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Journal articles on the topic 'Charge transfer in biology'

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Author: Grafiati

Published: 4 June 2021

Last updated: 19 February 2022

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1

Wahadoszamen, Md, Tjaart P. J. Krüger, Anjue Mane Ara, Rienk van Grondelle, and Michal Gwizdala. "Charge transfer states in phycobilisomes." Biochimica et Biophysica Acta (BBA) - Bioenergetics 1861, no. 7 (July 2020): 148187. http://dx.doi.org/10.1016/j.bbabio.2020.148187.

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2

Kozma, Balázs, Romain Berraud-Pache, Attila Tajti, and Péter G. Szalay. "Potential energy surfaces of charge transfer states." Molecular Physics 118, no. 19-20 (June 16, 2020): e1776903. http://dx.doi.org/10.1080/00268976.2020.1776903.

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3

Pepi, Lauren E., Zachary J. Sasiene, Praneeth M. Mendis, Glen P. Jackson, and I. Jonathan Amster. "Structural Characterization of Sulfated Glycosaminoglycans Using Charge-Transfer Dissociation." Journal of the American Society for Mass Spectrometry 31, no. 10 (August 21, 2020): 2143–53. http://dx.doi.org/10.1021/jasms.0c00252.

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4

Torrens, Francisco, and Gloria Castellano. "Topological Charge-Transfer Indices: From Small Molecules to Proteins." Current Proteomics 6, no. 4 (December 1, 2009): 204–13. http://dx.doi.org/10.2174/157016409789973770.

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5

Kornyshev, Alexei, Marshall Newton, Jens Ulstrup, and Brett Sanderson. "Molecular charge transfer in condensed media – from physics and chemistry to biology and nanoengineering." Chemical Physics 319, no. 1-3 (December 2005): 1–3. http://dx.doi.org/10.1016/j.chemphys.2005.09.014.

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6

Rigin, Sergei, Georgii Bogdanov, Marina Fonari, and Tatiana V. Timofeeva. "Computational analysis of charge-transfer crystalline complexes." Acta Crystallographica Section A Foundations and Advances 74, a1 (July 20, 2018): a310. http://dx.doi.org/10.1107/s0108767318096903.

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7

Bacchus-Montabonel, Marie-Christine. "Charge Transfer in Ionic and Molecular Systems." International Journal of Molecular Sciences 3, no. 3 (March 28, 2002): 114. http://dx.doi.org/10.3390/i3030114.

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8

Bacchus-Montabonel, Marie-Christine, Ezinvi Baloïtcha, Michèle Desouter-Lecomte, and Nathalie Vaeck. "Rate Coefficient Determination in Charge Transfer Reactions." International Journal of Molecular Sciences 3, no. 3 (March 28, 2002): 176–89. http://dx.doi.org/10.3390/i3030176.

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9

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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10

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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11

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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12

Burggraf, Fabian, and Thorsten Koslowski. "Charge transfer through a cytochrome multiheme chain: Theory and simulation." Biochimica et Biophysica Acta (BBA) - Bioenergetics 1837, no. 1 (January 2014): 186–92. http://dx.doi.org/10.1016/j.bbabio.2013.09.005.

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13

Tadini-Buoninsegni, Francesco, Gianluca Bartolommei, Maria Rosa Moncelli, and Klaus Fendler. "Charge transfer in P-type ATPases investigated on planar membranes." Archives of Biochemistry and Biophysics 476, no. 1 (August 2008): 75–86. http://dx.doi.org/10.1016/j.abb.2008.02.031.

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14

Kottke, Tilman, Aihua Xie, Delmar S. Larsen, and Wouter D. Hoff. "Photoreceptors Take Charge: Emerging Principles for Light Sensing." Annual Review of Biophysics 47, no. 1 (May 20, 2018): 291–313. http://dx.doi.org/10.1146/annurev-biophys-070317-033047.

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The first stage in biological signaling is based on changes in the functional state of a receptor protein triggered by interaction of the receptor with its ligand(s). The light-triggered nature of photoreceptors allows studies on the mechanism of such changes in receptor proteins using a wide range of biophysical methods and with superb time resolution. Here, we critically evaluate current understanding of proton and electron transfer in photosensory proteins and their involvement both in primary photochemistry and subsequent processes that lead to the formation of the signaling state. An insight emerging from multiple families of photoreceptors is that ultrafast primary photochemistry is followed by slower proton transfer steps that contribute to triggering large protein conformational changes during signaling state formation. We discuss themes and principles for light sensing shared by the six photoreceptor families: rhodopsins, phytochromes, photoactive yellow proteins, light-oxygen-voltage proteins, blue-light sensors using flavin, and cryptochromes.

