crofts, Stephanie B; Cheng, Jerry; Rose, Stuart

2006-08-01

The Q-cycle mechanism of the bc1 complex explains how the electron transfer from ubihydroquinone (quinol, QH2) to cytochrome (cyt) c (or c2 in bacteria) is coupled to the pumping of protons across the membrane. The efficiency of proton pumping depends on the effectiveness of the bifurcated reaction at the Q(o)-site of the complex. This directs the two electrons from QH2 down two different pathways, one to the high potential chain for delivery to an electron acceptor, and the other across the membrane through a chain containing heme bL and bH to the Qi-site, to provide the vectorial charge transfer contributing to the proton gradient. In this review, we discuss problems associated with the turnover of the bc1 complex that center around rates calculated for the normal forward and reverse reactions, and for bypass (or short-circuit) reactions. Based on rate constants given by distances between redox centers in known structures, these appeared to preclude conventional electron transfer mechanisms involving an intermediate semiquinone (SQ) in the Q(o)-site reaction. However, previous research has strongly suggested that SQ is the reductant for O2 in generation of superoxide at the Q(o)-site, introducing an apparent paradox. A simple gating mechanism, in which an intermediate SQ mobile in the volume of the Q(o)-site is a necessary component, can readily account for the observed data through a coulombic interaction that prevents SQ anion from close approach to heme bL when the latter is reduced. This allows rapid and reversible QH2 oxidation, but prevents rapid bypass reactions. The mechanism is quite natural, and is well supported by experiments in which the role of a key residue, Glu-295, which facilitates proton transfer from the site through a rotational displacement, has been tested by mutation.

Engineering Shewanella oneidensis enables xylose-fed microbial fuel cell.

PubMed

Li, Feng; Li, Yuanxiu; Sun, Liming; Li, Xiaofei; Yin, Changji; An, Xingjuan; Chen, Xiaoli; Tian, Yao; Song, Hao

2017-01-01

The microbial fuel cell (MFC) is a green and sustainable technology for electricity energy harvest from biomass, in which exoelectrogens use metabolism and extracellular electron transfer pathways for the conversion of chemical energy into electricity. However, Shewanella oneidensis MR-1, one of the most well-known exoelectrogens, could not use xylose (a key pentose derived from hydrolysis of lignocellulosic biomass) for cell growth and power generation, which limited greatly its practical applications. Herein, to enable S. oneidensis to directly utilize xylose as the sole carbon source for bioelectricity production in MFCs, we used synthetic biology strategies to successfully construct four genetically engineered S. oneidensis (namely XE, GE, XS, and GS) by assembling one of the xylose transporters (from Candida intermedia and Clostridium acetobutylicum ) with one of intracellular xylose metabolic pathways (the isomerase pathway from Escherichia coli and the oxidoreductase pathway from Scheffersomyces stipites ), respectively. We found that among these engineered S. oneidensis strains, the strain GS (i.e. harbouring Gxf1 gene encoding the xylose facilitator from C. intermedi , and XYL1 , XYL2 , and XKS1 genes encoding the xylose oxidoreductase pathway from S. stipites ) was able to generate the highest power density, enabling a maximum electricity power density of 2.1 ± 0.1 mW/m 2 . To the best of our knowledge, this was the first report on the rationally designed Shewanella that could use xylose as the sole carbon source and electron donor to produce electricity. The synthetic biology strategies developed in this study could be further extended to rationally engineer other exoelectrogens for lignocellulosic biomass utilization to generate electricity power.

Dipole-Guided Electron Capture Causes Abnormal Dissociations of Phosphorylated Pentapeptides

NASA Astrophysics Data System (ADS)

Moss, Christopher L.; Chung, Thomas W.; Wyer, Jean A.; Nielsen, Steen Brøndsted; Hvelplund, Preben; Tureček, František

2011-04-01

Electron transfer and capture mass spectra of a series of doubly charged ions that were phosphorylated pentapeptides of a tryptic type (pS,A,A,A,R) showed conspicuous differences in dissociations of charge-reduced ions. Electron transfer from both gaseous cesium atoms at 100 keV kinetic energies and fluoranthene anion radicals in an ion trap resulted in the loss of a hydrogen atom, ammonia, and backbone cleavages forming complete series of sequence z ions. Elimination of phosphoric acid was negligible. In contrast, capture of low-energy electrons by doubly charged ions in a Penning ion trap induced loss of a hydrogen atom followed by elimination of phosphoric acid as the dominant dissociation channel. Backbone dissociations of charge-reduced ions also occurred but were accompanied by extensive fragmentation of the primary products. z-Ions that were terminated with a deaminated phosphoserine radical competitively eliminated phosphoric acid and H2PO4 radicals. A mechanism is proposed for this novel dissociation on the basis of a computational analysis of reaction pathways and transition states. Electronic structure theory calculations in combination with extensive molecular dynamics mapping of the potential energy surface provided structures for the precursor phosphopeptide dications. Electron attachment produces a multitude of low lying electronic states in charge-reduced ions that determine their reactivity in backbone dissociations and H- atom loss. The predominant loss of H atoms in ECD is explained by a distortion of the Rydberg orbital space by the strong dipolar field of the peptide dication framework. The dipolar field steers the incoming electron to preferentially attach to the positively charged arginine side chain to form guanidinium radicals and trigger their dissociations.

Design and engineering of photosynthetic light-harvesting and electron transfer using length, time, and energy scales.

PubMed

Noy, Dror; Moser, Christopher C; Dutton, P Leslie

2006-02-01

Decades of research on the physical processes and chemical reaction-pathways in photosynthetic enzymes have resulted in an extensive database of kinetic information. Recently, this database has been augmented by a variety of high and medium resolution crystal structures of key photosynthetic enzymes that now include the two photosystems (PSI and PSII) of oxygenic photosynthetic organisms. Here, we examine the currently available structural and functional information from an engineer's point of view with the long-term goal of reproducing the key features of natural photosystems in de novo designed and custom-built molecular solar energy conversion devices. We find that the basic physics of the transfer processes, namely, the time constraints imposed by the rates of incoming photon flux and the various decay processes allow for a large degree of tolerance in the engineering parameters. Moreover, we find that the requirements to guarantee energy and electron transfer rates that yield high efficiency in natural photosystems are largely met by control of distance between chromophores and redox cofactors. Thus, for projected de novo designed constructions, the control of spatial organization of cofactor molecules within a dense array is initially given priority. Nevertheless, constructions accommodating dense arrays of different cofactors, some well within 1 nm from each other, still presents a significant challenge for protein design.

Electrochemical Detection of Circadian Redox Rhythm in Cyanobacterial Cells via Extracellular Electron Transfer.

PubMed

Nishio, Koichi; Pornpitra, Tunanunkul; Izawa, Seiichiro; Nishiwaki-Ohkawa, Taeko; Kato, Souichiro; Hashimoto, Kazuhito; Nakanishi, Shuji

2015-06-01

Recent research on cellular circadian rhythms suggests that the coupling of transcription-translation feedback loops and intracellular redox oscillations is essential for robust circadian timekeeping. For clarification of the molecular mechanism underlying the circadian rhythm, methods that allow for the dynamic and simultaneous detection of transcription/translation and redox oscillations in living cells are needed. Herein, we report that the cyanobacterial circadian redox rhythm can be electrochemically detected based on extracellular electron transfer (EET), a process in which intracellular electrons are exchanged with an extracellular electrode. As the EET-based method is non-destructive, concurrent detection with transcription/translation rhythm using bioluminescent reporter strains becomes possible. An EET pathway that electrochemically connected the intracellular region of cyanobacterial cells with an extracellular electrode was constructed via a newly synthesized electron mediator with cell membrane permeability. In the presence of the mediator, the open circuit potential of the culture medium exhibited temperature-compensated rhythm with approximately 24 h periodicity. Importantly, such circadian rhythm of the open circuit potential was not observed in the absence of the electron mediator, indicating that the EET process conveys the dynamic information regarding the intracellular redox state to the extracellular electrode. These findings represent the first direct demonstration of the intracellular circadian redox rhythm of cyanobacterial cells. © The Author 2015. Published by Oxford University Press on behalf of Japanese Society of Plant Physiologists. All rights reserved. For permissions, please email: journals.permissions@oup.com.

Identification of the 2-Hydroxyglutarate and Isovaleryl-CoA Dehydrogenases as Alternative Electron Donors Linking Lysine Catabolism to the Electron Transport Chain of Arabidopsis Mitochondria[W][OA

PubMed Central

Araújo, Wagner L.; Ishizaki, Kimitsune; Nunes-Nesi, Adriano; Larson, Tony R.; Tohge, Takayuki; Krahnert, Ina; Witt, Sandra; Obata, Toshihiro; Schauer, Nicolas; Graham, Ian A.; Leaver, Christopher J.; Fernie, Alisdair R.

2010-01-01

The process of dark-induced senescence in plants is relatively poorly understood, but a functional electron-transfer flavoprotein/electron-transfer flavoprotein:ubiquinone oxidoreductase (ETF/ETFQO) complex, which supports respiration during carbon starvation, has recently been identified. Here, we studied the responses of Arabidopsis thaliana mutants deficient in the expression of isovaleryl-CoA dehydrogenase and 2-hydroxyglutarate dehydrogenase to extended darkness and other environmental stresses. Evaluations of the mutant phenotypes following carbon starvation induced by extended darkness identify similarities to those exhibited by mutants of the ETF/ETFQO complex. Metabolic profiling and isotope tracer experimentation revealed that isovaleryl-CoA dehydrogenase is involved in degradation of the branched-chain amino acids, phytol, and Lys, while 2-hydroxyglutarate dehydrogenase is involved exclusively in Lys degradation. These results suggest that isovaleryl-CoA dehydrogenase is the more critical for alternative respiration and that a series of enzymes, including 2-hydroxyglutarate dehydrogenase, plays a role in Lys degradation. Both physiological and metabolic phenotypes of the isovaleryl-CoA dehydrogenase and 2-hydroxyglutarate dehydrogenase mutants were not as severe as those observed for mutants of the ETF/ETFQO complex, indicating some functional redundancy of the enzymes within the process. Our results aid in the elucidation of the pathway of plant Lys catabolism and demonstrate that both isovaleryl-CoA dehydrogenase and 2-hydroxyglutarate dehydrogenase act as electron donors to the ubiquinol pool via an ETF/ETFQO-mediated route. PMID:20501910

Identification of the 2-hydroxyglutarate and isovaleryl-CoA dehydrogenases as alternative electron donors linking lysine catabolism to the electron transport chain of Arabidopsis mitochondria.

PubMed

Araújo, Wagner L; Ishizaki, Kimitsune; Nunes-Nesi, Adriano; Larson, Tony R; Tohge, Takayuki; Krahnert, Ina; Witt, Sandra; Obata, Toshihiro; Schauer, Nicolas; Graham, Ian A; Leaver, Christopher J; Fernie, Alisdair R

2010-05-01

The process of dark-induced senescence in plants is relatively poorly understood, but a functional electron-transfer flavoprotein/electron-transfer flavoprotein:ubiquinone oxidoreductase (ETF/ETFQO) complex, which supports respiration during carbon starvation, has recently been identified. Here, we studied the responses of Arabidopsis thaliana mutants deficient in the expression of isovaleryl-CoA dehydrogenase and 2-hydroxyglutarate dehydrogenase to extended darkness and other environmental stresses. Evaluations of the mutant phenotypes following carbon starvation induced by extended darkness identify similarities to those exhibited by mutants of the ETF/ETFQO complex. Metabolic profiling and isotope tracer experimentation revealed that isovaleryl-CoA dehydrogenase is involved in degradation of the branched-chain amino acids, phytol, and Lys, while 2-hydroxyglutarate dehydrogenase is involved exclusively in Lys degradation. These results suggest that isovaleryl-CoA dehydrogenase is the more critical for alternative respiration and that a series of enzymes, including 2-hydroxyglutarate dehydrogenase, plays a role in Lys degradation. Both physiological and metabolic phenotypes of the isovaleryl-CoA dehydrogenase and 2-hydroxyglutarate dehydrogenase mutants were not as severe as those observed for mutants of the ETF/ETFQO complex, indicating some functional redundancy of the enzymes within the process. Our results aid in the elucidation of the pathway of plant Lys catabolism and demonstrate that both isovaleryl-CoA dehydrogenase and 2-hydroxyglutarate dehydrogenase act as electron donors to the ubiquinol pool via an ETF/ETFQO-mediated route.

Kinetic consequences of introducing a proximal selenocysteine ligand into cytochrome P450cam.

PubMed

Vandemeulebroucke, An; Aldag, Caroline; Stiebritz, Martin T; Reiher, Markus; Hilvert, Donald

2015-11-10

The structural, electronic, and catalytic properties of cytochrome P450cam are subtly altered when the cysteine that coordinates to the heme iron is replaced with a selenocysteine. To map the effects of the sulfur-to-selenium substitution on the individual steps of the catalytic cycle, we conducted a comparative kinetic analysis of the selenoenzyme and its cysteine counterpart. Our results show that the more electron-donating selenolate ligand has only negligible effects on substrate, product, and oxygen binding, electron transfer, catalytic turnover, and coupling efficiency. Off-pathway reduction of oxygen to give superoxide is the only step significantly affected by the mutation. Incorporation of selenium accelerates this uncoupling reaction approximately 50-fold compared to sulfur, but because the second electron transfer step is much faster, the impact on overall catalytic turnover is minimal. Density functional theory calculations with pure and hybrid functionals suggest that superoxide formation is governed by a delicate interplay of spin distribution, spin state, and structural effects. In light of the remarkably similar electronic structures and energies calculated for the sulfur- and selenium-containing enzymes, the ability of the heavier atom to enhance the rate of spin crossover may account for the experimental observations. Because the selenoenzyme closely mimics wild-type P450cam, even at the level of individual steps in the reaction cycle, selenium represents a unique mechanistic probe for analyzing the role of the proximal ligand and spin crossovers in P450 chemistry.

Reduction of nitrobenzene with alkaline ascorbic acid: Kinetics and pathways.

PubMed

Liang, Chenju; Lin, Ya-Ting; Shiu, Jia-Wei

2016-01-25

Alkaline ascorbic acid (AA) exhibits the potential to reductively degrade nitrobenzene (NB), which is the simplest of the nitroaromatic compounds. The nitro group (NO2(-)) of NB has a +III oxidation state of the N atom and tends to gain electrons. The effect of alkaline pH ranging from 9 to 13 was initially assessed and the results demonstrated that the solution pH, when approaching or above the pKa2 of AA (11.79), would increase reductive electron transfer to NB. The rate equation for the reactions between NB and AA at pH 12 can be described as r=((0.89±0.11)×10(-4) mM(1-(a+b))h(-1))×[NB](a=1.35±0.10)[AA](b=0.89±0.01). The GC/MS analytical method identified nitrosobenzene, azoxybenzene, and azobenzene as NB reduction intermediates, and aniline (AN) as a final product. These experimental results indicate that the alkaline AA reduction of NB to AN mainly proceeds via the direct route, consisting of a series of two-electron or four-electron transfers, and the condensation reaction plays a minor route. Preliminary evaluation of the remediation of spiked NB contaminated soils revealed that maintenance of alkaline pH and a higher water to soil ratio are essential for a successful alkaline AA application. Copyright © 2015 Elsevier B.V. All rights reserved.

Theoretical study of the hydrogen abstraction of substituted phenols by nitrogen dioxide as a source of HONO.

PubMed

Shenghur, Abraham; Weber, Kevin H; Nguyen, Nhan D; Sontising, Watit; Tao, Fu-Ming

2014-11-20

The mild yet promiscuous reactions of nitrogen dioxide (NO2) and phenolic derivatives to produce nitrous acid (HONO) have been explored with density functional theory calculations. The reaction is found to occur via four distinct pathways with both proton coupled electron transfer (PCET) and hydrogen atom transfer (HAT) mechanisms available. While the parent reaction with phenol may not be significant in the gas phase, electron donating groups in the ortho and para positions facilitate the reduction of nitrogen dioxide by electronically stabilizing the product phenoxy radical. Hydrogen bonding groups in the ortho position may additionally stabilize the nascent resonantly stabilized radical product, thus enhancing the reaction. Catechol (ortho-hydroxy phenol) has a predicted overall free energy change ΔG(0) = -0.8 kcal mol(-1) and electronic activation energy Ea = 7.0 kcal mol(-1). Free amines at the ortho and para positions have ΔG(0) = -3.8 and -1.5 kcal mol(-1); Ea = 2.3 and 2.1 kcal mol(-1), respectively. The results indicate that the hydrogen abstraction reactions of these substituted phenols by NO2 are fast and spontaneous. Hammett constants produce a linear correlation with bond dissociation energy (BDE) demonstrating that the BDE is the main parameter controlling the dark abstraction reaction. The implications for atmospheric chemistry and ground-level nitrous acid production are discussed.

Coherent pump pulses in Double Electron Electron Resonance Spectroscopy

PubMed Central

Tait, Claudia E.; Stoll, Stefan

2016-01-01

The recent introduction of shaped pulses to Double Electron Electron Resonance (DEER) spectroscopy has led to significant enhancements in sensitivity through increased excitation bandwidths and improved control over spin dynamics. The application of DEER has so far relied on the presence of an incoherent pump channel to average out most undesired coherent effects of the pump pulse(s) on the observer spins. However, in fully coherent EPR spectrometers that are increasingly used to generate shaped pulses, the presence of coherent pump pulses means that these effects need to be explicitly considered. In this paper, we examine the effects of coherent rectangular and sech/tanh pump pulses in DEER experiments with up to three pump pulses. We show that, even in the absence of significant overlap of the observer and pump pulse excitation bandwidths, coherence transfer pathways involving both types of pulses generate spin echoes of considerable intensity. These echoes introduce artefacts, which, if not identified and removed, can easily lead to misinterpretation. We demonstrate that the observed echoes can be quantitatively modelled using a simple spin quantum dynamics approach that includes instrumental transfer functions. Based on an analysis of the echo crossing artefacts, we propose efficient phase cycling schemes for their suppression. This enables the use of advanced DEER experiments, characterized by high sensitivity and increased accuracy for long-distance measurements, on novel fully coherent EPR spectrometers. PMID:27339858

Spectroscopic characterization of the iron-oxo intermediate in cytochrome P450.

PubMed

Jung, Christiane; Schünemann, Volker; Lendzian, Friedhelm; Trautwein, Alfred X; Contzen, Jörg; Galander, Marcus; Böttger, Lars H; Richter, Matthias; Barra, Anne-Laure

2005-10-01

From analogy to chloroperoxidase from Caldariomyces fumago, it is believed that the electronic structure of the intermediate iron-oxo species in the catalytic cycle of cytochrome P450 corresponds to an iron(IV) porphyrin-pi-cation radical (compound I). However, our recent studies on P450cam revealed that after 8 ms a tyrosine radical and iron(IV) were formed in the reaction of ferric P450 with external oxidants in the shunt pathway. The present study on the heme domain of P450BM3 (P450BMP) shows a similar result. In addition to a tyrosine radical, a contribution from a tryptophan radical was found in the electron paramagnetic resonance (EPR) spectra of P450BMP. Here we present comparative multi-frequency EPR (9.6, 94 and 285 GHz) and Mössbauer spectroscopic studies on freeze-quenched intermediates produced using peroxy acetic acid as oxidant for both P450 cytochromes. After 8 ms in both systems, amino acid radicals occurred instead of the proposed iron(IV) porphyrin-pi-cation radical, which may be transiently formed on a much faster time scale. These findings are discussed with respect to other heme thiolate proteins. Our studies demonstrate that intramolecular electron transfer from aromatic amino acids is a common feature in these enzymes. The electron transfer quenches the presumably transiently formed porphyrin-pi-cation radical, which makes it extremely difficult to trap compound I.

Efficient Photochemical Dihydrogen Generation Initiated by a Bimetallic Self-Quenching Mechanism

DOE PAGES

Chambers, Matthew B.; Kurtz, Daniel A.; Pitman, Catherine L.; ...

