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Journal articles on the topic 'Biology - Electron Transfer'

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Author: Grafiati
Published: 7 September 2023

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1

Williams, R. J. P. "Electron transfer in biology." Molecular Physics 68, no. 1 (September 1, 1989): 1–23. http://dx.doi.org/10.1080/00268978900101931.

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2

Sledow, James N., and Ann L. Umbach. "Plant Mitochondrial Electron Transfer and Molecular Biology." Plant Cell 7, no. 7 (July 1995): 821. http://dx.doi.org/10.2307/3870039.

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3

Agapakis, Christina M., and Pamela A. Silver. "Modular electron transfer circuits for synthetic biology." Bioengineered Bugs 1, no. 6 (November 2010): 413–18. http://dx.doi.org/10.4161/bbug.1.6.12462.

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4

Matyushov, Dmitry V. "Protein electron transfer: is biology (thermo)dynamic?" Journal of Physics: Condensed Matter 27, no. 47 (November 12, 2015): 473001. http://dx.doi.org/10.1088/0953-8984/27/47/473001.

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5

Blankenship, Robert E. "Protein electron transfer." FEBS Letters 398, no. 2-3 (December 2, 1996): 339. http://dx.doi.org/10.1016/0014-5793(97)81275-6.

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6

Moser, Christopher C., Christopher C. Page, Ramy Farid, and P. Leslie Dutton. "Biological electron transfer." Journal of Bioenergetics and Biomembranes 27, no. 3 (June 1995): 263–74. http://dx.doi.org/10.1007/bf02110096.

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7

Rivas, Maria Gabriela, Pablo Javier Gonzalez, Felix Martin Ferroni, Alberto Claudio Rizzi, and Carlos Brondino. "Studying Electron Transfer Pathways in Oxidoreductases." Science Reviews - from the end of the world 1, no. 2 (March 16, 2020): 6–23. http://dx.doi.org/10.52712/sciencereviews.v1i2.15.

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Oxidoreductases containing transition metal ions are widespread in nature and are essential for living organisms. The copper-containing nitrite reductase (NirK) and the molybdenum-containing aldehyde oxidoreductase (Aor) are typical examples of oxidoreductases. Metal ions in these enzymes are present either as mononuclear centers or organized into clusters and accomplish two main roles. One of them is to be the active site where the substrate is converted into product, and the other one is to serve as electron transfer center. Both enzymes transiently bind the substrate and an external electron donor/acceptor in NirK/Aor, respectively, at distinct protein points for them to exchange the electrons involved in the redox reaction. Electron exchange occurs through a specific intra-protein chemical pathway that connects the different enzyme metal cofactors. Based on the two oxidoreductases presented here, we describe how the different actors involved in the intra-protein electron transfer process can be characterized and studied employing molecular biology, spectroscopic, electrochemical, and structural techniques.
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8

Parsons, Roger. "Electron transfer in biology and the solid state." Journal of Electroanalytical Chemistry and Interfacial Electrochemistry 305, no. 1 (April 1991): 166. http://dx.doi.org/10.1016/0022-0728(91)85214-a.

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9

Berg, Hermann. "Electron and Proton Transfer in Chemistry and Biology." Bioelectrochemistry and Bioenergetics 32, no. 1 (September 1993): 97–98. http://dx.doi.org/10.1016/0302-4598(93)80027-r.

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10

Holtzhauer, Martin, and Peter Mohr. "Electron and Proton Transfer in Chemistry and Biology." Zeitschrift für Physikalische Chemie 186, Part_1 (January 1994): 119. http://dx.doi.org/10.1524/zpch.1994.186.part_1.119.

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11

Fischer-Hjalmars, I., H. Holmgren, and A. Henriksson-Enflo. "Metals in biology: Iron complexes modeling electron transfer." International Journal of Quantum Chemistry 28, S12 (June 19, 2009): 57–67. http://dx.doi.org/10.1002/qua.560280708.

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12

Farid, Ramy S., Christopher C. Moser, and P. Leslie Dutton. "Electron transfer in proteins." Current Opinion in Structural Biology 3, no. 2 (April 1993): 225–33. http://dx.doi.org/10.1016/s0959-440x(05)80157-5.