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15

Rawtani, Deepak, Binal Kuntmal, and Y. Agrawal. "Charge transfer in DNA and its diverse modelling approaches." Frontiers in Life Science 9, no. 3 (July 2, 2016): 214–25. http://dx.doi.org/10.1080/21553769.2016.1207570.

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16

Tosi, G., L. Cardellini, and G. Bocelli. "Charge-transfer complexes of hydrazones. VI. Structures of six hydrazone derivatives. Infrared and structural evidence for substituent effects on charge-transfer interactions." Acta Crystallographica Section B Structural Science 44, no. 1 (February 1, 1988): 55–63. http://dx.doi.org/10.1107/s0108768187009042.

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17

Tadini-Buoninsegni, Francesco, and Serena Smeazzetto. "Mechanisms of charge transfer in human copper ATPases ATP7A and ATP7B." IUBMB Life 69, no. 4 (February 5, 2017): 218–25. http://dx.doi.org/10.1002/iub.1603.

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18

Reece, Steven Y., Justin M. Hodgkiss, JoAnne Stubbe, and Daniel G. Nocera. "Proton-coupled electron transfer: the mechanistic underpinning for radical transport and catalysis in biology." Philosophical Transactions of the Royal Society B: Biological Sciences 361, no. 1472 (July 17, 2006): 1351–64. http://dx.doi.org/10.1098/rstb.2006.1874.

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Charge transport and catalysis in enzymes often rely on amino acid radicals as intermediates. The generation and transport of these radicals are synonymous with proton-coupled electron transfer (PCET), which intrinsically is a quantum mechanical effect as both the electron and proton tunnel. The caveat to PCET is that proton transfer (PT) is fundamentally limited to short distances relative to electron transfer (ET). This predicament is resolved in biology by the evolution of enzymes to control PT and ET coordinates on highly different length scales. In doing so, the enzyme imparts exquisite thermodynamic and kinetic controls over radical transport and radical-based catalysis at cofactor active sites. This discussion will present model systems containing orthogonal ET and PT pathways, thereby allowing the proton and electron tunnelling events to be disentangled. Against this mechanistic backdrop, PCET catalysis of oxygen–oxygen bond activation by mono-oxygenases is captured at biomimetic porphyrin redox platforms. The discussion concludes with the case study of radical-based quantum catalysis in a natural biological enzyme, class I Escherichia coli ribonucleotide reductase. Studies are presented that show the enzyme utilizes both collinear and orthogonal PCET to transport charge from an assembled diiron-tyrosyl radical cofactor to the active site over 35 Å away via an amino acid radical-hopping pathway spanning two protein subunits.

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19

Torrens, Francisco. "Valence topological charge-transfer indices for dipole moments." Molecular Diversity 8, no. 4 (2004): 365–70. http://dx.doi.org/10.1023/b:modi.0000047508.78271.b1.

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20

Bull, James N., Robert G. A. R. Maclagan, and Peter W. Harland. "Orientation dependence of the Na + CH3NO2 charge-transfer reaction." Molecular Physics 107, no. 8-12 (April 20, 2009): 1123–37. http://dx.doi.org/10.1080/00268970902755017.

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21

Li, Pengfei, and Glen P. Jackson. "Charge Transfer Dissociation (CTD) Mass Spectrometry of Peptide Cations: Study of Charge State Effects and Side-Chain Losses." Journal of The American Society for Mass Spectrometry 28, no. 7 (January 13, 2017): 1271–81. http://dx.doi.org/10.1007/s13361-016-1574-y.

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22

Henriksson-Enflo, A., and H. Holmgren. "Metals in biology: Electronic structure, properties and charge transfer for copper complexes of glyoxal and dithiene." Theoretica Chimica Acta 87, no. 4-5 (January 1994): 247–66. http://dx.doi.org/10.1007/bf01113382.

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23

Nishida, H. I., H. Arai, and T. Nishida. "Cholesterol ester transfer mediated by lipid transfer protein as influenced by changes in the charge characteristics of plasma lipoproteins." Journal of Biological Chemistry 268, no. 22 (August 1993): 16352–60. http://dx.doi.org/10.1016/s0021-9258(19)85428-5.