2016-09-27

Artificial photosynthesis relies on coupling light absorption with chemical fuel generation. A mechanistic study of visible light-driven H 2 production from [Cp*Ir(bpy)H] + (1) has revealed a new, highly efficient pathway for integrating light absorption with bond formation. The net reaction of 1 with a proton source produces H 2, but the rate of excited state quenching is surprisingly acid-independent and displays no observable deuterium kinetic isotopic effect. Time-resolved photoluminescence and labeling studies are consistent with diffusion-limited bimetallic self-quenching by electron transfer. Accordingly, the quantum yield of H 2 release nearly reaches unity as the concentration of 1 increases. Furthermore,more » this unique pathway for photochemical H 2 generation provides insight into transformations catalyzed by 1.« less

A density functional theory (DFT) and time-dependent density functional theory (TDDFT) study on optical transitions in oligo(p-phenylenevinylene)-fullerene dyads and the applicability to resonant energy transfer.

PubMed

Toivonen, Teemu L J; Hukka, Terttu I

2007-06-07

The optical transitions of three different size oligo(p-phenylenevinylene)-fullerene dyads (OPV(n)-MPC(60); n = 2-4) and of the corresponding separate molecules are studied using density functional theory (DFT) and time-dependent density functional theory. The DFT is used to determine the geometries and the electronic structures of the ground states. Transition energies and excited-state structures are obtained from the TDDFT calculations. Resonant energy transfer from OPV(n) to MPC(60) is also studied and the Fermi golden rule is used, along with two simple models to describe the electronic coupling to calculate the energy transfer rates. The hybrid-type PBE0 functional is used with a split-valence basis set augmented with a polarization function (SV(P)) in calculations and the calculated results are compared to the corresponding experimental results. The calculated PBE0 spectra of the OPV(n)-MPC(60) dyads correspond to the experimental spectra very well and are approximately sums of the absorption spectra of the separate OPV(n) and MPC(60) molecules. Also, the absorption energies of OPV(n) and MPC(60) and the emission energies of OPV(n) are predicted well with the PBE0 functional. The PBE0 calculated resonant energy transfer rates are in a good agreement with the experimental rates and show the existence of many possible pathways for energy transfer from the first excited singlet states of the OPV(n) molecules to the MPC(60) molecule.

Quantum tunneling resonant electron transfer process in Lorentzian plasmas

DOE Office of Scientific and Technical Information (OSTI.GOV)

Hong, Woo-Pyo; Jung, Young-Dae, E-mail: ydjung@hanyang.ac.kr; Department of Applied Physics and Department of Bionanotechnology, Hanyang University, Ansan, Kyunggi-Do 426-791

The quantum tunneling resonant electron transfer process between a positive ion and a neutral atom collision is investigated in nonthermal generalized Lorentzian plasmas. The result shows that the nonthermal effect enhances the resonant electron transfer cross section in Lorentzian plasmas. It is found that the nonthermal effect on the classical resonant electron transfer cross section is more significant than that on the quantum tunneling resonant charge transfer cross section. It is shown that the nonthermal effect on the resonant electron transfer cross section decreases with an increase of the Debye length. In addition, the nonthermal effect on the quantum tunnelingmore » resonant electron transfer cross section decreases with increasing collision energy. The variation of nonthermal and plasma shielding effects on the quantum tunneling resonant electron transfer process is also discussed.« less

Ultrafast direct electron transfer at organic semiconductor and metal interfaces.

PubMed

Xiang, Bo; Li, Yingmin; Pham, C Huy; Paesani, Francesco; Xiong, Wei

2017-11-01

The ability to control direct electron transfer can facilitate the development of new molecular electronics, light-harvesting materials, and photocatalysis. However, control of direct electron transfer has been rarely reported, and the molecular conformation-electron dynamics relationships remain unclear. We describe direct electron transfer at buried interfaces between an organic polymer semiconductor film and a gold substrate by observing the first dynamical electric field-induced vibrational sum frequency generation (VSFG). In transient electric field-induced VSFG measurements on this system, we observe dynamical responses (<150 fs) that depend on photon energy and polarization, demonstrating that electrons are directly transferred from the Fermi level of gold to the lowest unoccupied molecular orbital of organic semiconductor. Transient spectra further reveal that, although the interfaces are prepared without deliberate alignment control, a subensemble of surface molecules can adopt conformations for direct electron transfer. Density functional theory calculations support the experimental results and ascribe the observed electron transfer to a flat-lying polymer configuration in which electronic orbitals are found to be delocalized across the interface. The present observation of direct electron transfer at complex interfaces and the insights gained into the relationship between molecular conformations and electron dynamics will have implications for implementing novel direct electron transfer in energy materials.

Disentangling nutrient concentrations trends in transfer pathways of agricultural watersheds

NASA Astrophysics Data System (ADS)

Mellander, P. E.; Jordan, P.

2017-12-01

Targeted schemes designed to attenuate agricultural pollution to water are needed to reach goals of sustainable food production. Such approaches require insight into temporal and spatial variability in the most representative flows and active pollution transfer pathways. Interpreting changes in total stream flow can be misleading since some changes may only be apparent in specific pathways. The aim of this study was to investigate changing land use pressures on water quality. The objectives were to assess intra-annual and inter-annual changes in phosphorus (P) and nitrogen (N) concentrations and loads in apportioned pathways. Pathways were separated using hydrograph and loadograph separation techniques on a seven-year dataset of sub-hourly river discharge and concentrations of NO3-N, reactive P and total P in two intensively managed agricultural watersheds of contrasting hydrology in Ireland. Active transfer pathways were dictated by soil drainage. There were intra-annual variability in both P and N concentrations in different pathways and loads, and these had the largest influence of all-year baseflow (BF) concentrations and summer quickflow (QF) concentrations. Nutrient loss responded to seasonality in the river discharge in all pathways in both watersheds and was mostly transport limited. In both watersheds there were inter-annual trends in P concentration in some pathways and seasons that did not correspond to the trend of total river P concentration. The response in stream water quality to management, mitigation measures and changes in weather may be hidden by counteracting responses in different pathways. The hydrology had a major impact on seasonal changes in N and P loss. By apportioning different transfer pathways more information on the temporal and site-specific nature of nutrient transfer was provided. BF and QF pathways largely contributed to the river P concentrations in summer while all pathways contributed to the P and N loads in wintertime. The data indicated that increasing trends in river P concentrations were mostly linked to trends in BF concentration in both catchment types. This may be explained by increased point source influence, increased vertical transfer through increased soil P loading, or decreased stream bed attenuation. Each will require different policy considerations.

Transfer of the high-GC cyclohexane carboxylate degradation pathway from Rhodopseudomonas palustris to Escherichia coli for production of biotin.

PubMed

Bernstein, Jeffrey R; Bulter, Thomas; Liao, James C

2008-01-01

This work demonstrates the transfer of the five-gene cyclohexane carboxylate (CHC) degradation pathway from the high-GC alphaproteobacterium Rhodopseudomonas palustris to Escherichia coli, a gammaproteobacterium. The degradation product of this pathway is pimeloyl-CoA, a key metabolite in E. coli's biotin biosynthetic pathway. This pathway is useful for biotin overproduction in E. coli; however, the expression of GC-rich genes is troublesome in this host. When the native R. palustris CHC degradation pathway is transferred to a DeltabioH pimeloyl-CoA auxotroph of E. coli, it is unable to complement growth in the presence of CHC. To overcome this expression problem we redesigned the operon with decreased GC content and removed stretches of high-GC intergenic DNA which comprise the 5' untranslated region of each gene, replacing these features with shorter low-GC sequences. We show this synthetic construct enables growth of the DeltabioH strain in the presence of CHC. When the synthetic degradation pathway is overexpressed in conjunction with the downstream genes for biotin biosynthesis, we measured significant accumulation of biotin in the growth medium, showing that the pathway transfer is successfully integrated with the host metabolism.

Electrostatic redesign of the [myoglobin, cytochrome b5] interface to create a well-defined docked complex with rapid interprotein electron transfer.

PubMed

Xiong, Peng; Nocek, Judith M; Griffin, Amanda K K; Wang, Jingyun; Hoffman, Brian M

2009-05-27

Cyt b(5) is the electron-carrier "repair" protein that reduces met-Mb and met-Hb to their O(2)-carrying ferroheme forms. Studies of electron transfer (ET) between Mb and cyt b(5) revealed that they react on a "Dynamic Docking" (DD) energy landscape on which binding and reactivity are uncoupled: binding is weak and involves an ensemble of nearly isoenergetic configurations, only a few of which are reactive; those few contribute negligibly to binding. We set the task of redesigning the surface of Mb so that its reaction with cyt b(5) instead would occur on a conventional "simple docking" (SD) energy landscape, on which a complex exhibits a well-defined (set of) reactive binding configuration(s), with binding and reactivity thus no longer being decoupled. We prepared a myoglobin (Mb) triple mutant (D44K/D60K/E85K; Mb(+6)) substituted with Zn-deuteroporphyrin and monitored cytochrome b(5) (cyt b(5)) binding and electron transfer (ET) quenching of the (3)ZnMb(+6) triplet state. In contrast, to Mb(WT), the three charge reversals around the "front-face" heme edge of Mb(+6) have directed cyt b(5) to a surface area of Mb adjacent to its heme, created a well-defined, most-stable structure that supports good ET pathways, and apparently coupled binding and ET: both K(a) and k(et) are increased by the same factor of approximately 2 x 10(2), creating a complex that exhibits a large ET rate constant, k(et) = 10(6 1) s(-1), and is in slow exchange (k(off) < k(et)). In short, these mutations indeed appear to have created the sought-for conversion from DD to simple docking (SD) energy landscapes.

A fluorescent pH probe for acidic organelles in living cells.

PubMed

Chen, Jyun-Wei; Chen, Chih-Ming; Chang, Cheng-Chung

2017-09-26

A water-soluble pH sensor, 2-(6-(4-aminostyryl)-1,3-dioxo-1H-benzo[de]isoquinolin-2(3H)-yl)-N, N-dimethylethanamine (ADA), was synthesized based on the molecular design of photoinduced electron transfer (PET) and intramolecular charge transfer (ICT). The fluorescence emission response against a pH value is in the range 3-6, which is suitable for labelling intracellular pH-dependent microenvironments. After biological evolution, ADA is more than a pH biosensor because it is also an endocytosis pathway tracking biosensor that labels endosomes, late endosomes, and lysosome pH gradients. From this, the emissive aggregates of ADA and protonated-ADA in these organs were evaluated to explore how this probe stresses emission colour change to cause these unique cellular images.

Contribution of direct electron transfer mechanisms to overall electron transfer in microbial fuel cells utilising Shewanella oneidensis as biocatalyst.

PubMed

Fapetu, Segun; Keshavarz, Taj; Clements, Mark; Kyazze, Godfrey

2016-09-01

To investigate the contribution of direct electron transfer mechanisms to electricity production in microbial fuel cells by physically retaining Shewanella oneidensis cells close to or away from the anode electrode. A maximum power output of 114 ± 6 mWm(-2) was obtained when cells were retained close to the anode using a dialysis membrane. This was 3.5 times more than when the cells were separated away from the anode. Without the membrane the maximum power output was 129 ± 6 mWm(-2). The direct mechanisms of electron transfer contributed significantly to overall electron transfer from S. oneidensis to electrodes, a result that was corroborated by another experiment where S. oneidensis cells were entrapped in alginate gels. S. oneidensis transfers electrons primarily by direct electron transfer as opposed to mediated electron transfer.

Sugar Radical Formation by a Proton Coupled Hole Transfer in 2′-Deoxyguanosine Radical Cation (2′-dG•+): A Theoretical Treatment

PubMed Central

Kumar, Anil; Sevilla, Michael D.

2009-01-01

Previous experimental and theoretical work has established that electronic excitation of a guanine cation radical in nucleosides or in DNA itself leads to sugar radical formation by deprotonation from the dexoxyribose sugar. In this work we investigate a ground electronic state pathway for such sugar radical formation in a hydrated one electron oxidized 2′-deoxyguanosine (dG•+ + 7H2O), using density functional theory (DFT) with the B3LYP functional and the 6-31G* basis set. We follow the stretching of the C5′-H bond in dG•+ to gain an understanding of the energy requirements to transfer the hole from the base to sugar ring and then to deprotonate to proton acceptor sites in solution and on the guanine ring. The geometries of reactant (dG•+ + 7H2O), transition state (TS) for deprotonation of C5′ site and product (dG(•C5′, N7-H+) + 7 H2O) were fully optimized. The zero point energy (ZPE) corrected activation energy (TS) for the proton transfer (PT) from C5′ is calculated to be 9.0 kcal/mol and is achieved by stretching the C5′-H bond by 0.13 Å from its equilibrium bond distance (1.099 Å). Remarkably, this small bond stretch is sufficient to transfer the “hole” (positive charge and spin) from guanine to the C5′ site on the deoxyribose group. Beyond the TS, the proton (H+) spontaneously adds to water to form a hydronium ion (H3O+) as an intermediate. The proton subsequently transfers to the N7 site of the guanine (product). The 9 kcal/mol barrier suggests slow thermal conversion of the cation radical to the sugar radical but also suggests that localized vibrational excitations would be sufficient to induce rapid sugar radical formation in DNA base cation radicals. PMID:19754084

Nonadiabatic Photo-Process Involving the πσ* State in Intramolecular Charge Transfer: a Concerted Spectroscopic and Computational Study 4-(DIMETHYLAMINO)BENZETHYNE and 4-(DIMETHYLAMINO)BENZONITRILE.

NASA Astrophysics Data System (ADS)

Fujiwara, Takashige; Segarra-Martí, Javier; Coto, Pedro B.

2014-06-01

The ubiquitous nature of the low-lying πσ* state in the photo-excited aromatic molecules or biomolecules is widely recognized to play an important role in nonadiabatic photo-process such as photodissociation or intramolecular charge transfer (ICT). For instance, the O--H elimination channel in phenol is attributed to the state-cross of the repulsive πσ* state that exhibits a conical intersection with the lowest bright ππ* state and with the ground state, leading to ultrafast electronic deactivation. A similar decay pathway has been found in the ICT formation of 4-(dialkylamino)benzonitriles in a polar environment, where an initially photoexcited Frank-Condon state bifurcates in the presence of a dark intermediate πσ* state that crosses the fluorescent ππ* state, followed by a conical intersection with the twisted intramolecular charge transfer (TICT) state. We proposed such a two-fold decay mechanism that πσ*-state highly mediates intramolecular charge transfer in 4-(dialkylamino)benzonitriles, which is supported from both our high-level ab initio calculations and ultrafast laser spectroscopies in the previous study. 4-(Dimethylamino)benzethyne (DMABE) is isoelectronic with 4-(dimethylamino)benzonitrile (DMABN), and the electronic structures and electronic spectra of the two molecules bear very close resemblance. However, DMABN does show the ICT formation in a polar environment, whereas DMABE does not. To probe the photophysical differences among the low-lying excited-state configurations, we performed concerted time-resolved laser spectroscopies and high level ab initio multireference perturbation theory quantum-chemical (CASPT2//CASSCF) computations on the two molecules. In this paper we demonstrate the importance of the bound excited-state of a πσ* configuration that induce highly πσ*-state mediated intramolecular charge transfer in 4-(dialkylamino)benzonitriles.

Suppression of BRCA2 by Mutant Mitochondrial DNA in Prostate Cancer

DTIC Science & Technology

2011-05-01

Briefly, the electron transfer activities of complex I/III (NADH dehydrogenase/cytochrome bc1 complex: catalyzes the electron transfer from NADH to...ferricytochrome c) and complex II/III (succinate dehydrogenase/cytochrome bc1 complex: catalyzes the electron transfer from succinate to ferricytochrome...The electron transfer activity of complex IV (cytochrome c oxidase: catalyzes the final step of the respiratory chain by transferring electrons from

Fabrication of a biofuel cell improved by the π-conjugated electron pathway effect induced from a new enzyme catalyst employing terephthalaldehyde

NASA Astrophysics Data System (ADS)

Chung, Yongjin; Hyun, Kyu Hwan; Kwon, Yongchai

2015-12-01

A model explaining the π-conjugated electron pathway effect induced by a novel cross-linker adopted enzyme catalyst is suggested and the performance and stability of an enzymatic biofuel cell (EBC) adopting the new catalyst are evaluated. For this purpose, new terephthalaldehyde (TPA) and conventional glutaraldehyde (GA) cross-linkers are adopted on a glucose oxidase (GOx), polyethyleneimine (PEI) and carbon nanotube (CNT)(GOx/PEI/CNT) structure. GOx/PEI/CNT cross-linked by TPA (TPA/[GOx/PEI/CNT]) results in a superior EBC performance and stability to other catalysts. It is attributed to the π bonds conjugated between the aldehyde of TPA and amine of the GOx/PEI molecules. By π conjugation, electrons bonded with carbon and nitrogen are delocalized, promoting the electron transfer and catalytic activity with an excellent EBC performance. The maximum power density (MPD) of an EBC adopting TPA/[GOx/PEI/CNT] (0.66 mW cm-2) is far better than that of the other EBCs (the MPD of EBC adopting GOx/PEI/CNT is 0.40 mW cm-2). Regarding stability, the covalent bonding formed between TPA and GOx/PEI plays a critical role in preventing the denaturation of GOx molecules, leading to an excellent stability. By repeated measurements of the catalytic activity, TPA/[GOx/PEI/CNT] maintains its activity to 92% of its initial value even after five weeks.A model explaining the π-conjugated electron pathway effect induced by a novel cross-linker adopted enzyme catalyst is suggested and the performance and stability of an enzymatic biofuel cell (EBC) adopting the new catalyst are evaluated. For this purpose, new terephthalaldehyde (TPA) and conventional glutaraldehyde (GA) cross-linkers are adopted on a glucose oxidase (GOx), polyethyleneimine (PEI) and carbon nanotube (CNT)(GOx/PEI/CNT) structure. GOx/PEI/CNT cross-linked by TPA (TPA/[GOx/PEI/CNT]) results in a superior EBC performance and stability to other catalysts. It is attributed to the π bonds conjugated between the aldehyde of TPA and amine of the GOx/PEI molecules. By π conjugation, electrons bonded with carbon and nitrogen are delocalized, promoting the electron transfer and catalytic activity with an excellent EBC performance. The maximum power density (MPD) of an EBC adopting TPA/[GOx/PEI/CNT] (0.66 mW cm-2) is far better than that of the other EBCs (the MPD of EBC adopting GOx/PEI/CNT is 0.40 mW cm-2). Regarding stability, the covalent bonding formed between TPA and GOx/PEI plays a critical role in preventing the denaturation of GOx molecules, leading to an excellent stability. By repeated measurements of the catalytic activity, TPA/[GOx/PEI/CNT] maintains its activity to 92% of its initial value even after five weeks. Electronic supplementary information (ESI) available. See DOI: 10.1039/c5nr06703k

Electrochemical Measurement of Electron Transfer Kinetics by Shewanella oneidensis MR-1*

PubMed Central

Baron, Daniel; LaBelle, Edward; Coursolle, Dan; Gralnick, Jeffrey A.; Bond, Daniel R.

