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Journal articles on the topic 'Biology - Electron Transfer'

Author: Grafiati

Published: 7 September 2023

Last updated: 31 July 2025

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1

Williams, R. J. P. "Electron transfer in biology." Molecular Physics 68, no. 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 (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 (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 (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 (1996): 339. http://dx.doi.org/10.1016/0014-5793(97)81275-6.

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6

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 (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 electro

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7

PANG, XIAO-FENG. "THE MECHANISM AND PROPERTIES OF ELECTRON TRANSFER IN THE BIOLOGICAL ORGANISM." International Journal of Modern Physics B 27, no. 21 (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 w

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8

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

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9

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

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10

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

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11

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

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12

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

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13

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

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14

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

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15

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

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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 (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, b

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17

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

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18

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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19

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 (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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20

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

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21

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

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22

Murgida, Daniel Horacio. "Modulation of Functional Features in Electron Transferring Metalloproteins." Science Reviews - from the end of the world 1, no. 2 (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 st

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23

van Wonderen, Jessica H., Katrin Adamczyk, Xiaojing Wu, 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 (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

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24

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 (1986): 211–79. http://dx.doi.org/10.1016/s8755-9668(86)80030-8.

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25

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 (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 testos

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26

Guberman-Pfeffer, Matthew J., and Nikhil S. Malvankar. "Making protons tag along with electrons." Biochemical Journal 478, no. 23 (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

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27

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 (2007): 1617–24. http://dx.doi.org/10.1016/j.jasms.2007.06.002.

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28

Xu, Wu, Parag Chitnis, Alfia Valieva, et al. "Electron Transfer in Cyanobacterial Photosystem I." Journal of Biological Chemistry 278, no. 30 (2003): 27864–75. http://dx.doi.org/10.1074/jbc.m302962200.

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29

Xu, Wu, Parag R. Chitnis, Alfia Valieva, et al. "Electron Transfer in Cyanobacterial Photosystem I." Journal of Biological Chemistry 278, no. 30 (2003): 27876–87. http://dx.doi.org/10.1074/jbc.m302965200.

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30

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

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31

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 (2010): 10370–75. http://dx.doi.org/10.1074/jbc.m109.078337.

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32

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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33

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

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34

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

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35

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

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36

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 (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 D

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37

Rich, P. R. "The osmochemistry of electron-transfer complexes." Bioscience Reports 11, no. 6 (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

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38

Parrish, Jonathan C., J. Guy Guillemette, and Carmichael JA Wallace. "Contribution of leucine 85 to the structure and function of Saccharomyces cerevisiae iso-1 cytochrome c." Biochemistry and Cell Biology 79, no. 4 (2001): 517–24. http://dx.doi.org/10.1139/o01-077.

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Cytochrome c is a small electron-transport protein whose major role is to transfer electrons between complex III (cytochrome reductase) and complex IV (cytochrome c oxidase) in the inner mitochondrial membrane of eukaryotes. Cytochrome c is used as a model for the examination of protein folding and structure and for the study of biological electron-transport processes. Amongst 96 cytochrome c sequences, residue 85 is generally conserved as either isoleucine or leucine. Spatially, the side chain is associated closely with that of the invariant residue Phe82, and this interaction may be importan

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39

Craven, Galen T., and Abraham Nitzan. "Electron transfer across a thermal gradient." Proceedings of the National Academy of Sciences 113, no. 34 (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 multidi

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40

Rabiço, Franciene, Matheus Pedrino, Julia Pereira Narcizo, Adalgisa Rodrigues de Andrade, Valeria Reginatto, and María-Eugenia Guazzaroni. "Synthetic Biology Toolkit for a New Species of Pseudomonas Promissory for Electricity Generation in Microbial Fuel Cells." Microorganisms 11, no. 8 (2023): 2044. http://dx.doi.org/10.3390/microorganisms11082044.

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Microbial fuel cells (MFCs) offer sustainable solutions for various biotechnological applications and are a crucial area of research in biotechnology. MFCs can effectively treat various refuse, such as wastewater and biodiesel waste by decomposing organic matter and generating electricity. Certain Pseudomonas species possess extracellular electron transfer (EET) pathways, enabling them to transfer electrons from organic compounds to the MFC’s anode. Moreover, Pseudomonas species can grow under low-oxygen conditions, which is advantageous considering that the electron transfer process in an MFC

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41

Nishitani, Junichi, Yo-ichi Yamamoto, Christopher W. West, Shutaro Karashima, and Toshinori Suzuki. "Binding energy of solvated electrons and retrieval of true UV photoelectron spectra of liquids." Science Advances 5, no. 8 (2019): eaaw6896. http://dx.doi.org/10.1126/sciadv.aaw6896.

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The electronic energy and dynamics of solvated electrons, the simplest yet elusive chemical species, is of interest in chemistry, physics, and biology. Here, we present the electron binding energy distributions of solvated electrons in liquid water, methanol, and ethanol accurately measured using extreme ultraviolet (EUV) photoelectron spectroscopy of liquids with a single-order high harmonic. The distributions are Gaussian in all cases. Using the EUV and UV photoelectron spectra of solvated electrons, we succeeded in retrieving sharp electron kinetic energy distributions from the spectra broa

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42

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 (2004): 1–26. http://dx.doi.org/10.1016/j.bbapap.2003.10.003.

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43

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 (2012): 38338–46. http://dx.doi.org/10.1074/jbc.m112.374918.

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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 (2010): 646–56. http://dx.doi.org/10.1016/j.jasms.2010.01.001.

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45

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 (1994): 234–38. http://dx.doi.org/10.1038/nsb0494-234.

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46

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

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47

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

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48

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

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49

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

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50

Bjerrum, Morten J., Danilo R. Casimiro, I. Jy Chang, et al. "Electron transfer in ruthenium-modified proteins." Journal of Bioenergetics and Biomembranes 27, no. 3 (1995): 295–302. http://dx.doi.org/10.1007/bf02110099.

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