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13

Canters, Gerard W., and Mart van de Kamp. "Protein-mediated electron transfer." Current Opinion in Structural Biology 2, no. 6 (January 1992): 859–69. http://dx.doi.org/10.1016/0959-440x(92)90112-k.

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14

Mathews, F. Scott, and Scott White. "Electron transfer proteins/enzymes." Current Opinion in Structural Biology 3, no. 6 (January 1993): 902–11. http://dx.doi.org/10.1016/0959-440x(93)90154-d.

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15

PANG, XIAO-FENG. "THE MECHANISM AND PROPERTIES OF ELECTRON TRANSFER IN THE BIOLOGICAL ORGANISM." International Journal of Modern Physics B 27, no. 21 (July 30, 2013): 1350090. http://dx.doi.org/10.1142/s0217979213500902.

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The mechanism and properties of electron transfer along protein molecules at finite temperature T ≠ 0 in the life systems are studied using nonlinear theory of bio-energy transport and Green function method, in which the electrons are transferred from donors to acceptors in virtue of the supersound soliton excited by the energy released in ATP hydrolysis. The electron transfer is, in essence, a process of oxidation–reduction reaction. In this study we first give the Hamiltonian and wavefunction of the system and find out the soliton solution of the dynamical equation in the protein molecules with finite temperature, and obtain the dynamical coefficient of the electron transfer. The results show that the speed of the electron transfer is related to the velocity of motion of the soliton, distribution of electrons in the donor and acceptor as well as the interaction strength among them. We finally concluded the changed rule of electric current, arising from the electron transfer, with increasing time. These results are useful in molecular and chemical biology.
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16

Gon, Stéphanie, Marie-Thérèse Giudici-Orticoni, Vincent Méjean, and Chantal Iobbi-Nivol. "Electron Transfer and Binding of thec-Type Cytochrome TorC to the TrimethylamineN-Oxide Reductase inEscherichia coli." Journal of Biological Chemistry 276, no. 15 (October 30, 2000): 11545–51. http://dx.doi.org/10.1074/jbc.m008875200.

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Reduction of trimethylamineN-oxide (E′0(TMAO/TMA)= +130 mV) inEscherichia coliis carried out by the Tor system, an electron transfer chain encoded by thetorCADoperon and made up of the periplasmic terminal reductase TorA and the membrane-anchored pentahemicc-type cytochrome TorC. Although the role of TorA in the reduction of trimethylamineN-oxide (TMAO) has been clearly established, no direct evidence for TorC involvement has been presented. TorC belongs to the NirT/NapCc-type cytochrome family based on homologies of its N-terminal tetrahemic domain (TorCN) to the cytochromes of this family, but TorC contains a C-terminal extension (TorCC) with an additional heme-binding site. In this study, we show that both domains are required for the anaerobic bacterial growth with TMAO. The intact TorC protein and its two domains, TorCNand TorCC, were produced independently and purified for a biochemical characterization. The reduced form of TorC exhibited visible absorption maxima at 552, 523, and 417 nm. Mediated redox potentiometry of the heme centers of the purified components identified two negative midpoint potentials (−177 and −98 mV) localized in the tetrahemic TorCNand one positive midpoint potential (+120 mV) in the monohemic TorCC. In agreement with these values, thein vitroreconstitution of electron transfer between TorC, TorCN, or TorCCand TorA showed that only TorC and TorCCwere capable of electron transfer to TorA. Surprisingly, interaction studies revealed that only TorC and TorCNstrongly bind TorA. Therefore, TorCCdirectly transfers electrons to TorA, whereas TorCN, which probably receives electrons from the menaquinone pool, is involved in both the electron transfer to TorCCand the binding to TorA.
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17

Bellelli, Andrea, Maurizio Brunori, Peter Brzezinski, and Michael T. Wilson. "Photochemically Induced Electron Transfer." Methods 24, no. 2 (June 2001): 139–52. http://dx.doi.org/10.1006/meth.2001.1175.