2009-01-01

Shewanella oneidensis strain MR-1 can respire using carbon electrodes and metal oxyhydroxides as electron acceptors, requiring mechanisms for transferring electrons from the cell interior to surfaces located beyond the cell. Although purified outer membrane cytochromes will reduce both electrodes and metals, S. oneidensis also secretes flavins, which accelerate electron transfer to metals and electrodes. We developed techniques for detecting direct electron transfer by intact cells, using turnover and single turnover voltammetry. Metabolically active cells attached to graphite electrodes produced thin (submonolayer) films that demonstrated both catalytic and reversible electron transfer in the presence and absence of flavins. In the absence of soluble flavins, electron transfer occurred in a broad potential window centered at ∼0 V (versus standard hydrogen electrode), and was altered in single (ΔomcA, ΔmtrC) and double deletion (ΔomcA/ΔmtrC) mutants of outer membrane cytochromes. The addition of soluble flavins at physiological concentrations significantly accelerated electron transfer and allowed catalytic electron transfer to occur at lower applied potentials (−0.2 V). Scan rate analysis indicated that rate constants for direct electron transfer were slower than those reported for pure cytochromes (∼1 s−1). These observations indicated that anodic current in the higher (>0 V) window is due to activation of a direct transfer mechanism, whereas electron transfer at lower potentials is enabled by flavins. The electrochemical dissection of these activities in living cells into two systems with characteristic midpoint potentials and kinetic behaviors explains prior observations and demonstrates the complementary nature of S. oneidensis electron transfer strategies. PMID:19661057

Analysis of Triplet Exciton Loss Pathways in PTB7:PC71BM Bulk Heterojunction Solar Cells

NASA Astrophysics Data System (ADS)

Kraus, Hannes; Heiber, Michael C.; Väth, Stefan; Kern, Julia; Deibel, Carsten; Sperlich, Andreas; Dyakonov, Vladimir

2016-07-01

A strategy for increasing the conversion efficiency of organic photovoltaics has been to increase the VOC by tuning the energy levels of donor and acceptor components. However, this opens up a new loss pathway from an interfacial charge transfer state to a triplet exciton (TE) state called electron back transfer (EBT), which is detrimental to device performance. To test this hypothesis, we study triplet formation in the high performing PTB7:PC71BM blend system and determine the impact of the morphology-optimizing additive 1,8-diiodoctane (DIO). Using photoluminescence and spin-sensitive optically detected magnetic resonance (ODMR) measurements at low temperature, we find that TEs form on PC71BM via intersystem crossing from singlet excitons and on PTB7 via EBT mechanism. For DIO blends with smaller fullerene domains, an increased density of PTB7 TEs is observed. The EBT process is found to be significant only at very low temperature. At 300 K, no triplets are detected via ODMR, and electrically detected magnetic resonance on optimized solar cells indicates that TEs are only present on the fullerenes. We conclude that in PTB7:PC71BM devices, TE formation via EBT is impacted by fullerene domain size at low temperature, but at room temperature, EBT does not represent a dominant loss pathway.

Reconstructing metabolic pathways of a member of the genus Pelotomaculum suggesting its potential to oxidize benzene to carbon dioxide with direct reduction of sulfate.

PubMed

Dong, Xiyang; Dröge, Johannes; von Toerne, Christine; Marozava, Sviatlana; McHardy, Alice C; Meckenstock, Rainer U

2017-03-01

The enrichment culture BPL is able to degrade benzene with sulfate as electron acceptor and is dominated by an organism of the genus Pelotomaculum. Members of Pelotomaculum are usually known to be fermenters, undergoing syntrophy with anaerobic respiring microorganisms or methanogens. By using a metagenomic approach, we reconstructed a high-quality genome (∼2.97 Mbp, 99% completeness) for Pelotomaculum candidate BPL. The proteogenomic data suggested that (1) anaerobic benzene degradation was activated by a yet unknown mechanism for conversion of benzene to benzoyl-CoA; (2) the central benzoyl-CoA degradation pathway involved reductive dearomatization by a class II benzoyl-CoA reductase followed by hydrolytic ring cleavage and modified β-oxidation; (3) the oxidative acetyl-CoA pathway was utilized for complete oxidation to CO2. Interestingly, the genome of Pelotomaculum candidate BPL has all the genes for a complete sulfate reduction pathway including a similar electron transfer mechanism for dissimilatory sulfate reduction as in other Gram-positive sulfate-reducing bacteria. The proteome analysis revealed that the essential enzymes for sulfate reduction were all formed during growth with benzene. Thus, our data indicated that, besides its potential to anaerobically degrade benzene, Pelotomaculum candidate BPL is the first member of the genus that can perform sulfate reduction. © FEMS 2016. All rights reserved. For permissions, please e-mail: journals.permissions@oup.com.

Scanning tunneling microscopy of atomically precise graphene nanoribbons exfoliated onto H:Si(100)

NASA Astrophysics Data System (ADS)

Radocea, Adrian; Mehdi Pour, Mohammad; Vo, Timothy; Shekhirev, Mikhail; Sinitskii, Alexander; Lyding, Joseph

Atomically precise graphene nanoribbons (GNRs) are promising materials for next generation transistors due to their well-controlled bandgaps and the high thermal conductivity of graphene. The solution synthesis of graphene nanoribbons offers a pathway towards scalable manufacturing. While scanning tunneling microscopy (STM) can access size scales required for characterization, solvent residue increases experimental difficulty and precludes band-gap determination via scanning tunneling spectroscopy (STS). Our work addresses this challenge through a dry contact transfer method that cleanly transfers solution-synthesized GNRs onto H:Si(100) under UHV using a fiberglass applicator. The semiconducting silicon surface avoids problems with image charge screening enabling intrinsic bandgap measurements. We characterize the nanoribbons using STM and STS. For chevron GNRs, we find a 1.6 eV bandgap, in agreement with computational modeling, and map the electronic structure spatially with detailed spectra lines and current imaging tunneling spectroscopy. Mapping the electronic structure of graphene nanoribbons is an important step towards taking advantage of the ability to form atomically precise nanoribbons and finely tune their properties.

Understanding the Reaction Chemistry of 2,2':5',2''-Terthiophene Films with Vapor-Deposited Ag, Al, and Ca

DOE Office of Scientific and Technical Information (OSTI.GOV)

Sang, Lingzi; Matz, Dallas L.; Pemberton, Jeanne E.

The reaction chemistry of vapor-deposited 2,2':5',2''-terthiophene (α-3T) solid-state thin films with postdeposited Ag, Al, and Ca is investigated in ultrahigh vacuum using Raman spectroscopy. Vapor-deposited Ag forms nanoparticles on these films and induces considerable surface enhanced Raman scattering (SERS) along with a change in molecular symmetry of adjacent α-3T and formation of Ag–S bonds; no other reaction chemistry is observed. Vapor-deposited Al and Ca undergo chemical reaction with α-3T initiated by metal-to-α-3T electron transfer. For Al, the resulting product is predominantly amorphous carbon through initial radical formation and subsequent decomposition reactions. For Ca, the spectral evidence suggests two pathways: onemore » leading to α-3T polymerization and the other resulting in thiophene ring opening, both initiated by radical formation through Ca-to-α-3T electron transfer. These interfacial reactions reflect the complex chemistry that can occur between low work function metals and thiophene-based oligomers. This reactivity is strongly correlated with metal work function.« less

Understanding the Reaction Chemistry of 2,2':5',2"-Terthiophene Films with Vapor-Deposited Ag, Al, and Ca

DOE Office of Scientific and Technical Information (OSTI.GOV)

Sang, Lingzi; Matz, Dallas L.; Pemberton, Jeanne E.

The reaction chemistry of vapor-deposited 2,2':5',2''-terthiophene (α-3T) solid-state thin films with postdeposited Ag, Al, and Ca is investigated in ultrahigh vacuum using Raman spectroscopy. Vapor-deposited Ag forms nanoparticles on these films and induces considerable surface enhanced Raman scattering (SERS) along with a change in molecular symmetry of adjacent α-3T and formation of Ag–S bonds; no other reaction chemistry is observed. Vapor-deposited Al and Ca undergo chemical reaction with α-3T initiated by metal-to-α-3T electron transfer. For Al, the resulting product is predominantly amorphous carbon through initial radical formation and subsequent decomposition reactions. For Ca, the spectral evidence suggests two pathways: onemore » leading to α-3T polymerization and the other resulting in thiophene ring opening, both initiated by radical formation through Ca-to-α-3T electron transfer. These interfacial reactions reflect the complex chemistry that can occur between low work function metals and thiophene-based oligomers. This reactivity is strongly correlated with metal work function.« less

To Tunnel or not to Tunnel, Proton Transfer is the Question.

NASA Astrophysics Data System (ADS)

Chew, Kathryn; Nemchick, Deacon; Vaccaro, Patrick

2014-06-01

The transduction of protons between donor and acceptor sites, as mediated by the action of adjoining hydrogen bonds, represents one of the most ubiquitous of chemical transformations. While the basic mechanisms underlying such phenomena often can be ascribed to simple acid-base chemistry, the putative roles of selective nuclear and electronic displacements should not be discounted, especially when the presence of a sizeable potential barrier impedes classical hydron-migration pathways. The vibrational and isotopic specificity of hindered intramolecular proton transfer taking place within the ground (˜{X1}{A}1) and the lowest-lying excited (˜{A1}B2 (π *π) electronic states of the prototypical tropolone (TrOH) system has been probed by implementing multiple-color variants of resonant four-wave mixing (RFWM) spectroscopy, with polarization-resolved detection allowing for the extraction of quantitative rotation-tunneling information. The marked dependence of unimolecular dynamics on the extent and the type of excitation deposited into TrOH internal degrees of freedom will be discussed. Experimentally observed trends and propensities for tunneling-mediated reactivity will be interpreted through use of accompanying quantum-chemical calculations.

Theoretical insights into the photo-protective mechanisms of natural biological sunscreens: building blocks of eumelanin and pheomelanin.

PubMed

Marchetti, Barbara; Karsili, Tolga N V

2016-02-07

Eumelanin (EM) and pheomelanin (PM) are ubiquitous in mammalian skin and hair--protecting against harmful radiation from the sun. Their primary roles are to absorb solar radiation and efficiently dissipate the excess excited state energy in the form of heat without detriment to the polymeric structure. EU and PM exist as polymeric chains consisting of exotic arrangements of functionalised heteroaromatic molecules. Here we have used state-of-the-art electronic structure calculations and on-the-fly surface hopping molecular dynamics simulations to study the intrinsic deactivation paths of various building blocks of EU and PM. Ultrafast excited state decay, via electron-driven proton transfer (in EU and PM) and proton-transfer coupled ring-opening (in PM) reactions, have been identified to proceed along hitherto unknown charge-separated states in EU and PM oligomers. These results shed light on the possible relaxation pathways that dominate the photochemistry of natural skin melanins. Extrapolation of such findings could provide a gateway into engineering more effective molecular constituents in commercial sunscreens--with reduced phototoxicity.

Spontaneous modification of carbon surface with neutral red from its diazonium salts for bioelectrochemical systems.

PubMed

Guo, Kun; Chen, Xin; Freguia, Stefano; Donose, Bogdan C

2013-09-15

This study introduces a novel and simple method to covalently graft neutral red (NR) onto carbon surfaces based on spontaneous reduction of in situ generated NR diazonium salts. Immobilization of neutral red on carbon surface was achieved by immersing carbon electrodes in NR-NaNO2-HCl solution. The functionalized electrodes were characterized by cyclic voltammetry (CV), atomic force microscope (AFM), and X-ray photoelectron spectroscopy (XPS). Results demonstrated that NR attached in this way retains high electrochemical activity and proved that NR was covalently bound to the carbon surface via the pathway of reduction of aryl diazonium salts. The NR-modified electrodes showed a good stability when stored in PBS solution in the dark. The current output of an acetate-oxidising microbial bioanode made of NR-modified graphite felts were 3.63±0.36 times higher than the unmodified electrodes, which indicates that covalently bound NR can act as electron transfer mediator to facilitate electron transfer from bacteria to electrodes. Copyright © 2013 Elsevier B.V. All rights reserved.

Hydrated Electron Transfer to Nucleobases in Aqueous Solutions Revealed by Ab Initio Molecular Dynamics Simulations.

PubMed

Zhao, Jing; Wang, Mei; Fu, Aiyun; Yang, Hongfang; Bu, Yuxiang

2015-08-03

We present an ab initio molecular dynamics (AIMD) simulation study into the transfer dynamics of an excess electron from its cavity-shaped hydrated electron state to a hydrated nucleobase (NB)-bound state. In contrast to the traditional view that electron localization at NBs (G/A/C/T), which is the first step for electron-induced DNA damage, is related only to dry or prehydrated electrons, and a fully hydrated electron no longer transfers to NBs, our AIMD simulations indicate that a fully hydrated electron can still transfer to NBs. We monitored the transfer dynamics of fully hydrated electrons towards hydrated NBs in aqueous solutions by using AIMD simulations and found that due to solution-structure fluctuation and attraction of NBs, a fully hydrated electron can transfer to a NB gradually over time. Concurrently, the hydrated electron cavity gradually reorganizes, distorts, and even breaks. The transfer could be completed in about 120-200 fs in four aqueous NB solutions, depending on the electron-binding ability of hydrated NBs and the structural fluctuation of the solution. The transferring electron resides in the π*-type lowest unoccupied molecular orbital of the NB, which leads to a hydrated NB anion. Clearly, the observed transfer of hydrated electrons can be attributed to the strong electron-binding ability of hydrated NBs over the hydrated electron cavity, which is the driving force, and the transfer dynamics is structure-fluctuation controlled. This work provides new insights into the evolution dynamics of hydrated electrons and provides some helpful information for understanding the DNA-damage mechanism in solution. © 2015 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

Electron transfer and conformational change in complexes of trimethylamine dehydrogenase and electron transferring flavoprotein.

PubMed

Jones, Matthew; Talfournier, Francois; Bobrov, Anton; Grossmann, J Günter; Vekshin, Nikolai; Sutcliffe, Michael J; Scrutton, Nigel S

2002-03-08

The trimethylamine dehydrogenase-electron transferring flavoprotein (TMADH.ETF) electron transfer complex has been studied by fluorescence and absorption spectroscopies. These studies indicate that a series of conformational changes occur during the assembly of the TMADH.ETF electron transfer complex and that the kinetics of assembly observed with mutant TMADH (Y442F/L/G) or ETF (alpha R237A) complexes are much slower than are the corresponding rates of electron transfer in these complexes. This suggests that electron transfer does not occur in the thermodynamically most favorable state (which takes too long to form), but that one or more metastable states (which are formed more rapidly) are competent in transferring electrons from TMADH to ETF. Additionally, fluorescence spectroscopy studies of the TMADH.ETF complex indicate that ETF undergoes a stable conformational change (termed structural imprinting) when it interacts transiently with TMADH to form a second, distinct, structural form. The mutant complexes compromise imprinting of ETF, indicating a dependence on the native interactions present in the wild-type complex. The imprinted form of semiquinone ETF exhibits an enhanced rate of electron transfer to the artificial electron acceptor, ferricenium. Overall molecular conformations as probed by small-angle x-ray scattering studies are indistinguishable for imprinted and non-imprinted ETF, suggesting that changes in structure likely involve confined reorganizations within the vicinity of the FAD. Our results indicate a series of conformational events occur during the assembly of the TMADH.ETF electron transfer complex, and that the properties of electron transfer proteins can be affected lastingly by transient interaction with their physiological redox partners. This may have significant implications for our understanding of biological electron transfer reactions in vivo, because ETF encounters TMADH at all times in the cell. Our studies suggest that caution needs to be exercised in extrapolating the properties of in vitro interprotein electron transfer reactions to those occurring in vivo.

31 CFR 208.3 - Payment by electronic funds transfer.

Code of Federal Regulations, 2011 CFR

2011-07-01

... 31 Money and Finance:Treasury 2 2011-07-01 2011-07-01 false Payment by electronic funds transfer... DISBURSEMENTS § 208.3 Payment by electronic funds transfer. Subject to § 208.4, and notwithstanding any other... electronic funds transfer. ...

48 CFR 18.124 - Electronic funds transfer.

Code of Federal Regulations, 2011 CFR

2011-10-01

... 48 Federal Acquisition Regulations System 1 2011-10-01 2011-10-01 false Electronic funds transfer. 18.124 Section 18.124 Federal Acquisition Regulations System FEDERAL ACQUISITION REGULATION... Electronic funds transfer. Electronic funds transfer payments may be waived for acquisitions to support...

48 CFR 18.124 - Electronic funds transfer.

Code of Federal Regulations, 2013 CFR

2013-10-01

... 48 Federal Acquisition Regulations System 1 2013-10-01 2013-10-01 false Electronic funds transfer. 18.124 Section 18.124 Federal Acquisition Regulations System FEDERAL ACQUISITION REGULATION... Electronic funds transfer. Electronic funds transfer payments may be waived for acquisitions to support...

31 CFR 208.3 - Payment by electronic funds transfer.

Code of Federal Regulations, 2012 CFR

2012-07-01

... 31 Money and Finance:Treasury 2 2012-07-01 2012-07-01 false Payment by electronic funds transfer... DISBURSEMENTS § 208.3 Payment by electronic funds transfer. Subject to § 208.4, and notwithstanding any other... electronic funds transfer. ...

48 CFR 18.123 - Electronic funds transfer.

Code of Federal Regulations, 2010 CFR

2010-10-01

... 48 Federal Acquisition Regulations System 1 2010-10-01 2010-10-01 false Electronic funds transfer. 18.123 Section 18.123 Federal Acquisition Regulations System FEDERAL ACQUISITION REGULATION... Electronic funds transfer. Electronic funds transfer payments may be waived for acquisitions to support...

48 CFR 18.124 - Electronic funds transfer.

Code of Federal Regulations, 2012 CFR

2012-10-01

... 48 Federal Acquisition Regulations System 1 2012-10-01 2012-10-01 false Electronic funds transfer. 18.124 Section 18.124 Federal Acquisition Regulations System FEDERAL ACQUISITION REGULATION... Electronic funds transfer. Electronic funds transfer payments may be waived for acquisitions to support...

48 CFR 18.124 - Electronic funds transfer.

Code of Federal Regulations, 2014 CFR

2014-10-01

... 48 Federal Acquisition Regulations System 1 2014-10-01 2014-10-01 false Electronic funds transfer. 18.124 Section 18.124 Federal Acquisition Regulations System FEDERAL ACQUISITION REGULATION... Electronic funds transfer. Electronic funds transfer payments may be waived for acquisitions to support...

Protonated serotonin: Geometry, electronic structures and photophysical properties

NASA Astrophysics Data System (ADS)

Omidyan, Reza; Amanollahi, Zohreh; Azimi, Gholamhassan

2017-07-01

The geometry and electronic structures of protonated serotonin have been investigated by the aim of MP2 and CC2 methods. The relative stabilities, transition energies and geometry of sixteen different protonated isomers of serotonin have been presented. It has been predicted that protonation does not exhibit essential alteration on the S1 ← S0 electronic transition energy of serotonin. Instead, more complicated photophysical nature in respect to its neutral analogue is suggested for protonated system owing to radiative and non-radiative deactivation pathways. In addition to hydrogen detachment (HD), hydrogen/proton transfer (H/PT) processes from ammonium to indole ring along the NH+⋯ π hydrogen bond have been predicted as the most important photophysical consequences of SERH+ at S1 excited state. The PT processes is suggested to be responsible for fluorescence of SERH+ while the HD driving coordinate is proposed for elucidation of its nonradiative deactivation mechanism.

Structural basis for energy transduction by respiratory alternative complex III.

PubMed

Sousa, Joana S; Calisto, Filipa; Langer, Julian D; Mills, Deryck J; Refojo, Patrícia N; Teixeira, Miguel; Kühlbrandt, Werner; Vonck, Janet; Pereira, Manuela M

2018-04-30

Electron transfer in respiratory chains generates the electrochemical potential that serves as energy source for the cell. Prokaryotes can use a wide range of electron donors and acceptors and may have alternative complexes performing the same catalytic reactions as the mitochondrial complexes. This is the case for the alternative complex III (ACIII), a quinol:cytochrome c/HiPIP oxidoreductase. In order to understand the catalytic mechanism of this respiratory enzyme, we determined the structure of ACIII from Rhodothermus marinus at 3.9 Å resolution by single-particle cryo-electron microscopy. ACIII presents a so-far unique structure, for which we establish the arrangement of the cofactors (four iron-sulfur clusters and six c-type hemes) and propose the location of the quinol-binding site and the presence of two putative proton pathways in the membrane. Altogether, this structure provides insights into a mechanism for energy transduction and introduces ACIII as a redox-driven proton pump.

The bioenergetics mechanisms and applications of sulfate-reducing bacteria in remediation of pollutants in drainage: A review.

PubMed

Li, Xin; Lan, Shi-Ming; Zhu, Zhong-Ping; Zhang, Chang; Zeng, Guang-Ming; Liu, Yun-Guo; Cao, Wei-Cheng; Song, Biao; Yang, Hong; Wang, Sheng-Fan; Wu, Shao-Hua

2018-04-20

Sulfate-reducing bacteria (SRB), a group of anaerobic prokaryotes, can use sulfur species as a terminal electron acceptor for the oxidation of organic compounds. They not only have significant ecological functions, but also play an important role in bioremediation of contaminated sites. Although numerous studies on metabolism and applications of SRB have been conducted, they still remain incompletely understood and even controversial. Fully understanding the metabolism of SRB paves the way for allowing the microorganisms to provide more beneficial services in bioremediation. Here we review progress in bioenergetics mechanisms and application of SRB including: (1) electron acceptors and donors for SRB; (2) pathway for sulfate reduction; (3) electron transfer in sulfate reduction; (4) application of SRB for economical and concomitant treatment of heavy metal, organic contaminants and sulfates. Moreover, current knowledge gaps and further research needs are identified. Copyright © 2018 Elsevier Inc. All rights reserved.

Torsional Dynamics, Intramolecular Charge Transfer, and Solvent Friction in the S2 (11Bu+) Excited State of Peridinin: A Mechanism for Enhanced Mid-Visible Light Harvesting in the Peridinin-Chlorophyll a Protein

NASA Astrophysics Data System (ADS)

Beck, Warren; Roscioli, Jerome; Ghosh, Soumen; Bishop, Michael; Lafountain, Amy; Frank, Harry

The structural mechanism that allows peridinin to provide one of the highest quantum efficiencies for excitation energy transfer to chlorophyll (Chl) a acceptors in the peridinin-chlorophyll a protein (PCP) from dinoflagellates involves an order-of-magnitude slowing of the S2 (11Bu+)--> S1 (21Ag-)nonradiative decay pathway compared to carotenoids lacking carbonyl substitution. Using femtosecond transient grating spectroscopy with heterodyne detection, we have determined for the first time that the decay of an intermediate state termed Sx, which we assign to a twisted form of the S2 state, is substantially slowed by solvent friction in peridinin due to its intramolecular charge transfer (ICT) character. The Sx intermediate exhibits a long enough lifetime to serve as an efficient excitation energy transfer donor to Chl a in PCP. The possibility that the Franck-Condon S2 state also transfers excitation via quantum coherent mechanisms is being considered currently using broadband two-dimensional electronic spectroscopy. Support from the DOE/BES Photosynthetic Systems Program, Grant DE-SC0010847.

Connection between the membrane electron transport system and Hyn hydrogenase in the purple sulfur bacterium, Thiocapsa roseopersicina BBS.

PubMed

Tengölics, Roland; Mészáros, Lívia; Győri, E; Doffkay, Zsolt; Kovács, Kornél L; Rákhely, Gábor

2014-10-01

Thiocapsa. roseopersicina BBS has four active [NiFe] hydrogenases, providing an excellent opportunity to examine their metabolic linkages to the cellular redox processes. Hyn is a periplasmic membrane-associated hydrogenase harboring two additional electron transfer subunits: Isp1 is a transmembrane protein, while Isp2 is located on the cytoplasmic side of the membrane. In this work, the connection of HynSL to various electron transport pathways is studied. During photoautotrophic growth, electrons, generated from the oxidation of thiosulfate and sulfur, are donated to the photosynthetic electron transport chain via cytochromes. Electrons formed from thiosulfate and sulfur oxidation might also be also used for Hyn-dependent hydrogen evolution which was shown to be light and proton motive force driven. Hyn-linked hydrogen uptake can be promoted by both sulfur and nitrate. The electron flow from/to HynSL requires the presence of Isp2 in both directions. Hydrogenase-linked sulfur reduction could be inhibited by a QB site competitive inhibitor, terbutryne, suggesting a redox coupling between the Hyn hydrogenase and the photosynthetic electron transport chain. Based on these findings, redox linkages of Hyn hydrogenase are modeled. Copyright © 2014 Elsevier B.V. All rights reserved.

Relaxation pathways of photoexcited iodide-methanol clusters: a computational investigation.

PubMed

Mak, Chun C; Peslherbe, Gilles H

2014-06-26

Upon photoexcitation of iodide-methanol clusters, I(-)(CH3OH)n, to a charge-transfer-to-solvent (CTTS) excited state, extensive relaxation was found to occur, accompanied by a convoluted modulation of the stability of the excited electron, which ultimately decreases substantially. In order to develop a molecular-level understanding of the relaxation processes of CTTS excited I(-)(CH3OH)n, high-level quantum chemical calculations are first used to investigate the ground, excited, and ionized states of I(-)(CH3OH)n (n = 2). Because of the relatively small size of I(-)(CH3OH)2, it was possible to characterize the contributions of solvent-solvent interactions to the stability of the CTTS excited cluster relative to dissociation into methanol, iodine, and a free electron, which exhibits a substantial dependence on the cluster geometric configuration. Ab initio molecular dynamics simulations of CTTS excited I(-)(CH3OH)3 are then performed to shed some light onto the nature of the relaxation pathways involved in the modulation of the stability of the excited electron in larger clusters. Simulation results suggest that separation of I and (CH3OH)3(-) accompanied by solvent reorganization in the latter can initially stabilize the excited electron, while gradual cluster fragmentation to I, (CH3OH)2(-), and CH3OH ultimately destabilizes it. This work shows, for the first time, that the inability of small CTTS excited I(-)(CH3OH)n to retain a solvated electron may be attributed to the limited hydrogen-bonding capacity of CH3OH, which increases the propensity for fragmentation to smaller clusters with lower excess-electron binding energies, and highlights the critical role of intricate molecular interactions in the electron solvation process.

Atomic Layer Deposition of Nickel on ZnO Nanowire Arrays for High-Performance Supercapacitors.

PubMed

Ren, Qing-Hua; Zhang, Yan; Lu, Hong-Liang; Wang, Yong-Ping; Liu, Wen-Jun; Ji, Xin-Ming; Devi, Anjana; Jiang, An-Quan; Zhang, David Wei

2018-01-10

A novel hybrid core-shell structure of ZnO nanowires (NWs)/Ni as a pseudocapacitor electrode was successfully fabricated by atomic layer deposition of a nickel shell, and its capacitive performance was systemically investigated. Transmission electron microscopy and X-ray photoelectron spectroscopy results indicated that the NiO was formed at the interface between ZnO and Ni where the Ni was oxidized by ZnO during the ALD of the Ni layer. Electrochemical measurement results revealed that the Ti/ZnO NWs/Ni (1500 cycles) electrode with a 30 nm thick Ni-NiO shell layer had the best supercapacitor properties including ultrahigh specific capacitance (∼2440 F g -1 ), good rate capability (80.5%) under high current charge-discharge conditions, and a relatively better cycling stability (86.7% of the initial value remained after 750 cycles at 10 A g -1 ). These attractive capacitive behaviors are mainly attributed to the unique core-shell structure and the combined effect of ZnO NW arrays as short charge transfer pathways for ion diffusion and electron transfer as well as conductive Ni serving as channel for the fast electron transport to Ti substrate. This high-performance Ti/ZnO NWs/Ni hybrid structure is expected to be one of a promising electrodes for high-performance supercapacitor applications.

De Novo Construction of Redox Active Proteins.

PubMed

Moser, C C; Sheehan, M M; Ennist, N M; Kodali, G; Bialas, C; Englander, M T; Discher, B M; Dutton, P L

2016-01-01

Relatively simple principles can be used to plan and construct de novo proteins that bind redox cofactors and participate in a range of electron-transfer reactions analogous to those seen in natural oxidoreductase proteins. These designed redox proteins are called maquettes. Hydrophobic/hydrophilic binary patterning of heptad repeats of amino acids linked together in a single-chain self-assemble into 4-alpha-helix bundles. These bundles form a robust and adaptable frame for uncovering the default properties of protein embedded cofactors independent of the complexities introduced by generations of natural selection and allow us to better understand what factors can be exploited by man or nature to manipulate the physical chemical properties of these cofactors. Anchoring of redox cofactors such as hemes, light active tetrapyrroles, FeS clusters, and flavins by His and Cys residues allow cofactors to be placed at positions in which electron-tunneling rates between cofactors within or between proteins can be predicted in advance. The modularity of heptad repeat designs facilitates the construction of electron-transfer chains and novel combinations of redox cofactors and new redox cofactor assisted functions. Developing de novo designs that can support cofactor incorporation upon expression in a cell is needed to support a synthetic biology advance that integrates with natural bioenergetic pathways. © 2016 Elsevier Inc. All rights reserved.

Photoinduced electron transfer from semiconductor quantum dots to metal oxide nanoparticles

PubMed Central

Tvrdy, Kevin; Frantsuzov, Pavel A.; Kamat, Prashant V.

2011-01-01

Quantum dot-metal oxide junctions are an integral part of next-generation solar cells, light emitting diodes, and nanostructured electronic arrays. Here we present a comprehensive examination of electron transfer at these junctions, using a series of CdSe quantum dot donors (sizes 2.8, 3.3, 4.0, and 4.2 nm in diameter) and metal oxide nanoparticle acceptors (SnO2, TiO2, and ZnO). Apparent electron transfer rate constants showed strong dependence on change in system free energy, exhibiting a sharp rise at small driving forces followed by a modest rise further away from the characteristic reorganization energy. The observed trend mimics the predicted behavior of electron transfer from a single quantum state to a continuum of electron accepting states, such as those present in the conduction band of a metal oxide nanoparticle. In contrast with dye-sensitized metal oxide electron transfer studies, our systems did not exhibit unthermalized hot-electron injection due to relatively large ratios of electron cooling rate to electron transfer rate. To investigate the implications of these findings in photovoltaic cells, quantum dot-metal oxide working electrodes were constructed in an identical fashion to the films used for the electron transfer portion of the study. Interestingly, the films which exhibited the fastest electron transfer rates (SnO2) were not the same as those which showed the highest photocurrent (TiO2). These findings suggest that, in addition to electron transfer at the quantum dot-metal oxide interface, other electron transfer reactions play key roles in the determination of overall device efficiency. PMID:21149685

Photoinduced electron transfer from semiconductor quantum dots to metal oxide nanoparticles.

PubMed

Tvrdy, Kevin; Frantsuzov, Pavel A; Kamat, Prashant V

2011-01-04

Quantum dot-metal oxide junctions are an integral part of next-generation solar cells, light emitting diodes, and nanostructured electronic arrays. Here we present a comprehensive examination of electron transfer at these junctions, using a series of CdSe quantum dot donors (sizes 2.8, 3.3, 4.0, and 4.2 nm in diameter) and metal oxide nanoparticle acceptors (SnO(2), TiO(2), and ZnO). Apparent electron transfer rate constants showed strong dependence on change in system free energy, exhibiting a sharp rise at small driving forces followed by a modest rise further away from the characteristic reorganization energy. The observed trend mimics the predicted behavior of electron transfer from a single quantum state to a continuum of electron accepting states, such as those present in the conduction band of a metal oxide nanoparticle. In contrast with dye-sensitized metal oxide electron transfer studies, our systems did not exhibit unthermalized hot-electron injection due to relatively large ratios of electron cooling rate to electron transfer rate. To investigate the implications of these findings in photovoltaic cells, quantum dot-metal oxide working electrodes were constructed in an identical fashion to the films used for the electron transfer portion of the study. Interestingly, the films which exhibited the fastest electron transfer rates (SnO(2)) were not the same as those which showed the highest photocurrent (TiO(2)). These findings suggest that, in addition to electron transfer at the quantum dot-metal oxide interface, other electron transfer reactions play key roles in the determination of overall device efficiency.

Ultrafast non-radiative dynamics of atomically thin MoSe 2

DOE PAGES

Lin, Ming -Fu; Kochat, Vidya; Krishnamoorthy, Aravind; ...

2017-10-17

Non-radiative energy dissipation in photoexcited materials and resulting atomic dynamics provide a promising pathway to induce structural phase transitions in two-dimensional materials. However, these dynamics have not been explored in detail thus far because of incomplete understanding of interaction between the electronic and atomic degrees of freedom, and a lack of direct experimental methods to quantify real-time atomic motion and lattice temperature. Here, we explore the ultrafast conversion of photoenergy to lattice vibrations in a model bi-layered semiconductor, molybdenum diselenide, MoSe 2. Specifically, we characterize sub-picosecond lattice dynamics initiated by the optical excitation of electronic charge carriers in the highmore » electron-hole plasma density regime. Our results focuses on the first ten picosecond dynamics subsequent to photoexcitation before the onset of heat transfer to the substrate, which occurs on a ~100 picosecond time scale. Photoinduced atomic motion is probed by measuring the time dependent Bragg diffraction of a delayed mega-electronvolt femtosecond electron beam. Transient lattice temperatures are characterized through measurement of Bragg peak intensities and calculation of the Debye-Waller factor (DWF). These measurements show a sub-picosecond decay of Bragg diffraction and a correspondingly rapid rise in lattice temperatures. We estimate a high quantum yield for the conversion of excited charge carrier energy to lattice motion under our experimental conditions, indicative of a strong electron-phonon interaction. First principles nonadiabatic quantum molecular dynamics simulations (NAQMD) on electronically excited MoSe 2 bilayers reproduce the observed picosecond-scale increase in lattice temperature and ultrafast conversion of photoenergy to lattice vibrations. Calculation of excited-state phonon dispersion curves suggests that softened vibrational modes in the excited state are involved in efficient and rapid energy transfer between the electronic system and the lattice.« less

Ultrafast non-radiative dynamics of atomically thin MoSe 2

DOE Office of Scientific and Technical Information (OSTI.GOV)

Lin, Ming -Fu; Kochat, Vidya; Krishnamoorthy, Aravind

Non-radiative energy dissipation in photoexcited materials and resulting atomic dynamics provide a promising pathway to induce structural phase transitions in two-dimensional materials. However, these dynamics have not been explored in detail thus far because of incomplete understanding of interaction between the electronic and atomic degrees of freedom, and a lack of direct experimental methods to quantify real-time atomic motion and lattice temperature. Here, we explore the ultrafast conversion of photoenergy to lattice vibrations in a model bi-layered semiconductor, molybdenum diselenide, MoSe 2. Specifically, we characterize sub-picosecond lattice dynamics initiated by the optical excitation of electronic charge carriers in the highmore » electron-hole plasma density regime. Our results focuses on the first ten picosecond dynamics subsequent to photoexcitation before the onset of heat transfer to the substrate, which occurs on a ~100 picosecond time scale. Photoinduced atomic motion is probed by measuring the time dependent Bragg diffraction of a delayed mega-electronvolt femtosecond electron beam. Transient lattice temperatures are characterized through measurement of Bragg peak intensities and calculation of the Debye-Waller factor (DWF). These measurements show a sub-picosecond decay of Bragg diffraction and a correspondingly rapid rise in lattice temperatures. We estimate a high quantum yield for the conversion of excited charge carrier energy to lattice motion under our experimental conditions, indicative of a strong electron-phonon interaction. First principles nonadiabatic quantum molecular dynamics simulations (NAQMD) on electronically excited MoSe 2 bilayers reproduce the observed picosecond-scale increase in lattice temperature and ultrafast conversion of photoenergy to lattice vibrations. Calculation of excited-state phonon dispersion curves suggests that softened vibrational modes in the excited state are involved in efficient and rapid energy transfer between the electronic system and the lattice.« less

Strategies for microbial synthesis of high-value phytochemicals

NASA Astrophysics Data System (ADS)

Li, Sijin; Li, Yanran; Smolke, Christina D.

2018-03-01

Phytochemicals are of great pharmaceutical and agricultural importance, but often exhibit low abundance in nature. Recent demonstrations of industrial-scale production of phytochemicals in yeast have shown that microbial production of these high-value chemicals is a promising alternative to sourcing these molecules from native plant hosts. However, a number of challenges remain in the broader application of this approach, including the limited knowledge of plant secondary metabolism and the inefficient reconstitution of plant metabolic pathways in microbial hosts. In this Review, we discuss recent strategies to achieve microbial biosynthesis of complex phytochemicals, including strategies to: (1) reconstruct plant biosynthetic pathways that have not been fully elucidated by mining enzymes from native and non-native hosts or by enzyme engineering; (2) enhance plant enzyme activity, specifically cytochrome P450 activity, by improving efficiency, selectivity, expression or electron transfer; and (3) enhance overall reaction efficiency of multi-enzyme pathways by dynamic control, compartmentalization or optimization with the host's metabolism. We also highlight remaining challenges to — and future opportunities of — this approach.

Electrochemical control over photoinduced electron transfer and trapping in CdSe-CdTe quantum-dot solids.

PubMed

Boehme, Simon C; Walvis, T Ardaan; Infante, Ivan; Grozema, Ferdinand C; Vanmaekelbergh, Daniël; Siebbeles, Laurens D A; Houtepen, Arjan J

2014-07-22

Understanding and controlling charge transfer between different kinds of colloidal quantum dots (QDs) is important for devices such as light-emitting diodes and solar cells and for thermoelectric applications. Here we study photoinduced electron transfer between CdTe and CdSe QDs in a QD film. We find that very efficient electron trapping in CdTe QDs obstructs electron transfer to CdSe QDs under most conditions. Only the use of thiol ligands results in somewhat slower electron trapping; in this case the competition between trapping and electron transfer results in a small fraction of electrons being transferred to CdSe. However, we demonstrate that electron trapping can be controlled and even avoided altogether by using the unique combination of electrochemistry and transient absorption spectroscopy. When the Fermi level is raised electrochemically, traps are filled with electrons and electron transfer from CdTe to CdSe QDs occurs with unity efficiency. These results show the great importance of knowing and controlling the Fermi level in QD films and open up the possibility of studying the density of trap states in QD films as well as the systematic investigation of the intrinsic electron transfer rates in donor-acceptor films.

Impact of season, weekends and bank holidays on emergency department transfers of nursing home residents.

PubMed

Fan, C W; Keating, T; Brazil, E; Power, D; Duggan, J

2016-08-01

For urgent, unexpected clinical events, nursing home (NH) residents are transferred to the acute hospital emergency department (ED). A previous study showed that a third of transfers occurred during working hours. Our aims were to profile a one-year NH transfers to the ED and to examine the re-presentation, patient-oriented outcome and the impact of season, weekends and bank holidays on NH transfers. All NH transfers from a catchment to an ED over one year were identified using electronic patient record. Age, gender, reason for presentation, patient-oriented outcome and date and time of presentation were recorded. Representation and the interval between transfers were calculated. Number of transfers was calculated for season, weekdays/weekends and bank holidays. Student t test, Chi-square statistics and one-way ANOVA were used. Significance was set at 0.05. There were 802 transfers from 465 NH residents over a year; 501 (62.5 %) resulted in admissions, 189 (40.6 %) residents represent to the service and 80 episodes occurred within a fortnight of the last attendance. The highest transfers occurred in May (2.81 patients/day), during working hours and on Wednesdays and Thursdays (>2.5 transfers/day). 'Unwell adult' and 'falls' were the two commonest reasons for presentation. Our study showed that NH transfers occurred mainly within working hours and during weekdays. Insights into the transfer pattern and the reasons for NH patients to utilise ED will facilitate improved design and operation of the department by creating care pathways for these patients.

Hot-electron transfer in quantum-dot heterojunction films.