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18

Anderson, Robert F., Russ Hille, Sujata S. Shinde, and Gary Cecchini. "Electron Transfer within Complex II." Journal of Biological Chemistry 280, no. 39 (August 5, 2005): 33331–37. http://dx.doi.org/10.1074/jbc.m506002200.

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19

Farver, Ole, Scot Wherland, Olga Koroleva, Dmitry S. Loginov, and Israel Pecht. "Intramolecular electron transfer in laccases." FEBS Journal 278, no. 18 (August 31, 2011): 3463–71. http://dx.doi.org/10.1111/j.1742-4658.2011.08268.x.

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20

Schuergers, N., C. Werlang, C. M. Ajo-Franklin, and A. A. Boghossian. "A synthetic biology approach to engineering living photovoltaics." Energy & Environmental Science 10, no. 5 (2017): 1102–15. http://dx.doi.org/10.1039/c7ee00282c.

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21

Nohl, Hans, Werner Jordan, and Richard J. Youngman. "Quinones in Biology: Functions in electron transfer and oxygen activation." Advances in Free Radical Biology & Medicine 2, no. 1 (January 1986): 211–79. http://dx.doi.org/10.1016/s8755-9668(86)80030-8.

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22

Sutcliffe, Michael J., Kamaldeep K. Chohan, and Nigel S. Scrutton. "Major Structural Reorganisation Most Likely Accompanies the Transient Formation of a Physiological Electron Transfer Complex." Protein & Peptide Letters 5, no. 4 (August 1998): 231–36. http://dx.doi.org/10.2174/092986650504221111114610.

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Abstract: Modelling studies coupled with experimental observations show that the transfer of electrons from trimethylamine dehydrogenase to its electron transferring flavoprotein (ETF) requires a large quaternary change in ETF. These studies describe for the first time how complex and substantial changes in quaternary structure could control interprotein electron transfer reactions, and direct electrons onto specific and ntended redox partners.
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23

Medzihradszky, K. F., S. Guan, D. A. Maltby, and A. L. Burlingame. "Sulfopeptide fragmentation in electron-capture and electron-transfer dissociation." Journal of the American Society for Mass Spectrometry 18, no. 9 (September 2007): 1617–24. http://dx.doi.org/10.1016/j.jasms.2007.06.002.

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24

Xu, Wu, Parag Chitnis, Alfia Valieva, Art van der Est, Yulia N. Pushkar, Maciej Krzystyniak, Christian Teutloff, et al. "Electron Transfer in Cyanobacterial Photosystem I." Journal of Biological Chemistry 278, no. 30 (April 29, 2003): 27864–75. http://dx.doi.org/10.1074/jbc.m302962200.

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25

Xu, Wu, Parag R. Chitnis, Alfia Valieva, Art van der Est, Klaus Brettel, Mariana Guergova-Kuras, Yulia N. Pushkar, et al. "Electron Transfer in Cyanobacterial Photosystem I." Journal of Biological Chemistry 278, no. 30 (April 29, 2003): 27876–87. http://dx.doi.org/10.1074/jbc.m302965200.

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26

Kiger, Laurent, and Michael C. Marden. "Electron Transfer Kinetics between Hemoglobin Subunits." Journal of Biological Chemistry 276, no. 51 (October 15, 2001): 47937–43. http://dx.doi.org/10.1074/jbc.m106807200.

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27

Paquete, Catarina M., Ivo H. Saraiva, Eduardo Calçada, and Ricardo O. Louro. "Molecular Basis for Directional Electron Transfer." Journal of Biological Chemistry 285, no. 14 (January 20, 2010): 10370–75. http://dx.doi.org/10.1074/jbc.m109.078337.

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28

Blank, Martin, and Lily Soo. "Electromagnetic acceleration of electron transfer reactions." Journal of Cellular Biochemistry 81, no. 2 (2001): 278–83. http://dx.doi.org/10.1002/1097-4644(20010501)81:2<278::aid-jcb1042>3.0.co;2-f.