PubMed

Grimaldi, Gianluca; Crisp, Ryan W; Ten Brinck, Stephanie; Zapata, Felipe; van Ouwendorp, Michiko; Renaud, Nicolas; Kirkwood, Nicholas; Evers, Wiel H; Kinge, Sachin; Infante, Ivan; Siebbeles, Laurens D A; Houtepen, Arjan J

2018-06-13

Thermalization losses limit the photon-to-power conversion of solar cells at the high-energy side of the solar spectrum, as electrons quickly lose their energy relaxing to the band edge. Hot-electron transfer could reduce these losses. Here, we demonstrate fast and efficient hot-electron transfer between lead selenide and cadmium selenide quantum dots assembled in a quantum-dot heterojunction solid. In this system, the energy structure of the absorber material and of the electron extracting material can be easily tuned via a variation of quantum-dot size, allowing us to tailor the energetics of the transfer process for device applications. The efficiency of the transfer process increases with excitation energy as a result of the more favorable competition between hot-electron transfer and electron cooling. The experimental picture is supported by time-domain density functional theory calculations, showing that electron density is transferred from lead selenide to cadmium selenide quantum dots on the sub-picosecond timescale.

Electron-transfer oxidation properties of DNA bases and DNA oligomers.

PubMed

Fukuzumi, Shunichi; Miyao, Hiroshi; Ohkubo, Kei; Suenobu, Tomoyoshi

2005-04-21

Kinetics for the thermal and photoinduced electron-transfer oxidation of a series of DNA bases with various oxidants having the known one-electron reduction potentials (E(red)) in an aqueous solution at 298 K were examined, and the resulting electron-transfer rate constants (k(et)) were evaluated in light of the free energy relationship of electron transfer to determine the one-electron oxidation potentials (E(ox)) of DNA bases and the intrinsic barrier of the electron transfer. Although the E(ox) value of GMP at pH 7 is the lowest (1.07 V vs SCE) among the four DNA bases, the highest E(ox) value (CMP) is only 0.19 V higher than that of GMP. The selective oxidation of GMP in the thermal electron-transfer oxidation of GMP results from a significant decrease in the pH dependent oxidation potential due to the deprotonation of GMP*+. The one-electron reduced species of the photosensitizer produced by photoinduced electron transfer are observed as the transient absorption spectra when the free energy change of electron transfer is negative. The rate constants of electron-transfer oxidation of the guanine moieties in DNA oligomers with Fe(bpy)3(3+) and Ru(bpy)3(3+) were also determined using DNA oligomers containing different guanine (G) sequences from 1 to 10 G. The rate constants of electron-transfer oxidation of the guanine moieties in single- and double-stranded DNA oligomers with Fe(bpy)3(2+) and Ru(bpy)3(3+) are dependent on the number of sequential guanine molecules as well as on pH.

Implications of State and Local Policy on Community College Transfer in California

ERIC Educational Resources Information Center

Neault, Lynn Ceresino; Piland, William E.

2014-01-01

Lower division transfer preparation for the university has been the primary mission of community colleges since their inception creating an important pathway to baccalaureate degree attainment for many students who may not otherwise have the opportunity for higher education. Once considered fairly straightforward, the transfer pathway has become…

Advising and Progress in the Community College STEM Transfer Pathway

ERIC Educational Resources Information Center

Packard, Becky Wai-Ling; Jeffers, Kimberly C.

2013-01-01

Community college students enrolled in science and technology fields face many challenges as they pursue transfer pathways to earn a 4-year degree. Despite clear links to student persistence, advising interactions that facilitate or inhibit transfer progress are not clearly understood. In this study, 82 community college students pursuing science…

Optimal control of multiphoton ionization dynamics of small alkali aggregates

NASA Astrophysics Data System (ADS)

Lindinger, A.; Bartelt, A.; Lupulescu, C.; Vajda, S.; Woste, Ludger

2003-11-01

We have performed transient multi-photon ionization experiments on small alkali clusters of different size in order to probe their wave packet dynamics, structural reorientations, charge transfers and dissociative events in different vibrationally excited electronic states including their ground state. The observed processes were highly dependent on the irradiated pulse parameters like wavelength range or its phase and amplitude; an emphasis to employ a feedback control system for generating the optimum pulse shapes. Their spectral and temporal behavior reflects interesting properties about the investigated system and the irradiated photo-chemical process. First, we present the vibrational dynamics of bound electronically excited states of alkali dimers and trimers. The scheme for observing the wave packet dynamics in the electronic ground state using stimulated Raman-pumping is shown. Since the employed pulse parameters significantly influence the efficiency of the irradiated dynamic pathways photo-induced ioniziation experiments were carried out. The controllability of 3-photon ionization pathways is investigated on the model-like systems NaK and K2. A closed learning loop for adaptive feedback control is used to find the optimal fs pulse shape. Sinusoidal parameterizations of the spectral phase modulation are investigated in regard to the obtained optimal field. By reducing the number of parameters and thereby the complexity of the phase moduation, optimal pulse shapes can be generated that carry fingerprints of the molecule's dynamical properties. This enables to find "understandable" optimal pulse forms and offers the possiblity to gain insight into the photo-induced control process. Characteristic motions of the involved wave packets are proposed to explain the optimized dynamic dissociation pathways.

14 CFR 1274.931 - Electronic funds transfer payment methods.

Code of Federal Regulations, 2011 CFR

2011-01-01

... 14 Aeronautics and Space 5 2011-01-01 2010-01-01 true Electronic funds transfer payment methods... COOPERATIVE AGREEMENTS WITH COMMERCIAL FIRMS Other Provisions and Special Conditions § 1274.931 Electronic funds transfer payment methods. Electronic Funds Transfer Payment Methods July 2002 Payments under this...

77 FR 40459 - Electronic Fund Transfers (Regulation E); Correction

Federal Register 2010, 2011, 2012, 2013, 2014

2012-07-10

... Electronic Fund Transfers (Regulation E); Correction AGENCY: Bureau of Consumer Financial Protection. ACTION... published the Final Rule (77 FR 6194), which implements the Electronic Fund Transfer Act, and the official... Sec. 1005.3(a) in the interim final rule, Electronic Fund Transfers (Regulation E), published on...

14 CFR 1274.931 - Electronic funds transfer payment methods.

Code of Federal Regulations, 2013 CFR

2013-01-01

... 14 Aeronautics and Space 5 2013-01-01 2013-01-01 false Electronic funds transfer payment methods... COOPERATIVE AGREEMENTS WITH COMMERCIAL FIRMS Other Provisions and Special Conditions § 1274.931 Electronic funds transfer payment methods. Electronic Funds Transfer Payment Methods July 2002 Payments under this...

On the unusual stability of valence anions of thymine based on very rare tautomers. A computational study

DOE Office of Scientific and Technical Information (OSTI.GOV)

Mazurkiewicz, Kamil; Bachorz, Rafal; Gutowski, Maciej S.

2006-12-07

We characterized valence-type and dipole-bound anionic states of thymine using various electronic structure methods, with the most accurate results obtained at the CCSD(T)/aug-cc-pVDZ level of theory followed by extrapolations to complete basis set limits. We found that the most stable anion in the gas phase is related to neither the canonical 2,4-dioxo nor a rare imino-hydroxy tautomer. Instead, it is related to an imino-oxo tautomer, in which the N1H proton is transferred to the C5 atom. This valence anion is characterized by an electron vertical detachment energy (VDE) of 1251 meV and it is adiabatically stable with respect to themore » canonical neutral by 2.4 kcal/mol. It is also more stable than the dipole-bound and valence anion of the canonical tautomer. The latter is adiabatically unbound with respect to by 0.1 kcal/mol and this instability is smaller than the uncertainty of the computational model used. The VDE values for and are 55 and 457 meV, respectively. Another, anionic, low-lying imino-oxo tautomer with a VDE of 2458 meV has a proton transferred from N3H to C5. It is less stable than by 3.2 kcal/mol. The mechanism of formation of anionic tautomers with the carbons C5 or C6 protonated may involve intermolecular proton transfer or dissociative electron attachment to the canonical neutral tautomer followed by a barrier-free attachment of a hydrogen atom to C5. The six-member ring structure of anionic tautomers with carbon atoms protonated might be unstable upon an excess electron detachment. Indeed, the neutral systems resulting from electron detachment from and evolve, along barrier-free decomposition pathways, to a linear or a bicyclo structure, respectively, which might be viewed as lesions to DNA.« less

Inorganic carbon fixation by chemosynthetic ectosymbionts and nutritional transfers to the hydrothermal vent host-shrimp Rimicaris exoculata

PubMed Central

Ponsard, Julie; Cambon-Bonavita, Marie-Anne; Zbinden, Magali; Lepoint, Gilles; Joassin, André; Corbari, Laure; Shillito, Bruce; Durand, Lucile; Cueff-Gauchard, Valérie; Compère, Philippe

2013-01-01

The shrimp Rimicaris exoculata dominates several hydrothermal vent ecosystems of the Mid-Atlantic Ridge and is thought to be a primary consumer harbouring a chemoautotrophic bacterial community in its gill chamber. The aim of the present study was to test current hypotheses concerning the epibiont's chemoautotrophy, and the mutualistic character of this association. In-vivo experiments were carried out in a pressurised aquarium with isotope-labelled inorganic carbon (NaH13CO3 and NaH14CO3) in the presence of two different electron donors (Na2S2O3 and Fe2+) and with radiolabelled organic compounds (14C-acetate and 3H-lysine) chosen as potential bacterial substrates and/or metabolic by-products in experiments mimicking transfer of small biomolecules from epibionts to host. The bacterial epibionts were found to assimilate inorganic carbon by chemoautotrophy, but many of them (thick filaments of epsilonproteobacteria) appeared versatile and able to switch between electron donors, including organic compounds (heterotrophic acetate and lysine uptake). At least some of them (thin filamentous gammaproteobacteria) also seem capable of internal energy storage that could supply chemosynthetic metabolism for hours under conditions of electron donor deprivation. As direct nutritional transfer from bacteria to host was detected, the association appears as true mutualism. Import of soluble bacterial products occurs by permeation across the gill chamber integument, rather than via the digestive tract. This first demonstration of such capabilities in a decapod crustacean supports the previously discarded hypothesis of transtegumental absorption of dissolved organic matter or carbon as a common nutritional pathway. PMID:22914596

Enhanced Oxidative and Adsorptive Removal of Diclofenac in Heterogeneous Fenton-like Reaction with Sulfide Modified Nanoscale Zerovalent Iron.

PubMed

Su, Yiming; Jassby, David; Song, Shikun; Zhou, Xuefei; Zhao, Hongying; Filip, Jan; Petala, Eleni; Zhang, Yalei

2018-06-05

Sulfidation of nanoscale zerovalent iron (nZVI) has shown some fundamental improvements on reactivity and selectivity toward pollutants in dissolved-oxygen (DO)-stimulated Fenton-like reaction systems (DO/S-nZVI system). However, the pristine microstructure of sulfide-modified nanoscale zerovalent iron (S-nZVI) remains uncovered. In addition, the relationship between pollutant removal and the oxidation of the S-nZVI is largely unknown. The present study confirms that sulfidation not only imparts sulfide and sulfate groups onto the surface of the nanoparticle (both on the oxide shell and on flake-like structures) but also introduces sulfur into the Fe(0) core region. Sulfidation greatly inhibits the four-electron transfer pathway between Fe(0) and oxygen but facilitates the electron transfer from Fe(0) to surface-bound Fe(III) and consecutive single-electron transfer for the generation of H 2 O 2 and hydroxyl radical. In the DO/S-nZVI system, slight sulfidation (S/Fe molar ratio = 0.1) is able to nearly double the oxidative removal efficacy of diclofenac (DCF) (from 17.8 to 34.2%), whereas moderate degree of sulfidation (S/Fe molar ratio = 0.3) significantly enhances both oxidation and adsorption of DCF. Furthermore, on the basis of the oxidation model of S-nZVI, the DCF removal process can be divided into two steps, which are well modeled by parabolic and logarithmic law separately. This study bridges the knowledge gap between pollutant removal and the oxidation process of chemically modified iron-based nanomaterials.

A hybrid biocatalyst consisting of silver nanoparticle and naphthalenethiol self-assembled monolayer prepared for anchoring glucose oxidase and its use for an enzymatic biofuel cell

NASA Astrophysics Data System (ADS)

Christwardana, Marcelinus; Kim, Do-Heyoung; Chung, Yongjin; Kwon, Yongchai

2018-01-01

A novel hybrid biocatalyst is synthesized by the enzyme composite consisting of silver nanoparticle (AgNP), naphthalene-thiol based couplers (Naph-SH) and glucose oxidase (GOx), which is then bonded with the supporter consisting of polyethyleneimine (PEI) and carbon nanotube (CNT) (CNT/PEI/AgNPs/Naph-SH/GOx) to facilitate glucose oxidation reaction (GOR). Here, the AgNPs play a role in obstructing denaturation of the GOx molecules from the supporter because of Ag-thiol bond, while the PEIs have the AgNPs keep their states without getting ionized by hydrogen peroxide produced during anodic reaction. The Naph-SHs also prevent ionization of the AgNP by forming self-assembled monolayer on their surface. Such roles of each component enable the catalyst to form (i) hydrophobic interaction between the GOx molecules and supporter and (ii) π-conjugated electron pathway between the GOx molecules and AgNP, promoting electron transfer. Catalytic nature of the catalyst is characterized by measuring catalytic activity and performance of enzymatic biofuel cell (EBC) using the catalyst. Regarding the catalytic activity, the catalyst leads to high electron transfer rate constant (9.6 ± 0.4 s-1), low Michaelis-Menten constant (0.51 ± 0.04 mM), and low charge transfer resistance (7.3 Ω cm2) and high amount of immobilized GOx (54.6%), while regarding the EBC performance, high maximum power density (1.46 ± 0.07 mW cm-2) with superior long-term stability result are observed.

Proximity effects across oxide-interfaces of superconductor-insulator-ferromagnet hybrid heterostructure.

PubMed

Prajapat, C L; Singh, Surendra; Bhattacharya, D; Ravikumar, G; Basu, S; Mattauch, S; Zheng, Jian-Guo; Aoki, T; Paul, Amitesh

2018-02-27

A case study of electron tunneling or charge-transfer-driven orbital ordering in superconductor (SC)-ferromagnet (FM) interfaces has been conducted in heteroepitaxial YBa 2 Cu 3 O 7 (YBCO)/La 0.67 Sr 0.33 MnO 3 (LSMO) multilayers interleaved with and without an insulating SrTiO 3 (STO) layer between YBCO and LSMO. X-ray magnetic circular dichroism experiments revealed anti-parallel alignment of Mn magnetic moments and induced Cu magnetic moments in a YBCO/LSMO multilayer. As compared to an isolated LSMO layer, the YBCO/LSMO multilayer displayed a (50%) weaker Mn magnetic signal, which is related to the usual proximity effect. It was a surprise that a similar proximity effect was also observed in a YBCO/STO/LSMO multilayer, however, the Mn signal was reduced by 20%. This reduced magnetic moment of Mn was further verified by depth sensitive polarized neutron reflectivity. Electron energy loss spectroscopy experiment showed the evidence of Ti magnetic polarization at the interfaces of the YBCO/STO/LSMO multilayer. This crossover magnetization is due to a transfer of interface electrons that migrate from Ti (4+)-δ to Mn at the STO/LSMO interface and to Cu 2+ at the STO/YBCO interface, with hybridization via O 2p orbitals. So charge-transfer driven orbital ordering is the mechanism responsible for the observed proximity effect and Mn-Cu anti-parallel coupling in YBCO/STO/LSMO. This work provides an effective pathway in understanding the aspect of long range proximity effect and consequent orbital degeneracy parameter in magnetic coupling.

14 CFR § 1260.69 - Electronic funds transfer payment methods.

Code of Federal Regulations, 2014 CFR

2014-01-01

... 14 Aeronautics and Space 5 2014-01-01 2014-01-01 false Electronic funds transfer payment methods... GRANTS AND COOPERATIVE AGREEMENTS General Special Conditions § 1260.69 Electronic funds transfer payment methods. Electronic Funds Transfer Payment Methods October 2000 (a) Payments under this grant will be made...

14 CFR 1260.69 - Electronic funds transfer payment methods.

Code of Federal Regulations, 2013 CFR

2013-01-01

... 14 Aeronautics and Space 5 2013-01-01 2013-01-01 false Electronic funds transfer payment methods... COOPERATIVE AGREEMENTS General Special Conditions § 1260.69 Electronic funds transfer payment methods. Electronic Funds Transfer Payment Methods October 2000 (a) Payments under this grant will be made by the...

14 CFR 1260.69 - Electronic funds transfer payment methods.

Code of Federal Regulations, 2012 CFR

2012-01-01

... 14 Aeronautics and Space 5 2012-01-01 2012-01-01 false Electronic funds transfer payment methods... COOPERATIVE AGREEMENTS General Special Conditions § 1260.69 Electronic funds transfer payment methods. Electronic Funds Transfer Payment Methods October 2000 (a) Payments under this grant will be made by the...

14 CFR 1260.69 - Electronic funds transfer payment methods.

Code of Federal Regulations, 2011 CFR

2011-01-01

... 14 Aeronautics and Space 5 2011-01-01 2010-01-01 true Electronic funds transfer payment methods... COOPERATIVE AGREEMENTS General Special Conditions § 1260.69 Electronic funds transfer payment methods. Electronic Funds Transfer Payment Methods October 2000 (a) Payments under this grant will be made by the...

Theoretical Analysis of Cobalt Hangman Porphyrins: Ligand Dearomatization and Mechanistic Implications for Hydrogen Evolution

DOE PAGES

Solis, Brian H.; Maher, Andrew G.; Honda, Tatsuhiko; ...

2014-11-06

The design of molecular electrocatalysts for hydrogen evolution has been targeted as a strategy for the conversion of solar energy to chemical fuels. In cobalt hangman porphyrins, a carboxylic acid group on a xanthene backbone is positioned over a metalloporphyrin to serve as a proton relay. A key proton-coupled electron transfer (PCET) step along the hydrogen evolution pathway occurs via a sequential ET-PT mechanism in which electron transfer (ET) is followed by proton transfer (PT). Herein theoretical calculations are employed to investigate the mechanistic pathways of these hangman metalloporphyrins. The calculations confirm the ET-PT mechanism by illustrating that the calculatedmore » reduction potentials for this mechanism are consistent with experimental data. Under strong-acid conditions, the calculations indicate that this catalyst evolves H 2 by protonation of a formally Co(II) hydride intermediate, as suggested by previous experiments. Under weak-acid conditions, however, the calculations reveal a mechanism that proceeds via a phlorin intermediate, in which the meso carbon of the porphyrin is protonated. In the first electrochemical reduction, the neutral Co(II) species is reduced to a monoanionic singlet Co(I) species. Subsequent reduction leads to a dianionic doublet, formally a Co(0) complex in which substantial mixing of Co and porphyrin orbitals indicates ligand redox noninnocence. The partial reduction of the ligand disrupts the aromaticity in the porphyrin ring. As a result of this ligand dearomatization, protonation of the dianionic species is significantly more thermodynamically favorable at the meso carbon than at the metal center, and the ET-PT mechanism leads to a dianionic phlorin species. According to the proposed mechanism, the carboxylate group of this dianionic phlorin species is reprotonated, the species is reduced again, and H 2 is evolved from the protonated carboxylate and the protonated carbon. This proposed mechanism is a guidepost for future experimental studies of proton relays involving noninnocent ligand platforms.« less

Regulation of Photosynthetic Electron Transport and Photoinhibition

PubMed Central

Roach, Thomas; Krieger-Liszkay, Anja Krieger

2014-01-01

Photosynthetic organisms and isolated photosystems are of interest for technical applications. In nature, photosynthetic electron transport has to work efficiently in contrasting environments such as shade and full sunlight at noon. Photosynthetic electron transport is regulated on many levels, starting with the energy transfer processes in antenna and ending with how reducing power is ultimately partitioned. This review starts by explaining how light energy can be dissipated or distributed by the various mechanisms of non-photochemical quenching, including thermal dissipation and state transitions, and how these processes influence photoinhibition of photosystem II (PSII). Furthermore, we will highlight the importance of the various alternative electron transport pathways, including the use of oxygen as the terminal electron acceptor and cyclic flow around photosystem I (PSI), the latter which seem particularly relevant to preventing photoinhibition of photosystem I. The control of excitation pressure in combination with the partitioning of reducing power influences the light-dependent formation of reactive oxygen species in PSII and in PSI, which may be a very important consideration to any artificial photosynthetic system or technical device using photosynthetic organisms. PMID:24678670

The influence of dielectric relaxation on intramolecular electron transfer

NASA Astrophysics Data System (ADS)

Heitele, H.; Michel-Beyerle, M. E.; Finckh, P.