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29

Brettel, Klaus, and Winfried Leibl. "Electron transfer in photosystem I." Biochimica et Biophysica Acta (BBA) - Bioenergetics 1507, no. 1-3 (October 2001): 100–114. http://dx.doi.org/10.1016/s0005-2728(01)00202-x.

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30

Palmer, Graham, and Jan Reedijk. "Nonmenclature of electron-transfer proteins." Biochimica et Biophysica Acta (BBA) - Bioenergetics 1060, no. 3 (November 1991): vii—xix. http://dx.doi.org/10.1016/s0005-2728(05)80311-1.

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31

Keltjens, J. T., and C. Drift. "Electron transfer reactions in methanogens." FEMS Microbiology Letters 39, no. 3 (August 1986): 259–303. http://dx.doi.org/10.1111/j.1574-6968.1986.tb01862.x.

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32

Murgida, Daniel Horacio. "Modulation of Functional Features in Electron Transferring Metalloproteins." Science Reviews - from the end of the world 1, no. 2 (March 16, 2020): 45–65. http://dx.doi.org/10.52712/sciencereviews.v1i2.18.

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Electron transferring metalloproteins are typically implicated in shuttling electrons between energy transduction chains membrane complexes, such as in (aerobic and anaerobic) respiration and photosynthesis, among other functions. The thermodynamic and kinetic electron transfer parameters of the different metalloproteins need to be adjusted in each case to the specific demands, which can be quite diverse among organisms. Notably, biology utilizes very few metals, essentially iron and copper, to cover this broad range of redox needs imposed by biodiversity. Here, I will describe some crucial structural and dynamical characteristics that modulate the electron transfer parameters (and alternative functions) of two prototypical metalloproteins: the iron protein cytochrome c and its redox partner, the CuA center of the terminal respiratory enzyme cytochrome c oxidase. Specifically, I will focus on summarizing results obtained in recent years in my laboratory.
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33

Rich, P. R. "The osmochemistry of electron-transfer complexes." Bioscience Reports 11, no. 6 (December 1, 1991): 539–71. http://dx.doi.org/10.1007/bf01130217.

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Detailed molecular mechanisms of electron transfer-driven translocation of ions and of the generation of electric fields across biological membranes are beginning to emerge. The ideas inherent in the early formulations of the chemiosmotic hypothesis have provided the framework for this understanding and have also been seminal in promoting many of the experimental approaches which have been successfully used. This article is an attempt to review present understanding of the structures and mechanisms of several osmoenzymes of central importance and to identify and define the underlying features which might be of general relevance to the study of chemiosmotic devices.
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34

Craven, Galen T., and Abraham Nitzan. "Electron transfer across a thermal gradient." Proceedings of the National Academy of Sciences 113, no. 34 (July 22, 2016): 9421–29. http://dx.doi.org/10.1073/pnas.1609141113.

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Charge transfer is a fundamental process that underlies a multitude of phenomena in chemistry and biology. Recent advances in observing and manipulating charge and heat transport at the nanoscale, and recently developed techniques for monitoring temperature at high temporal and spatial resolution, imply the need for considering electron transfer across thermal gradients. Here, a theory is developed for the rate of electron transfer and the associated heat transport between donor–acceptor pairs located at sites of different temperatures. To this end, through application of a generalized multidimensional transition state theory, the traditional Arrhenius picture of activation energy as a single point on a free energy surface is replaced with a bithermal property that is derived from statistical weighting over all configurations where the reactant and product states are equienergetic. The flow of energy associated with the electron transfer process is also examined, leading to relations between the rate of heat exchange among the donor and acceptor sites as functions of the temperature difference and the electronic driving bias. In particular, we find that an open electron transfer channel contributes to enhanced heat transport between sites even when they are in electronic equilibrium. The presented results provide a unified theory for charge transport and the associated heat conduction between sites at different temperatures.
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35

van Wonderen, Jessica H., Katrin Adamczyk, Xiaojing Wu, Xiuyun Jiang, Samuel E. H. Piper, Christopher R. Hall, Marcus J. Edwards, et al. "Nanosecond heme-to-heme electron transfer rates in a multiheme cytochrome nanowire reported by a spectrally unique His/Met-ligated heme." Proceedings of the National Academy of Sciences 118, no. 39 (September 23, 2021): e2107939118. http://dx.doi.org/10.1073/pnas.2107939118.

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Proteins achieve efficient energy storage and conversion through electron transfer along a series of redox cofactors. Multiheme cytochromes are notable examples. These proteins transfer electrons over distance scales of several nanometers to >10 μm and in so doing they couple cellular metabolism with extracellular redox partners including electrodes. Here, we report pump-probe spectroscopy that provides a direct measure of the intrinsic rates of heme–heme electron transfer in this fascinating class of proteins. Our study took advantage of a spectrally unique His/Met-ligated heme introduced at a defined site within the decaheme extracellular MtrC protein of Shewanella oneidensis. We observed rates of heme-to-heme electron transfer on the order of 109 s−1 (3.7 to 4.3 Å edge-to-edge distance), in good agreement with predictions based on density functional and molecular dynamics calculations. These rates are among the highest reported for ground-state electron transfer in biology. Yet, some fall 2 to 3 orders of magnitude below the Moser–Dutton ruler because electron transfer at these short distances is through space and therefore associated with a higher tunneling barrier than the through-protein tunneling scenario that is usual at longer distances. Moreover, we show that the His/Met-ligated heme creates an electron sink that stabilizes the charge separated state on the 100-μs time scale. This feature could be exploited in future designs of multiheme cytochromes as components of versatile photosynthetic biohybrid assemblies.
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36

Murataliev, Marat B., René Feyereisen, and F. Ann Walker. "Electron transfer by diflavin reductases." Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 1698, no. 1 (April 2004): 1–26. http://dx.doi.org/10.1016/j.bbapap.2003.10.003.

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37

Lin, Tzong-Yuan, Tobias Werther, Jae-Hun Jeoung, and Holger Dobbek. "Suppression of Electron Transfer to Dioxygen by Charge Transfer and Electron Transfer Complexes in the FAD-dependent Reductase Component of Toluene Dioxygenase." Journal of Biological Chemistry 287, no. 45 (September 19, 2012): 38338–46. http://dx.doi.org/10.1074/jbc.m112.374918.

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38

Jeng, Mei-Fen, S. Walter Englander, Kelli Pardue, Jill Short Rogalskyj, and George McLendon. "Structural dynamics in an electron–transfer complex." Nature Structural & Molecular Biology 1, no. 4 (April 1994): 234–38. http://dx.doi.org/10.1038/nsb0494-234.

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39

DiMagno, Theodore J., Zhiyu Wang, and James R. Norris. "Initial electron-transfer events in photosynthetic bacteria." Current Opinion in Structural Biology 2, no. 6 (January 1992): 836–42. http://dx.doi.org/10.1016/0959-440x(92)90108-j.

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40

Farooq, Yassar, and Gordon C. K. Roberts. "Kinetics of electron transfer between NADPH-cytochrome P450 reductase and cytochrome P450 3A4." Biochemical Journal 432, no. 3 (November 25, 2010): 485–94. http://dx.doi.org/10.1042/bj20100744.

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We have incorporated CYP3A4 (cytochrome P450 3A4) and CPR (NADPH-cytochrome P450 reductase) into liposomes with a high lipid/protein ratio by an improved method. In the purified proteoliposomes, CYP3A4 binds testosterone with Kd (app)=36±6 μM and Hill coefficient=1.5±0.3, and 75±4% of the CYP3A4 can be reduced by NADPH in the presence of testosterone. Transfer of the first electron from CPR to CYP3A4 was measured by stopped-flow, trapping the reduced CYP3A4 as its Fe(II)–CO complex and measuring the characteristic absorbance change. Rapid electron transfer is observed in the presence of testosterone, with the fast phase, representing 90% of the total absorbance change, having a rate of 14±2 s−1. Measurements of the first electron transfer were performed at various molar ratios of CPR/CYP3A4 in proteoliposomes; the rate was unaffected, consistent with a model in which first electron transfer takes place within a relatively stable CPR–CYP3A4 complex. Steady-state rates of NADPH oxidation and of 6β-hydroxytestosterone formation were also measured as a function of the molar ratio of CPR/CYP3A4 in the proteoliposomes. These rates increased with increasing CPR/CYP3A4 ratio, showing a hyperbolic dependency indicating a Kd (app) of ~0.4 μM. This suggests that the CPR–CYP3A4 complex can dissociate and reform between the first and second electron transfers.
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41