1987-07-01

An unusually strong temperature dependence on the intramolecular electron-transfer rate has been observed for bridged donor-acceptor compounds in propylene glycol solution. In the frame of recent electron-transfer theories this effect reflects the influence of dielectric relaxation dynamics on electron transfer. With increasing dielectric relaxation time a smooth transition from non-adiabatic to solvent-controlled adiabatic behaviour is observed. The electron transfer rate in the solvent-controlled adiabatic limit is dominated by an inhomogeneous distribution of relaxation times.

DOE Office of Scientific and Technical Information (OSTI.GOV)

Cheng, Tao; Xiao, Hai; Goddard, William A.

Copper is the only elemental metal that reduces a significant fraction of CO 2 to hydrocarbons and alcohols, but the atomistic reaction mechanism that controls the product distributions is not known because it has not been possible to detect the reaction intermediates on the electrode surface experimentally, or to carry out Quantum Mechanics (QM) calculations with a realistic description of the electrolyte (water). We carry out QM calculations with an explicit description of water on the Cu(100) surface (experimentally shown to be stable under CO 2 reduction reaction conditions) to examine the initial reaction pathways to form CO and formatemore » (HCOO –) from CO 2 through free energy calculations at 298 K and pH 7. We find that CO formation proceeds from physisorbed CO 2 to chemisorbed CO 2 (*CO 2 δ-), with a free energy barrier of ΔG ‡ = 0.43 eV, the rate-determining step (RDS). The subsequent barriers of protonating *CO 2 δ- to form COOH* and then dissociating COOH* to form *CO are 0.37 and 0.30 eV, respectively. HCOO– formation proceeds through a very different pathway in which physisorbed CO 2 reacts directly with a surface H* (along with electron transfer), leading to ΔG ‡ = 0.80 eV. Thus, the competition between CO formation and HCOO – formation occurs in the first electron-transfer step. On Cu(100), the RDS for CO formation is lower, making CO the predominant product. Therefore, to alter the product distribution, we need to control this first step of CO 2 binding, which might involve controlling pH, alloying, or changing the structure at the nanoscale.« less

Vibronic Wavepackets and Energy Transfer in Cryptophyte Light-Harvesting Complexes.

PubMed

Jumper, Chanelle C; van Stokkum, Ivo H M; Mirkovic, Tihana; Scholes, Gregory D

2018-06-21

Determining the key features of high-efficiency photosynthetic energy transfer remains an ongoing task. Recently, there has been evidence for the role of vibronic coherence in linking donor and acceptor states to redistribute oscillator strength for enhanced energy transfer. To gain further insights into the interplay between vibronic wavepackets and energy-transfer dynamics, we systematically compare four structurally related phycobiliproteins from cryptophyte algae by broad-band pump-probe spectroscopy and extend a parametric model based on global analysis to include vibrational wavepacket characterization. The four phycobiliproteins isolated from cryptophyte algae are two "open" structures and two "closed" structures. The closed structures exhibit strong exciton coupling in the central dimer. The dominant energy-transfer pathway occurs on the subpicosecond timescale across the largest energy gap in each of the proteins, from central to peripheral chromophores. All proteins exhibit a strong 1585 cm -1 coherent oscillation whose relative amplitude, a measure of vibronic intensity borrowing from resonance between donor and acceptor states, scales with both energy-transfer rates and damping rates. Central exciton splitting may aid in bringing the vibronically linked donor and acceptor states into better resonance resulting in the observed doubled rate in the closed structures. Several excited-state vibrational wavepackets persist on timescales relevant to energy transfer, highlighting the importance of further investigation of the interplay between electronic coupling and nuclear degrees of freedom in studies on high-efficiency photosynthesis.

Ultrafast time-resolved carotenoid to-bacteriochlorophyll energy transfer in LH2 complexes from photosynthetic bacteria.

PubMed

Cong, Hong; Niedzwiedzki, Dariusz M; Gibson, George N; LaFountain, Amy M; Kelsh, Rhiannon M; Gardiner, Alastair T; Cogdell, Richard J; Frank, Harry A

2008-08-28

Steady-state and ultrafast time-resolved optical spectroscopic investigations have been carried out at 293 and 10 K on LH2 pigment-protein complexes isolated from three different strains of photosynthetic bacteria: Rhodobacter (Rb.) sphaeroides G1C, Rb. sphaeroides 2.4.1 (anaerobically and aerobically grown), and Rps. acidophila 10050. The LH2 complexes obtained from these strains contain the carotenoids, neurosporene, spheroidene, spheroidenone, and rhodopin glucoside, respectively. These molecules have a systematically increasing number of pi-electron conjugated carbon-carbon double bonds. Steady-state absorption and fluorescence excitation experiments have revealed that the total efficiency of energy transfer from the carotenoids to bacteriochlorophyll is independent of temperature and nearly constant at approximately 90% for the LH2 complexes containing neurosporene, spheroidene, spheroidenone, but drops to approximately 53% for the complex containing rhodopin glucoside. Ultrafast transient absorption spectra in the near-infrared (NIR) region of the purified carotenoids in solution have revealed the energies of the S1 (2(1)Ag-)-->S2 (1(1)Bu+) excited-state transitions which, when subtracted from the energies of the S0 (1(1)Ag-)-->S2 (1(1)Bu+) transitions determined by steady-state absorption measurements, give precise values for the positions of the S1 (2(1)Ag-) states of the carotenoids. Global fitting of the ultrafast spectral and temporal data sets have revealed the dynamics of the pathways of de-excitation of the carotenoid excited states. The pathways include energy transfer to bacteriochlorophyll, population of the so-called S* state of the carotenoids, and formation of carotenoid radical cations (Car*+). The investigation has found that excitation energy transfer to bacteriochlorophyll is partitioned through the S1 (1(1)Ag-), S2 (1(1)Bu+), and S* states of the different carotenoids to varying degrees. This is understood through a consideration of the energies of the states and the spectral profiles of the molecules. A significant finding is that, due to the low S1 (2(1)Ag-) energy of rhodopin glucoside, energy transfer from this state to the bacteriochlorophylls is significantly less probable compared to the other complexes. This work resolves a long-standing question regarding the cause of the precipitous drop in energy transfer efficiency when the extent of pi-electron conjugation of the carotenoid is extended from ten to eleven conjugated carbon-carbon double bonds in LH2 complexes from purple photosynthetic bacteria.

12 CFR 205.15 - Electronic fund transfer of government benefits.

Code of Federal Regulations, 2011 CFR

2011-01-01

... 12 Banks and Banking 2 2011-01-01 2011-01-01 false Electronic fund transfer of government benefits. 205.15 Section 205.15 Banks and Banking FEDERAL RESERVE SYSTEM BOARD OF GOVERNORS OF THE FEDERAL RESERVE SYSTEM ELECTRONIC FUND TRANSFERS (REGULATION E) § 205.15 Electronic fund transfer of government...

12 CFR 1005.3 - Coverage.

Code of Federal Regulations, 2014 CFR

2014-01-01

...-time electronic fund transfer from a consumer's account. The consumer must authorize the transfer. (ii... one-time electronic fund transfer (in providing a check to a merchant or other payee for the MICR... transfer. A consumer authorizes a one-time electronic fund transfer from his or her account to pay the fee...

Low-Energy Ballistic Transfers to Lunar Halo Orbits

NASA Technical Reports Server (NTRS)

Parker, Jeffrey S.

2009-01-01

Recent lunar missions have begun to take advantage of the benefits of low-energy ballistic transfers between the Earth and the Moon rather than implementing conventional Hohmann-like lunar transfers. Both Artemis and GRAIL plan to implement low-energy lunar transfers in the next few years. This paper explores the characteristics and potential applications of many different families of low-energy ballistic lunar transfers. The transfers presented here begin from a wide variety of different orbits at the Earth and follow several different distinct pathways to the Moon. This paper characterizes these pathways to identify desirable low-energy lunar transfers for future lunar missions.

12 CFR 205.14 - Electronic fund transfer service provider not holding consumer's account.

Code of Federal Regulations, 2010 CFR

2010-01-01

... consumer learns of the loss or theft; and extends the time periods for reporting unauthorized transfers or... 12 Banks and Banking 2 2010-01-01 2010-01-01 false Electronic fund transfer service provider not... GOVERNORS OF THE FEDERAL RESERVE SYSTEM ELECTRONIC FUND TRANSFERS (REGULATION E) § 205.14 Electronic fund...

12 CFR 205.14 - Electronic fund transfer service provider not holding consumer's account.

Code of Federal Regulations, 2013 CFR

2013-01-01

... consumer learns of the loss or theft; and extends the time periods for reporting unauthorized transfers or... 12 Banks and Banking 2 2013-01-01 2013-01-01 false Electronic fund transfer service provider not... GOVERNORS OF THE FEDERAL RESERVE SYSTEM ELECTRONIC FUND TRANSFERS (REGULATION E) § 205.14 Electronic fund...

12 CFR 205.14 - Electronic fund transfer service provider not holding consumer's account.

Code of Federal Regulations, 2014 CFR

2014-01-01

... consumer learns of the loss or theft; and extends the time periods for reporting unauthorized transfers or... 12 Banks and Banking 2 2014-01-01 2014-01-01 false Electronic fund transfer service provider not... GOVERNORS OF THE FEDERAL RESERVE SYSTEM ELECTRONIC FUND TRANSFERS (REGULATION E) § 205.14 Electronic fund...

12 CFR 205.14 - Electronic fund transfer service provider not holding consumer's account.

Code of Federal Regulations, 2011 CFR

2011-01-01

... consumer learns of the loss or theft; and extends the time periods for reporting unauthorized transfers or... 12 Banks and Banking 2 2011-01-01 2011-01-01 false Electronic fund transfer service provider not... GOVERNORS OF THE FEDERAL RESERVE SYSTEM ELECTRONIC FUND TRANSFERS (REGULATION E) § 205.14 Electronic fund...

12 CFR 205.14 - Electronic fund transfer service provider not holding consumer's account.

Code of Federal Regulations, 2012 CFR

2012-01-01

... consumer learns of the loss or theft; and extends the time periods for reporting unauthorized transfers or... 12 Banks and Banking 2 2012-01-01 2012-01-01 false Electronic fund transfer service provider not... GOVERNORS OF THE FEDERAL RESERVE SYSTEM ELECTRONIC FUND TRANSFERS (REGULATION E) § 205.14 Electronic fund...

[Regulation effects of short sunlight on two electron transport pathways in nectarine flower bud during dormancy induction].

PubMed

Li, Dong-Mei; Zhang, Hai-Sen; Tan, Qiu-Ping; Li, Ling; Yu, Qin; Gao, Dong-Sheng

2011-11-01

Taking the nectarine variety 'Shuguang' (Prunus persica var. nectariana cv. Shuguang) as test material, and by using respiration inhibitors KCN and SHAM, this paper studied the cytochrome electron transport pathway and the alternative respiration pathway in nectarine flower bud during dormancy induction under the effects of short sunlight. Both the total respiration rate (V(t)) and the cytochrome electron transport pathway respiration rate (rho' V(cyt)) presented double hump-shaped variation. Short sunlight brought the first-hump of V(t) and rho' V(cyt), forward and delayed the second-hump synchronously, inhibited the rho' V(cyt), but had no significant effects on the V(t). The capacity (V(alt)) and activity (rho V (alt)) of alternative respiration pathway also varied in double hump-shape, and the variation was basically in synchronous. Short sunlight made the first climax of V(alt) and rhoV(alt) advanced, but had little effects on the later period climax. The inhibition of cytochrome electron transport pathway and the enhancement of alternative respiration pathway were the important features of nectarine flower bud during dormancy induction, and according to the respective contributions of the two electron transport pathways to the total respiration rate, the cytochrome electron transport pathway was still the main pathway of electron transport, whereas the alternative respiration pathway played an auxiliary and branched role.

Lichen Symbiosis: Nature's High Yielding Machines for Induced Hydrogen Production

PubMed Central

Papazi, Aikaterini; Kastanaki, Elizabeth; Pirintsos, Stergios; Kotzabasis, Kiriakos

2015-01-01

Hydrogen is a promising future energy source. Although the ability of green algae to produce hydrogen has long been recognized (since 1939) and several biotechnological applications have been attempted, the greatest obstacle, being the O2-sensitivity of the hydrogenase enzyme, has not yet been overcome. In the present contribution, 75 years after the first report on algal hydrogen production, taking advantage of a natural mechanism of oxygen balance, we demonstrate high hydrogen yields by lichens. Lichens have been selected as the ideal organisms in nature for hydrogen production, since they consist of a mycobiont and a photobiont in symbiosis. It has been hypothesized that the mycobiont’s and photobiont’s consumption of oxygen (increase of COX and AOX proteins of mitochondrial respiratory pathways and PTOX protein of chrolorespiration) establishes the required anoxic conditions for the activation of the phycobiont’s hydrogenase in a closed system. Our results clearly supported the above hypothesis, showing that lichens have the ability to activate appropriate bioenergetic pathways depending on the specific incubation conditions. Under light conditions, they successfully use the PSII-dependent and the PSII-independent pathways (decrease of D1 protein and parallel increase of PSaA protein) to transfer electrons to hydrogenase, while under dark conditions, lichens use the PFOR enzyme and the dark fermentative pathway to supply electrons to hydrogenase. These advantages of lichen symbiosis in combination with their ability to survive in extreme environments (while in a dry state) constitute them as unique and valuable hydrogen producing natural factories and pave the way for future biotechnological applications. PMID:25826211

Anomalous single-electron transfer in common-gate quadruple-dot single-electron devices with asymmetric junction capacitances

NASA Astrophysics Data System (ADS)

Imai, Shigeru; Ito, Masato

2018-06-01

In this paper, anomalous single-electron transfer in common-gate quadruple-dot turnstile devices with asymmetric junction capacitances is revealed. That is, the islands have the same total number of excess electrons at high and low gate voltages of the swing that transfers a single electron. In another situation, two electrons enter the islands from the source and two electrons leave the islands for the source and drain during a gate voltage swing cycle. First, stability diagrams of the turnstile devices are presented. Then, sequences of single-electron tunneling events by gate voltage swings are investigated, which demonstrate the above-mentioned anomalous single-electron transfer between the source and the drain. The anomalous single-electron transfer can be understood by regarding the four islands as “three virtual islands and a virtual source or drain electrode of a virtual triple-dot device”. The anomalous behaviors of the four islands are explained by the normal behavior of the virtual islands transferring a single electron and the behavior of the virtual electrode.

Apparatus and method of direct water cooling several parallel circuit cards each containing several chip packages

DOEpatents

Cipolla, Thomas M [Katonah, NY; Colgan, Evan George [Chestnut Ridge, NY; Coteus, Paul W [Yorktown Heights, NY; Hall, Shawn Anthony [Pleasantville, NY; Tian, Shurong [Mount Kisco, NY

2011-12-20

A cooling apparatus, system and like method for an electronic device includes a plurality of heat producing electronic devices affixed to a wiring substrate. A plurality of heat transfer assemblies each include heat spreaders and thermally communicate with the heat producing electronic devices for transferring heat from the heat producing electronic devices to the heat transfer assemblies. The plurality of heat producing electronic devices and respective heat transfer assemblies are positioned on the wiring substrate having the regions overlapping. A heat conduit thermally communicates with the heat transfer assemblies. The heat conduit circulates thermally conductive fluid therethrough in a closed loop for transferring heat to the fluid from the heat transfer assemblies via the heat spreader. A thermally conductive support structure supports the heat conduit and thermally communicates with the heat transfer assemblies via the heat spreader transferring heat to the fluid of the heat conduit from the support structure.

Latino and African-American Students' Transfer Pathway to Elite Education in California

ERIC Educational Resources Information Center

Melguizo, Tatiana

2007-01-01

Transfer is a crucial point in a student's educational pathway since a student who fails to transfer will not be able to attain a bachelor's degree or the benefits that accompany it, such as middle-class status and higher earnings. When members of ethnic minority groups are particularly disadvantaged in reaching their full educational potential, a…

Acid/base-regulated reversible electron transfer disproportionation of N–N linked bicarbazole and biacridine derivatives† †Electronic supplementary information (ESI) available: Experimental information, synthesis and characterization data, NMR spectra, solid state NMR data, X-ray data, ESR spectra, UV-Vis-NIR spectra, fluorescence spectra, kinetic experiments, theoretical calculations, Tables S1–S8, Scheme S1, Fig. S1–12, References. CCDC 1025063, 1038914, 1049677 and 1040722. For ESI and crystallographic data in CIF or other electronic format see DOI: 10.1039/c5sc00946d

PubMed Central

Pandit, Palash; Yamamoto, Koji; Nakamura, Toshikazu; Nishimura, Katsuyuki; Kurashige, Yuki; Yanai, Takeshi; Nakamura, Go; Masaoka, Shigeyuki; Furukawa, Ko; Yakiyama, Yumi; Kawano, Masaki

2015-01-01

Regulation of electron transfer on organic substances by external stimuli is a fundamental issue in science and technology, which affects organic materials, chemical synthesis, and biological metabolism. Nevertheless, acid/base-responsive organic materials that exhibit reversible electron transfer have not been well studied and developed, owing to the difficulty in inventing a mechanism to associate acid/base stimuli and electron transfer. We discovered a new phenomenon in which N–N linked bicarbazole (BC) and tetramethylbiacridine (TBA) derivatives undergo electron transfer disproportionation by acid stimulus, forming their stable radical cations and reduced species. The reaction occurs through a biradical intermediate generated by the acid-triggered N–N bond cleavage reaction of BC or TBA, which acts as a two electron acceptor to undergo electron transfer reactions with two equivalents of BC or TBA. In addition, in the case of TBA the disproportionation reaction is highly reversible through neutralization with NEt3, which recovers TBA through back electron transfer and N–N bond formation reactions. This highly reversible electron transfer reaction is possible due to the association between the acid stimulus and electron transfer via the acid-regulated N–N bond cleavage/formation reactions which provide an efficient switching mechanism, the ability of the organic molecules to act as multi-electron donors and acceptors, the extraordinary stability of the radical species, the highly selective reactivity, and the balance of the redox potentials. This discovery provides new design concepts for acid/base-regulated organic electron transfer systems, chemical reagents, or organic materials. PMID:29218181

Rate of Interfacial Electron Transfer through the 1,2,3-Triazole Linkage

PubMed Central

Devaraj, Neal K.; Decreau, Richard A.; Ebina, Wataru; Collman, James P.; Chidsey, Christopher E. D.

2012-01-01

The rate of electron transfer is measured to two ferrocene and one iron tetraphenylporphyrin redox species coupled through terminal acetylenes to azide-terminated thiol monolayers by the Cu(I)-catalyzed azide–alkyne cycloaddition (a Sharpless “click” reaction) to form the 1,2,3-triazole linkage. The high yield, chemoselectivity, convenience, and broad applicability of this triazole formation reaction make such a modular assembly strategy very attractive. Electron-transfer rate constants from greater than 60,000 to 1 s−1 are obtained by varying the length and conjugation of the electron-transfer bridge and by varying the surrounding diluent thiols in the monolayer. Triazole and the triazole carbonyl linkages provide similar electronic coupling for electron transfer as esters. The ability to vary the rate of electron transfer to many different redox species over many orders of magnitude by using modular coupling chemistry provides a convenient way to study and control the delivery of electrons to multielectron redox catalysts and similar interfacial systems that require controlled delivery of electrons. PMID:16898751

Resolving the role of femtosecond heated electrons in ultrafast spin dynamics.