Bjerrum, Morten J., Danilo R. Casimiro, I. Jy Chang, Angel J. Di Bilio, Harry B. Gray, Michael G. Hill, Ralf Langen, et al. "Electron transfer in ruthenium-modified proteins." Journal of Bioenergetics and Biomembranes 27, no. 3 (June 1995): 295–302. http://dx.doi.org/10.1007/bf02110099.

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42

Coon, Joshua J., Jeffrey Shabanowitz, Donald F. Hunt, and John E. P. Syka. "Electron transfer dissociation of peptide anions." Journal of the American Society for Mass Spectrometry 16, no. 6 (June 2005): 880–82. http://dx.doi.org/10.1016/j.jasms.2005.01.015.

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43

Han, Liang, and Catherine E. Costello. "Electron Transfer Dissociation of Milk Oligosaccharides." Journal of The American Society for Mass Spectrometry 22, no. 6 (April 14, 2011): 997–1013. http://dx.doi.org/10.1007/s13361-011-0117-9.

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44

Li, Xiaojuan, Cheng Lin, Liang Han, Catherine E. Costello, and Peter B. O’Connor. "Charge remote fragmentation in electron capture and electron transfer dissociation." Journal of the American Society for Mass Spectrometry 21, no. 4 (April 2010): 646–56. http://dx.doi.org/10.1016/j.jasms.2010.01.001.

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45

Guberman-Pfeffer, Matthew J., and Nikhil S. Malvankar. "Making protons tag along with electrons." Biochemical Journal 478, no. 23 (December 6, 2021): 4093–97. http://dx.doi.org/10.1042/bcj20210592.

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Every living cell needs to get rid of leftover electrons when metabolism extracts energy through the oxidation of nutrients. Common soil microbes such as Geobacter sulfurreducens live in harsh environments that do not afford the luxury of soluble, ingestible electron acceptors like oxygen. Instead of resorting to fermentation, which requires the export of reduced compounds (e.g. ethanol or lactate derived from pyruvate) from the cell, these organisms have evolved a means to anaerobically respire by using nanowires to export electrons to extracellular acceptors in a process called extracellular electron transfer (EET) [ 1]. Since 2005, these nanowires were thought to be pili filaments [ 2]. But recent studies have revealed that nanowires are composed of multiheme cytochromes OmcS [ 3, 4] and OmcZ [ 5] whereas pili remain inside the cell during EET and are required for the secretion of nanowires [ 6]. However, how electrons are passed to these nanowires remains a mystery ( Figure 1A). Periplasmic cytochromes (Ppc) called PpcA-E could be doing the job, but only two of them (PpcA and PpcD) can couple electron/proton transfer — a necessary condition for energy generation. In a recent study, Salgueiro and co-workers selectively replaced an aromatic with an aliphatic residue to couple electron/proton transfer in PpcB and PpcE (Biochem. J. 2021, 478 (14): 2871–2887). This significant in vitro success of their protein engineering strategy may enable the optimization of bioenergetic machinery for bioenergy, biofuels, and bioelectronics applications.
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46

HUBER, Robert. "A structural basis of light energy and electron transfer in biology." European Journal of Biochemistry 187, no. 2 (January 1990): 283–305. http://dx.doi.org/10.1111/j.1432-1033.1990.tb15305.x.

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47

Krishnan, V. "Electron transfer in chemistry and biology — The primary events in photosynthesis." Resonance 16, no. 12 (December 2011): 1201–10. http://dx.doi.org/10.1007/s12045-011-0135-8.

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48

Krishnan, V. "Electron transfer in chemistry and biology — The primary events in photosynthesis." Resonance 2, no. 12 (December 1997): 77–86. http://dx.doi.org/10.1007/bf02836909.

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49

Cho, Seung-Hyun, and Jon Beckwith. "Mutations of the Membrane-Bound Disulfide Reductase DsbD That Block Electron Transfer Steps from Cytoplasm to Periplasm in Escherichia coli." Journal of Bacteriology 188, no. 14 (July 15, 2006): 5066–76. http://dx.doi.org/10.1128/jb.00368-06.

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ABSTRACT The cytoplasmic membrane protein DsbD keeps the periplasmic disulfide isomerase DsbC reduced, using the cytoplasmic reducing power of thioredoxin. DsbD contains three domains, each containing two reactive cysteines. One membrane-embedded domain, DsbDβ, transfers electrons from thioredoxin to the carboxy-terminal thioredoxin-like periplasmic domain DsbDγ. To evaluate the role of conserved amino acid residues in DsbDβ in the electron transfer process, we substituted alanines for each of 19 conserved amino acid residues and assessed the in vivo redox states of DsbC and DsbD. The mutant DsbDs of 11 mutants which caused defects in DsbC reduction showed relatively oxidized redox states. To analyze the redox state of each DsbD domain, we constructed a thrombin-cleavable DsbD (DsbDTH) from which we could generate all three domains as separate polypeptide chains by thrombin treatment in vitro. We divided the mutants with strong defects into two classes. The first mutant class consists of mutant DsbDβ proteins that cannot receive electrons from cytoplasmic thioredoxin, resulting in a DsbD that has all six of its cysteines disulfide bonded. The second mutant class represents proteins in which the transfer of electrons from DsbDβ to DsbDγ appears to be blocked. This class includes the mutant with the most clear-cut defect, P284A. We relate the properties of the mutants to the positions of the amino acids in the structure of DsbD and discuss mechanisms that would interfere with the electron transfer process.
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50

Kuznetsov, Vadim Yu, Emek Blair, Patrick J. Farmer, Thomas L. Poulos, Amanda Pifferitti, and Irina F. Sevrioukova. "The Putidaredoxin Reductase-Putidaredoxin Electron Transfer Complex." Journal of Biological Chemistry 280, no. 16 (February 15, 2005): 16135–42. http://dx.doi.org/10.1074/jbc.m500771200.

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Abstract:
Interaction and electron transfer between putidaredoxin reductase (Pdr) and putidaredoxin (Pdx) fromPseudomonas putidawas studied by molecular modeling, mutagenesis, and stopped flow techniques. Based on the crystal structures of Pdr and Pdx, a complex between the proteins was generated using computer graphics methods. In the model, Pdx is docked above the isoalloxazine ring of FAD of Pdr with the distance between the flavin and [2Fe-2S] of 14.6 Å. This mode of interaction allows Pdx to easily adjust and optimize orientation of its cofactor relative to Pdr. The key residues of Pdx located at the center, Asp38and Trp106, and at the edge of the protein-protein interface, Tyr33and Arg66, were mutated to test the Pdr-Pdx computer model. The Y33F, Y33A, D38N, D38A, R66A, R66E, W106F, W106A, and Δ106 mutations did not affect assembly of the [2Fe-2S] cluster and resulted in a marginal change in the redox potential of Pdx. The electron-accepting ability of Δ106 Pdx was similar to that of the wild-type protein, whereas electron transfer rates from Pdr to other mutants were diminished to various degrees with the smallest and largest effects on the kinetic parameters of the Pdr-to-Pdx electron transfer reaction caused by the Trp106and Tyr33/Arg66substitutions, respectively. Compared with wild-type Pdx, the binding affinity of all studied mutants to Pdr was significantly higher. Experimental results were in agreement with theoretical predictions and suggest that: (i) Pdr-Pdx complex formation is mainly driven by steric complementarity, (ii) bulky side chains of Tyr33, Arg66, and Trp106prevent tight binding of oxidized Pdx and facilitate dissociation of the reduced iron-sulfur protein from Pdr, and (iii) transfer of an electron from FAD to [2Fe-2S] can occur with various orientations between the cofactors through multiple electron transfer pathways that do not involve Trp106but are likely to include Asp38and Cys39.
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