PubMed

Mendil, J; Nieves, P; Chubykalo-Fesenko, O; Walowski, J; Santos, T; Pisana, S; Münzenberg, M

2014-02-05

Magnetization manipulation is essential for basic research and applications. A fundamental question is, how fast can the magnetization be reversed in nanoscale magnetic storage media. When subject to an ultrafast laser pulse, the speed of the magnetization dynamics depends on the nature of the energy transfer pathway. The order of the spin system can be effectively influenced through spin-flip processes mediated by hot electrons. It has been predicted that as electrons drive spins into the regime close to almost total demagnetization, characterized by a loss of ferromagnetic correlations near criticality, a second slower demagnetization process takes place after the initial fast drop of magnetization. By studying FePt, we unravel the fundamental role of the electronic structure. As the ferromagnet Fe becomes more noble in the FePt compound, the electronic structure is changed and the density of states around the Fermi level is reduced, thereby driving the spin correlations into the limit of critical fluctuations. We demonstrate the impact of the electrons and the ferromagnetic interactions, which allows a general insight into the mechanisms of spin dynamics when the ferromagnetic state is highly excited, and identifies possible recording speed limits in heat-assisted magnetization reversal.

Reaction Intermediates of Quinol Oxidation in a Photoactivatable System that Mimics Electron Transfer in the Cytochrome bc1 Complex

DOE Office of Scientific and Technical Information (OSTI.GOV)

Cape, Jonathan L.; Bowman, Michael K.; Kramer, David M.

2005-03-30

Current competing models for the two-electron oxidation of quinol (QH{sub 2}) at the cytochrome bc{sub 1} complex and related complexes have different requirements for the reaction intermediate. At present, the intermediate species of the enzymatic oxidation process have not been observed or characterized, probably due to their transient nature. Here, we use a biomimetic oxidant, Ru(bpy){sub 2}(pbim)(PF6)2 (bpy = 2,2'-dipyridyl, pbim = 2-(2-benzimidazolate)pyridine) in an aprotic medium to probe the oxidation of the ubiquinol analogue, 2,3-dimethoxy-5-methyl-1,4-benzoquinol (UQH{sub 2}-0), an the plastoquinol analogue, trimethyl-1,4-benzoquinol (TMQH{sub 2}-0), using time-resolved and steady state spectroscopic techniques. This system qualitatively reproduces key features observed duringmore » ubiquinol oxidation by the mitochondrial cytochrome bc1 complex. Comparison of isotope dependent activation properties in the native and synthetic systems, as well as, analysis of the time-resolved direct-detection electron para magnetic resonance signals in the synthetic system allows us to conclude that: (1) the initial and rate-limiting step in quinol oxidation, both in the biological and biomimetic systems, involves electron and proton transfer, probably via a proton coupled electron transfer mechanism; (2) a neutral semiquinone intermediate is formed in the biomimetic system; and (3) oxidation of the QH*/QH{sub 2} couple for UQH{sub 2}-0, but not TMQH{sub 2}-0, exhibits a non-classical primary deuterium kinetic isotope effect on its Arrhenius activation energy ({Delta}G{sup TS}), where {Delta}G{sup TS} for the protiated form is larger than for the deuterated form. The same behavior is observed during steady state turnover of the cyt bc{sub 1} complex using ubiquinol, but not plastoquinol, as a substrate, leading to the conclusion that similar chemical pathways are involved in both systems. The synthetic system is an unambiguous n=1 electron acceptor and it is thus inferred that sequential oxidation of ubiquinol (by two sequential n=1 processes) is more rapid than a truly concerted (n=2) oxidation in the cyt bc{sub 1} complex.« less

On the physics of electron transfer (drift) in the substance: about the reason of “abnormal” fast transfer of electrons in the plasma of tokamak and at known Bohm’s diffusion

NASA Astrophysics Data System (ADS)

Boriev, I. A.

2018-03-01

An analysis of the problem of so-called “abnormal” fast transfer of electrons in tokamak plasma, which turned out much faster than the result of accepted calculation, is given. Such transfer of hot electrons leads to unexpectedly fast destruction of the inner tokamak wall with ejection of its matter in plasma volume, what violates a condition of plasma confinement for controlled thermonuclear fusion. It is shown, taking into account real physics of electron drift in the gas (plasma) and using the conservation law for momentum of electron transfer (drift), that the drift velocity of elastically scattered electrons should be significantly greater than that of accepted calculation. The reason is that the relaxation time of the momentum of electron transfer, to which the electron drift velocity is proportional, is significantly greater (from 16 up to 4 times) than the electron free path time. Therefore, generally accepted replacement of the relaxation time, which is unknown a priori, by the electron free path time, leads to significant (16 times for thermal electrons) underestimation of electron drift velocity (mobility). This result means, that transfer of elastically (and isotropically) scattered electrons in the gas phase should be so fast, and corresponds to multiplying coefficient (16), introduced by D. Bohm to explain the observed by him “abnormal” fast diffusion of electrons.

Marcus equation

DOE R&D Accomplishments Database

1998-09-21

In the late 1950s to early 1960s Rudolph A. Marcus developed a theory for treating the rates of outer-sphere electron-transfer reactions. Outer-sphere reactions are reactions in which an electron is transferred from a donor to an acceptor without any chemical bonds being made or broken. (Electron-transfer reactions in which bonds are made or broken are referred to as inner-sphere reactions.) Marcus derived several very useful expressions, one of which has come to be known as the Marcus cross-relation or, more simply, as the Marcus equation. It is widely used for correlating and predicting electron-transfer rates. For his contributions to the understanding of electron-transfer reactions, Marcus received the 1992 Nobel Prize in Chemistry. This paper discusses the development and use of the Marcus equation. Topics include self-exchange reactions; net electron-transfer reactions; Marcus cross-relation; and proton, hydride, atom and group transfers.

Coupled sensitizer-catalyst dyads: electron-transfer reactions in a perylene-polyoxometalate conjugate.

PubMed

Odobel, Fabrice; Séverac, Marjorie; Pellegrin, Yann; Blart, Errol; Fosse, Céline; Cannizzo, Caroline; Mayer, Cédric R; Elliott, Kristopher J; Harriman, Anthony

2009-01-01

Ultrafast discharge of a single-electron capacitor: A variety of intramolecular electron-transfer reactions are apparent for polyoxometalates functionalized with covalently attached perylene monoimide chromophores, but these are restricted to single-electron events. (et=electron transfer, cr=charge recombination, csr=charge-shift reaction, PER=perylene, POM=polyoxometalate).A new strategy is introduced that permits covalent attachment of an organic chromophore to a polyoxometalate (POM) cluster. Two examples are reported that differ according to the nature of the anchoring group and the flexibility of the linker. Both POMs are functionalized with perylene monoimide units, which function as photon collectors and form a relatively long-lived charge-transfer state under illumination. They are reduced to a stable pi-radical anion by electrolysis or to a protonated dianion under photolysis in the presence of aqueous triethanolamine. The presence of the POM opens up an intramolecular electron-transfer route by which the charge-transfer state reduces the POM. The rate of this process depends on the molecular conformation and appears to involve through-space interactions. Prior reduction of the POM leads to efficient fluorescence quenching, again due to intramolecular electron transfer. In most cases, it is difficult to resolve the electron-transfer products because of relatively fast reverse charge shift that occurs within a closed conformer. Although the POM can store multiple electrons, it has not proved possible to use these systems as molecular-scale capacitors because of efficient electron transfer from the one-electron-reduced POM to the excited singlet state of the perylene monoimide.

Unveiling the excited state energy transfer pathways in peridinin-chlorophyll a-protein by ultrafast multi-pulse transient absorption spectroscopy.

PubMed

Redeckas, Kipras; Voiciuk, Vladislava; Zigmantas, Donatas; Hiller, Roger G; Vengris, Mikas

2017-04-01

Time-resolved multi-pulse methods were applied to investigate the excited state dynamics, the interstate couplings, and the excited state energy transfer pathways between the light-harvesting pigments in peridinin-chlorophyll a-protein (PCP). The utilized pump-dump-probe techniques are based on perturbation of the regular PCP energy transfer pathway. The PCP complexes were initially excited with an ultrashort pulse, resonant to the S 0 →S 2 transition of the carotenoid peridinin. A portion of the peridinin-based emissive intramolecular charge transfer (ICT) state was then depopulated by applying an ultrashort NIR pulse that perturbed the interaction between S 1 and ICT states and the energy flow from the carotenoids to the chlorophylls. The presented data indicate that the peridinin S 1 and ICT states are spectrally distinct and coexist in an excited state equilibrium in the PCP complex. Moreover, numeric analysis of the experimental data asserts ICT→Chl-a as the main energy transfer pathway in the photoexcited PCP systems. Copyright © 2017 Elsevier B.V. All rights reserved.

On the Radiolysis of Ethylene Ices by Energetic Electrons and Implications to the Extraterrestrial Hydrocarbon Chemistry

NASA Astrophysics Data System (ADS)

Zhou, Li; Maity, Surajit; Abplanalp, Matt; Turner, Andrew; Kaiser, Ralf I.

2014-07-01

The chemical processing of ethylene ices (C2H4) by energetic electrons was investigated at 11 K to simulate the energy transfer processes and synthesis of new molecules induced by secondary electrons generated in the track of galactic cosmic ray particles. A combination of Fourier transform infrared spectrometry (solid state) and quadrupole mass spectrometry (gas phase) resulted in the identification of six hydrocarbon molecules: methane (CH4), the C2 species acetylene (C2H2), ethane (C2H6), the ethyl radical (C2H5), and—for the very first time in ethylene irradiation experiments—the C4 hydrocarbons 1-butene (C4H8) and n-butane (C4H10). By tracing the temporal evolution of the newly formed molecules spectroscopically online and in situ, we were also able to fit the kinetic profiles with a system of coupled differential equations, eventually providing mechanistic information, reaction pathways, and rate constants on the radiolysis of ethylene ices and the inherent formation of smaller (C1) and more complex (C2, C4) hydrocarbons involving carbon-hydrogen bond ruptures, atomic hydrogen addition processes, and radical-radical recombination pathways. We also discuss the implications of these results on the hydrocarbon chemistry on Titan's surface and on ice-coated, methane-bearing interstellar grains as present in cold molecular clouds such as TMC-1.

Chemical Constraints Governing the Origin of Metabolism: The Thermodynamic Landscape of Carbon Group Transformations

NASA Technical Reports Server (NTRS)

Weber, Arthur L.; Fonda, Mark (Technical Monitor)

2001-01-01

The thermodynamics of organic chemistry under mild aqueous conditions was examined in order to begin to understand its influence on the structure and operation of metabolism and its antecedents. Free energies were estimated for four types reactions of biochemical importance carbon-carbon bond cleavage and synthesis, hydrogen transfer between carbon groups, dehydration of alcohol groups, and aldo-keto isomerization. The energies were calculated for mainly aliphatic groups composed of carbon, hydrogen, and oxygen. The energy values showed that (1) when carbon-carbon bond cleavage involves two different types of functional groups, transfer of the shared electron-pair to the more reduced carbon group is energetically favored over transfer to the more oxidized carbon group, and (2) the energy of carbon-carbon bond transformation is strongly dependent on the type of functional group that donates the shared electron-pair during cleavage, and the group that accepts the shared electron-pair during synthesis, and (3) the energetics of C-C bond transformation is determined primarily by the half-reaction energies of the couples: carbonyl/carboxylic acid, carboxylic acid/carbon dioxide, alcohol/carbonyl, and hydrocarbon/alcohol. The energy of hydrogen-transfer between carbon groups was found to depend on the functional group class of both the hydrogen-donor and hydrogen-acceptor. From these and other observations we concluded that the chemistry of the origin of metabolism (and to a lesser degree modem metabolism) is strongly constrained by the (1) limited disproportionation energy of organic substrates that can be dissipated in a few irreversible reactions, (2) the energy-dominance of few half-reaction couples in carbon-carbon bond transformation that establishes whether a chemical reaction is energetically irreversible, reversible or unfeasible, and (3) the dependence of the transformation-energy on the oxidation state of carbon groups (functional group type) which is contingent on prior reactions in the synthetic pathway.

Neighbouring group processes in the deamination of protonated phenylalanine derivatives.

PubMed

Lioe, Hadi; O'Hair, Richard A J

2005-10-21

The gas-phase fragmentation of protonated phenylalanine and a series of its derivatives (tyrosine, 4-methylphenylalanine, 4-aminophenylalanine, 4-methoxyphenylalanine, 4-tert-butylphenylalanine, 4-fluorophenylalanine, 4-chlorophenylalanine, 4-bromophenylalanine, 4-iodophenylalanine, 4-cyanophenylalanine, 4-nitrophenylalanine, 3-fluorophenylalanine, and 3,4-dichlorophenylalanine) were examined using a combination of low energy CID in a quadrupole ion trap mass spectrometer as well as DFT calculations and RRKM modelling. In particular, the relationship between the electron-donating ability of the substituent and the competitive losses of H2O + CO and NH3 were explored through the application of the Hammett equation. It was found that electron-donating substituents promote the loss of NH3, while electron-withdrawing substituents suppress the loss of NH3 and favour the H2O + CO loss fragmentation channel instead. These observations are consistent with a neighbouring group pathway operating for the loss of NH3. Molecular orbital calculation (at the B3LYP/6-31+G(d,p) level of theory) were also performed for a range of derivatives to compare the relative transition state energy barriers for three competing mechanisms: (i) the combined loss of H2O + CO, which is triggered by an initial intramolecular proton transfer from the ammonium group to hydroxyl OH, followed by the combined loss of H2O and CO to form an immonium ion; (ii) loss of NH3 via an aryl assisted neighbouring group pathway to yield a phenonium ion; (iii) loss of NH3 via a 1,2-hydride migration process, which results in the formation of a benzyl cation. The relative energy barriers for H2O + CO loss remain nearly constant, while that for both NH3 pathways increase as the substituent moves from electron-donating to electron-withdrawing. The relative transition state energy for loss of NH3 via the aryl assisted neighbouring group pathway is always lower than that of the 1,2-hydride migration process. RRKM modelling of the DFT predicted barrier heights suggest that the rate constants for H2O + CO loss are insensitive to the substituent on the ring, while the NH3 loss channels are greatly affected by the substituent. These theoretical results are consistent with the experimental observation of the relative yields of the competing fragmentation channels. Finally, comparisons with published gas phase and condensed phase studies on related systems are made.

Chlorate reductase is cotranscribed with cytochrome c and other downstream genes in the gene cluster for chlorate respiration of Ideonella dechloratans.

PubMed

Hellberg Lindqvist, Miriam; Nilsson, Thomas; Sundin, Pontus; Rova, Maria

2015-03-01

The chlorate-respiring bacterium Ideonella dechloratans is a facultative anaerobe that can use both oxygen and chlorate as terminal electron acceptors. The genes for the enzymes chlorate reductase (clrABDC) and chlorite dismutase, necessary for chlorate metabolism and probably acquired by lateral gene transfer, are located in a gene cluster that also includes other genes potentially important for chlorate metabolism. Among those are a gene for cytochrome c (cyc) whose gene product may serve as an electron carrier during chlorate reduction, a cofactor biosynthesis gene (mobB) and a predicted transcriptional regulator (arsR). Only chlorate reductase and chlorite dismutase have been shown to be expressed in vivo. Here, we report the in vivo production of a single polycistronic transcript covering eight open reading frames including clrABDC, cyc, mobB and arsR. Transcription levels of the cyc and clrA genes were compared to each other by the use of qRT-PCR in RNA preparations from cells grown under aerobic or chlorate reducing anaerobic conditions. The two genes showed the same mRNA levels under both growth regimes, indicating that no transcription termination occurs between them. Higher transcription levels were observed at growth without external oxygen supply. Implications for electron pathway integration following lateral gene transfer are discussed. © FEMS 2015. All rights reserved. For permissions, please e-mail: journals.permissions@oup.com.

Electrocatalytic Mechanism Involving Michaelis-Menten Kinetics at the Preparative Scale: Theory and Applicability to Photocurrents from a Photosynthetic Algae Suspension With Quinones.

PubMed

Longatte, Guillaume; Guille-Collignon, Manon; Lemaître, Frédéric

2017-10-06

In the past years, many strategies have been implemented to benefit from oxygenic photosynthesis to harvest photosynthetic electrons and produce a significant photocurrent. Therefore, electrochemical tools were considered and have globally relied on the electron transfer(s) between the photosynthetic chain and a collecting electrode. In this context, we recently reported the implementation of an electrochemical set-up at the preparative scale to produce photocurrents from a Chlamydomonas reinhardtii algae suspension with an appropriate mediator (2,6-DCBQ) and a carbon gauze as the working electrode. In the present work, we wish to describe a mathematical modeling of the recorded photocurrents to better understand the effects of the experimental conditions on the photosynthetic extraction of electrons. In that way, we established a general model of an electrocatalytic mechanism at the preparative scale (that is, assuming a homogenous bulk solution at any time and a constant diffusion layer, both assumptions being valid under forced convection) in which the chemical step involves a Michaelis-Menten-like behaviour. Dependences of transient and steady-state corresponding currents were analysed as a function of different parameters by means of zone diagrams. This model was tested to our experimental data related to photosynthesis. The corresponding results suggest that competitive pathways beyond photosynthetic harvesting alone should be taken into account. © 2017 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.

Visualizing redox orbitals and their potentials in advanced lithium-ion battery materials using high-resolution x-ray Compton scattering

PubMed Central

Hafiz, Hasnain; Suzuki, Kosuke; Barbiellini, Bernardo; Orikasa, Yuki; Callewaert, Vincent; Kaprzyk, Staszek; Itou, Masayoshi; Yamamoto, Kentaro; Yamada, Ryota; Uchimoto, Yoshiharu; Sakurai, Yoshiharu; Sakurai, Hiroshi; Bansil, Arun

2017-01-01

Reduction-oxidation (redox) reactions are the key processes that underlie the batteries powering smartphones, laptops, and electric cars. A redox process involves transfer of electrons between two species. For example, in a lithium-ion battery, current is generated when conduction electrons from the lithium anode are transferred to the redox orbitals of the cathode material. The ability to visualize or image the redox orbitals and how these orbitals evolve under lithiation and delithiation processes is thus of great fundamental and practical interest for understanding the workings of battery materials. We show that inelastic scattering spectroscopy using high-energy x-ray photons (Compton scattering) can yield faithful momentum space images of the redox orbitals by considering lithium iron phosphate (LiFePO4 or LFP) as an exemplar cathode battery material. Our analysis reveals a new link between voltage and the localization of transition metal 3d orbitals and provides insight into the puzzling mechanism of potential shift and how it is connected to the modification of the bond between the transition metal and oxygen atoms. Our study thus opens a novel spectroscopic pathway for improving the performance of battery materials. PMID:28845452

Investigating the association between photosynthetic efficiency and generation of biophotoelectricity in autotrophic microbial fuel cells

PubMed Central

Ciniciato, Gustavo P. M. K.; Ng, Fong-Lee; Phang, Siew-Moi; Jaafar, Muhammad Musoddiq; Fisher, Adrian C.; Yunus, Kamran; Periasamy, Vengadesh

2016-01-01

Microbial fuel cells operating with autotrophic microorganisms are known as biophotovoltaic devices. It represents a great opportunity for environmentally-friendly power generation using the energy of the sunlight. The efficiency of electricity generation in this novel system is however low. This is partially reflected by the poor understanding of the bioelectrochemical mechanisms behind the electron transfer from these microorganisms to the electrode surface. In this work, we propose a combination of electrochemical and fluorescence techniques, giving emphasis to the pulse amplitude modulation fluorescence. The combination of these two techniques allow us to obtain information that can assist in understanding the electrical response obtained from the generation of electricity through the intrinsic properties related to the photosynthetic efficiency that can be obtained from the fluorescence emitted. These were achieved quantitatively by means of observed changes in four photosynthetic parameters with the bioanode generating electricity. These are the maximum quantum yield (Fv/Fm), alpha (α), light saturation coefficient (Ek) and maximum rate of electron transfer (rETRm). The relationship between the increases in the current density collected by the bioanode to the decrease of the rETRm values in the photosynthetic pathway for the two microorganisms was also discussed. PMID:27502051

Investigating the association between photosynthetic efficiency and generation of biophotoelectricity in autotrophic microbial fuel cells

NASA Astrophysics Data System (ADS)

Ciniciato, Gustavo P. M. K.; Ng, Fong-Lee; Phang, Siew-Moi; Jaafar, Muhammad Musoddiq; Fisher, Adrian C.; Yunus, Kamran; Periasamy, Vengadesh

2016-08-01

Microbial fuel cells operating with autotrophic microorganisms are known as biophotovoltaic devices. It represents a great opportunity for environmentally-friendly power generation using the energy of the sunlight. The efficiency of electricity generation in this novel system is however low. This is partially reflected by the poor understanding of the bioelectrochemical mechanisms behind the electron transfer from these microorganisms to the electrode surface. In this work, we propose a combination of electrochemical and fluorescence techniques, giving emphasis to the pulse amplitude modulation fluorescence. The combination of these two techniques allow us to obtain information that can assist in understanding the electrical response obtained from the generation of electricity through the intrinsic properties related to the photosynthetic efficiency that can be obtained from the fluorescence emitted. These were achieved quantitatively by means of observed changes in four photosynthetic parameters with the bioanode generating electricity. These are the maximum quantum yield (Fv/Fm), alpha (α), light saturation coefficient (Ek) and maximum rate of electron transfer (rETRm). The relationship between the increases in the current density collected by the bioanode to the decrease of the rETRm values in the photosynthetic pathway for the two microorganisms was also discussed.

Visualizing redox orbitals and their potentials in advanced lithium-ion battery materials using high-resolution x-ray Compton scattering.

PubMed

Hafiz, Hasnain; Suzuki, Kosuke; Barbiellini, Bernardo; Orikasa, Yuki; Callewaert, Vincent; Kaprzyk, Staszek; Itou, Masayoshi; Yamamoto, Kentaro; Yamada, Ryota; Uchimoto, Yoshiharu; Sakurai, Yoshiharu; Sakurai, Hiroshi; Bansil, Arun

2017-08-01

Reduction-oxidation (redox) reactions are the key processes that underlie the batteries powering smartphones, laptops, and electric cars. A redox process involves transfer of electrons between two species. For example, in a lithium-ion battery, current is generated when conduction electrons from the lithium anode are transferred to the redox orbitals of the cathode material. The ability to visualize or image the redox orbitals and how these orbitals evolve under lithiation and delithiation processes is thus of great fundamental and practical interest for understanding the workings of battery materials. We show that inelastic scattering spectroscopy using high-energy x-ray photons (Compton scattering) can yield faithful momentum space images of the redox orbitals by considering lithium iron phosphate (LiFePO 4 or LFP) as an exemplar cathode battery material. Our analysis reveals a new link between voltage and the localization of transition metal 3d orbitals and provides insight into the puzzling mechanism of potential shift and how it is connected to the modification of the bond between the transition metal and oxygen atoms. Our study thus opens a novel spectroscopic pathway for improving the performance of battery materials.

Thermal transfer structures coupling electronics card(s) to coolant-cooled structure(s)

DOEpatents

David, Milnes P; Graybill, David P; Iyengar, Madhusudan K; Kamath, Vinod; Kochuparambil, Bejoy J; Parida, Pritish R; Schmidt, Roger R

2014-12-16

Cooling apparatuses and coolant-cooled electronic systems are provided which include thermal transfer structures configured to engage with a spring force one or more electronics cards with docking of the electronics card(s) within a respective socket(s) of the electronic system. A thermal transfer structure of the cooling apparatus includes a thermal spreader having a first thermal conduction surface, and a thermally conductive spring assembly coupled to the conduction surface of the thermal spreader and positioned and configured to reside between and physically couple a first surface of an electronics card to the first surface of the thermal spreader with docking of the electronics card within a socket of the electronic system. The thermal transfer structure is, in one embodiment, metallurgically bonded to a coolant-cooled structure and facilitates transfer of heat from the electronics card to coolant flowing through the coolant-cooled structure.

Carbon-carbon bond activation of 2,2,6,6-tetramethyl-piperidine-1-oxyl by a Rh(II) metalloradical: a combined experimental and theoretical study.

PubMed

Chan, Kin Shing; Li, Xin Zhu; Dzik, Wojciech I; de Bruin, Bas

2008-02-13

Competitive major carbon-carbon bond activation (CCA) and minor carbon-hydrogen bond activation (CHA) channels are identified in the reaction between rhodium(II) meso-tetramesitylporphyrin [Rh(II)(tmp)] (1) and 2,2,6,6-tetramethyl-piperidine-1-oxyl (TEMPO) (2). The CCA and CHA pathways lead to formation of [Rh(III)(tmp)Me] (3) and [Rh(III)(tmp)H] (5), respectively. In the presence of excess TEMPO, [Rh(II)(tmp)] is regenerated from [Rh(III)(tmp)H] with formation of 2,2,6,6-tetramethyl-piperidine-1-ol (TEMPOH) (4) via a subsequent hydrogen atom abstraction pathway. The yield of the CCA product [Rh(III)(tmp)Me] increased with higher temperature at the cost of the CHA product TEMPOH in the temperature range 50-80 degrees C. Both the CCA and CHA pathways follow second-order kinetics. The mechanism of the TEMPO carbon-carbon bond activation was studied by means of kinetic investigations and DFT calculations. Broken symmetry, unrestricted b3-lyp calculations along the open-shell singlet surface reveal a low-energy transition state (TS1) for direct TEMPO methyl radical abstraction by the Rh(II) radical (SH2 type mechanism). An alternative ionic pathway, with a somewhat higher barrier, was identified along the closed-shell singlet surface. This ionic pathway proceeds in two sequential steps: Electron transfer from TEMPO to [Rh(II)(por)] producing the [TEMPO]+ [RhI(por)]- cation-anion pair, followed by net CH3+ transfer from TEMPO+ to Rh(I) with formation of [Rh(III)(por)Me] and (DMPO-like) 2,2,6-trimethyl-2,3,4,5-tetrahydro-1-pyridiniumolate. The transition state for this process (TS2) is best described as an SN2-like nucleophilic substitution involving attack of the d(z)2 orbital of [Rh(I)(por)]- at one of the C(Me)-C(ring) sigma* orbitals of [TEMPO]+. Although the calculated barrier of the open-shell radical pathway is somewhat lower than the barrier for the ionic pathway, R-DFT and U-DFT are not likely comparatively accurate enough to reliably distinguish between these possible pathways. Both the radical (SH2) and the ionic (SN2) pathway have barriers which are low enough to explain the experimental kinetic data.

Mitochondrial thiol oxidase Erv1: both shuttle cysteine residues are required for its function with distinct roles

PubMed Central

Ang, Swee Kim; Zhang, Mengqi; Lodi, Tiziana; Lu, Hui

2014-01-01

Erv1 (essential for respiration and viability 1), is an essential component of the MIA (mitochondrial import and assembly) pathway, playing an important role in the oxidative folding of mitochondrial intermembrane space proteins. In the MIA pathway, Mia40, a thiol oxidoreductase with a CPC motif at its active site, oxidizes newly imported substrate proteins. Erv1 a FAD-dependent thiol oxidase, in turn reoxidizes Mia40 via its N-terminal Cys30–Cys33 shuttle disulfide. However, it is unclear how the two shuttle cysteine residues of Erv1 relay electrons from the Mia40 CPC motif to the Erv1 active-site Cys130–Cys133 disulfide. In the present study, using yeast genetic approaches we showed that both shuttle cysteine residues of Erv1 are required for cell growth. In organelle and in vitro studies confirmed that both shuttle cysteine residues were indeed required for import of MIA pathway substrates and Erv1 enzyme function to oxidize Mia40. Furthermore, our results revealed that the two shuttle cysteine residues of Erv1 are functionally distinct. Although Cys33 is essential for forming the intermediate disulfide Cys33–Cys130′ and transferring electrons to the redox active-site directly, Cys30 plays two important roles: (i) dominantly interacts and receives electrons from the Mia40 CPC motif; and (ii) resolves the Erv1 Cys33–Cys130 intermediate disulfide. Taken together, we conclude that both shuttle cysteine residues are required for Erv1 function, and play complementary, but distinct, roles to ensure rapid turnover of active Erv1. PMID:24625320

Time-resolved luminescence measurements of the magnetic field effect on paramagnetic photosensitizers in photodynamic reactions

NASA Astrophysics Data System (ADS)

Mermut, O.; Bouchard, J.-P.; Cormier, J.-F.; Desroches, P.; Diamond, K. R.; Fortin, M.; Gallant, P.; Leclair, S.; Marois, J.-S.; Noiseux, I.; Morin, J.-F.; Patterson, M. S.; Vernon, M.

2008-02-01

The development of multimodal molecular probes and photosensitizing agents for use in photodynamic therapy (PDT) is vital for optimizing and monitoring cytotoxic responses. We propose a combinatorial approach utilizing photosensitizing molecules that are both paramagnetic and luminescent with multimodal functionality to perturb, control, and monitor molecular-scale reaction pathways in PDT. To this end, a time-domain single photon counting lifetime apparatus with a 400 nm excitation source has been developed and integrated with a variable low field magnet (0- 350mT). The luminescence lifetime decay function was measured in the presence of a sweeping magnetic field for a custom designed photosensitizing molecule in which photoinduced electron transfer was studied The photosensitizer studied was a donor-acceptor complex synthesized using a porphyrin linked to a fullerene molecule. The magneto-optic properties were investigated for the free-base photosensitizer complex as well as those containing either diamagnetic (paired electron) or paramagnetic (unpaired electron) metal centers, Zn(II) and Cu(II). The magnetic field was employed to affect and modify the spin states of radical pairs of the photosensitizing agents via magnetically induced hyperfine and Zeeman effects. Since the Type 1 reaction pathway of an excited triplet state photosensitizer involves the production of radical species, lifetime measurements were conducted at low dissolved oxygen concentration (0.01ppm) to elucidate the dependence of the magnetic perturbation on the photosensitization mechanistic pathway. To optimize the magnetic response, a solvent study was performed examining the dependence of the emission properties on the magnetic field in solutions of varying dielectric constants. Lastly, the cytotoxicity in murine tumor cell suspensions was investigated for the novel porphyrin-fullerene complex by inducing photodynamic treatments and determining the associated cell survival.

Potential electron mediators to extract electron energies of RBC glycolysis for prolonged in vivo functional lifetime of hemoglobin vesicles.

PubMed

Kettisen, Karin; Bülow, Leif; Sakai, Hiromi

2015-04-15

Developing a functional blood substitute as an alternative to donated blood for clinical use is believed to relieve present and future blood shortages, and to reduce the risks of infection and blood type mismatching. Hemoglobin vesicle (HbV) encapsulates a purified and concentrated human-derived Hb solution in a phospholipid vesicle (liposome). The in vivo safety and efficacy of HbV as a transfusion alternative have been clarified. Auto-oxidation of ferrous Hb in HbV gradually increases the level of ferric methemoglobin (metHb) and impairs the oxygen transport capabilities. The extension of the functional half-life of HbV has recently been proposed using an electron mediator, methylene blue (MB), which acts as a shuttle between red blood cells (RBC) and HbV. MB transfers electron energies of NAD(P)H, produced by RBC glycolysis, to metHb in HbV. Work presented here focuses on screening of 15 potential electron mediators, with appropriate redox potential and water solubility, for electron transfer from RBC to HbV. The results are assessed with regard to the chemical properties of the candidates. The compounds examined in this study were dimethyl methylene blue (DMB), methylene green, azure A, azure B, azure C, toluidine blue (TDB), thionin acetate, phenazine methosulfate, brilliant cresyl blue, cresyl violet, gallocyanine, toluylene blue, indigo carmine, indigotetrasulfonate, and MB. Six candidates were found to be unsuitable because of their insufficient diffusion across membranes, or overly high or nonexistent reactivity with relevant biomolecules. However, 9 displayed favorable metHb reduction. Among the suitable candidates, phenothiazines DMB and TDB exhibited effectiveness like MB did. In comparison to MB, they showed faster reduction by electron-donating NAD(P)H, coupled with showing a lower rate of reoxidation in the presence of molecular oxygen. Ascertaining the best electron mediator can provide a pathway for extending the lifetime and efficiency of potential blood substitutes.

EPR/ENDOR and Theoretical Study of the Jahn-Teller-Active [HIPTN3N]MoVL Complexes (L = N-, NH).

PubMed

Sharma, Ajay; Roemelt, Michael; Reithofer, Michael; Schrock, Richard R; Hoffman, Brian M; Neese, Frank

2017-06-19

The molybdenum trisamidoamine (TAA) complex [Mo] {[3,5-(2,4,6-i-Pr 3 C 6 H 2 ) 2 C 6 H 3 NCH 2 CH 2 N]Mo} carries out catalytic reduction of N 2 to ammonia (NH 3 ) by protons and electrons at room temperature. A key intermediate in the proposed [Mo] nitrogen reduction cycle is nitridomolybdenum(VI), [Mo(VI)]N. The addition of [e - /H + ] to [Mo(VI)]N to generate [Mo(V)]NH might, in principle, follow one of three possible pathways: direct proton-coupled electron transfer; H + first and then e - ; e - and then H + . In this study, the paramagnetic Mo(V) intermediate {[Mo]N} - and the [Mo]NH transfer product were generated by irradiating the diamagnetic [Mo]N and {[Mo]NH} + Mo(VI) complexes, respectively, with γ-rays at 77 K, and their electronic and geometric structures were characterized by electron paramagnetic resonance and electron nuclear double resonance spectroscopies, combined with quantum-chemical computations. In combination with previous X-ray studies, this creates the rare situation in which each one of the four possible states of [e - /H + ] delivery has been characterized. Because of the degeneracy of the electronic ground states of both {[Mo(V)]N} - and [Mo(V)]NH, only multireference-based methods such as the complete active-space self-consistent field (CASSCF) and related methods provide a qualitatively correct description of the electronic ground state and vibronic coupling. The molecular g values of {[Mo]N} - and [Mo]NH exhibit large deviations from the free-electron value g e . Their actual values reflect the relative strengths of vibronic and spin-orbit coupling. In the course of the computational treatment, the utility and limitations of a formal two-state model that describes this competition between couplings are illustrated, and the implications of our results for the chemical reactivity of these states are discussed.

Nonadiabatic excited-state molecular dynamics: modeling photophysics in organic conjugated materials.

PubMed

Nelson, Tammie; Fernandez-Alberti, Sebastian; Roitberg, Adrian E; Tretiak, Sergei

2014-04-15

To design functional photoactive materials for a variety of technological applications, researchers need to understand their electronic properties in detail and have ways to control their photoinduced pathways. When excited by photons of light, organic conjugated materials (OCMs) show dynamics that are often characterized by large nonadiabatic (NA) couplings between multiple excited states through a breakdown of the Born-Oppenheimer (BO) approximation. Following photoexcitation, various nonradiative intraband relaxation pathways can lead to a number of complex processes. Therefore, computational simulation of nonadiabatic molecular dynamics is an indispensable tool for understanding complex photoinduced processes such as internal conversion, energy transfer, charge separation, and spatial localization of excitons. Over the years, we have developed a nonadiabatic excited-state molecular dynamics (NA-ESMD) framework that efficiently and accurately describes photoinduced phenomena in extended conjugated molecular systems. We use the fewest-switches surface hopping (FSSH) algorithm to treat quantum transitions among multiple adiabatic excited state potential energy surfaces (PESs). Extended molecular systems often contain hundreds of atoms and involve large densities of excited states that participate in the photoinduced dynamics. We can achieve an accurate description of the multiple excited states using the configuration interaction single (CIS) formalism with a semiempirical model Hamiltonian. Analytical techniques allow the trajectory to be propagated "on the fly" using the complete set of NA coupling terms and remove computational bottlenecks in the evaluation of excited-state gradients and NA couplings. Furthermore, the use of state-specific gradients for propagation of nuclei on the native excited-state PES eliminates the need for simplifications such as the classical path approximation (CPA), which only uses ground-state gradients. Thus, the NA-ESMD methodology offers a computationally tractable route for simulating hundreds of atoms on ~10 ps time scales where multiple coupled excited states are involved. In this Account, we review recent developments in the NA-ESMD modeling of photoinduced dynamics in extended conjugated molecules involving multiple coupled electronic states. We have successfully applied the outlined NA-ESMD framework to study ultrafast conformational planarization in polyfluorenes where the rate of torsional relaxation can be controlled based on the initial excitation. With the addition of the state reassignment algorithm to identify instances of unavoided crossings between noninteracting PESs, NA-ESMD can now be used to study systems in which these so-called trivial unavoided crossings are expected to predominate. We employ this technique to analyze the energy transfer between poly(phenylene vinylene) (PPV) segments where conformational fluctuations give rise to numerous instances of unavoided crossings leading to multiple pathways and complex energy transfer dynamics that cannot be described using a simple Förster model. In addition, we have investigated the mechanism of ultrafast unidirectional energy transfer in dendrimers composed of poly(phenylene ethynylene) (PPE) chromophores and have demonstrated that differential nuclear motion favors downhill energy transfer in dendrimers. The use of native excited-state gradients allows us to observe this feature.

Single Molecule Spectroelectrochemistry of Interfacial Charge Transfer Dynamics In Hybrid Organic Solar Cell

DOE Office of Scientific and Technical Information (OSTI.GOV)

Pan, Shanlin

2014-11-16

Our research under support of this DOE grant is focused on applied and fundamental aspects of model organic solar cell systems. Major accomplishments are: 1) we developed a spectroelectorchemistry technique of single molecule single nanoparticle method to study charge transfer between conjugated polymers and semiconductor at the single molecule level. The fluorescence of individual fluorescent polymers at semiconductor surfaces was shown to exhibit blinking behavior compared to molecules on glass substrates. Single molecule fluorescence excitation anisotropy measurements showed the conformation of the polymer molecules did not differ appreciably between glass and semiconductor substrates. The similarities in molecular conformation suggest thatmore » the observed differences in blinking activity are due to charge transfer between fluorescent polymer and semiconductor, which provides additional pathways between states of high and low fluorescence quantum efficiency. Similar spectroelectrochemistry work has been done for small organic dyes for understand their charge transfer dynamics on various substrates and electrochemical environments; 2) We developed a method of transferring semiconductor nanoparticles (NPs) and graphene oxide (GO) nanosheets into organic solvent for a potential electron acceptor in bulk heterojunction organic solar cells which employed polymer semiconductor as the electron donor. Electron transfer from the polymer semiconductor to semiconductor and GO in solutions and thin films was established through fluorescence spectroscopy and electroluminescence measurements. Solar cells containing these materials were constructed and evaluated using transient absorption spectroscopy and dynamic fluorescence techniques to understand the charge carrier generation and recombination events; 3) We invented a spectroelectorchemistry technique using light scattering and electroluminescence for rapid size determination and studying electrochemistry of single NPs in an electrochemical cell. For example, we are able to use this technique to track electroluminescence of single Au NPs, and the electrodeposition of individual Ag NPs in-situ. These metallic NPs are useful to enhance light harvesting in organic photovoltaic systems. The scattering at the surface of an indium tin oxide (ITO) working electrode was measured during a potential sweep. Utilizing Mie scattering theory and high resolution scanning electron microscopy (SEM), the scattering data were used to calculate current-potential curves depicting the electrodeposition of individual Ag NPs. The oxidation of individual presynthesized and electrodeposited Ag NPs was also investigated using fluorescence and DFS microscopies. Our work has produced 1 US provisional patent, 15 published manuscripts, 1 submitted and two additional in-writing manuscripts. 5 graduate students, 1 postdoctoral student, 1 visiting professor, and two undergraduate students have received research training in the area of electrochemistry and optical spectroscopy under support of this award.« less