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24

Reece, Steven Y., JoAnne Stubbe, and Daniel G. Nocera. "pH dependence of charge transfer between tryptophan and tyrosine in dipeptides." Biochimica et Biophysica Acta (BBA) - Bioenergetics 1706, no. 3 (February 2005): 232–38. http://dx.doi.org/10.1016/j.bbabio.2004.11.011.

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25

Krishtalik, Lev I. "The medium reorganization energy for the charge transfer reactions in proteins." Biochimica et Biophysica Acta (BBA) - Bioenergetics 1807, no. 11 (November 2011): 1444–56. http://dx.doi.org/10.1016/j.bbabio.2011.07.002.

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26

Siletsky, Sergey A., Ashtamurthy S. Pawate, Kara Weiss, Robert B. Gennis, and Alexander A. Konstantinov. "Transmembrane Charge Separation during the Ferryl-oxo → Oxidized Transition in a Nonpumping Mutant of CytochromecOxidase." Journal of Biological Chemistry 279, no. 50 (September 22, 2004): 52558–65. http://dx.doi.org/10.1074/jbc.m407549200.

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The N139D mutant of cytochromecoxidase fromRhodobacter sphaeroidesretains full steady state oxidase activity but completely lacks proton translocation coupled to turnover in reconstituted liposomes (Pawate, A. S., Morgan, J., Namslauer, A., Mills, D., Brzezinski, P., Ferguson-Miller, S., and Gennis, R. B. (2002)Biochemistry41, 13417–13423). Here, time-resolved electron transfer and vectorial charge translocation in the ferryl-oxo → oxidized transition (transfer of the 4th electron in the catalytic cycle) have been studied with the N139D mutant using ruthenium(II)-tris-bipyridyl complex as a photoactive single-electron donor. With the wild type oxidase, the flash-induced generation of Δφ in the ferryl-oxo → oxidized transition begins with rapid vectorial electron transfer from CuAto heme a (τ ∼15 μs), followed by two protonic phases, referred to as the intermediate (0.4 ms) and slow electrogenic phases (1.5 ms). In the N139D mutant, only a single protonic phase (τ ∼0.6 ms) is observed, which was associated with electron transfer from heme a to the heme a3/CuBsite and decelerates ∼4-fold in D2O. With the wild type oxidase, such a high H2O/D2O solvent isotope effect is characteristic of only the slow (1.5 ms) phase. Presumably, the 0.6-ms electrogenic phase in the N139D mutant reports proton transfer from the inner aqueous phase to Glu-286, replacing the “chemical” proton transferred from Glu-286 to the heme a3/CuBsite. The transfer occurs through the D-channel, because it is observed also in the N139D/K362M double mutant in which the K-channel is blocked. It is concluded that the intermediate electrogenic phase observed in the wild type enzyme is missing in the N139D mutant and is because of translocation of the “pumped” proton from Glu-286 to the D-ring propionate of heme a3or to release of this proton to the outer aqueous phase. Significantly, with the wild type oxidase, the protonic electrogenic phase associated with proton pumping (∼0.4 ms) precedes the electrogenic phase associated with the oxygen chemistry (∼1.5 ms).

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27

Hosomi, Hiroyuki, Shigeru Ohba, and Yoshikatsu Ito. "Charge-transfer complexes ofN-methyl-andN-ethylcarbazole with 3,5-dinitrobenzonitrile." Acta Crystallographica Section C Crystal Structure Communications 56, no. 4 (April 15, 2000): e147-e148. http://dx.doi.org/10.1107/s0108270100003851.

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28

Wang, J., S.-J. Gao, P.-C. Zhang, S. Wang, H.-Q. Mao, and K. W. Leong. "Polyphosphoramidate gene carriers: effect of charge group on gene transfer efficiency." Gene Therapy 11, no. 12 (February 26, 2004): 1001–10. http://dx.doi.org/10.1038/sj.gt.3302248.

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29

Elson, Edward. "Developmental control in animals and a biological role for DNA charge transfer." Progress in Biophysics and Molecular Biology 95, no. 1-3 (September 2007): 1–15. http://dx.doi.org/10.1016/j.pbiomolbio.2006.07.001.

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30

Levendis, Demetrius, and David Reid. "Hypervalent chalcogen–chalcogen heteropentalenes and their charge-transfer adducts." Acta Crystallographica Section A Foundations and Advances 75, a2 (August 18, 2019): e506-e506. http://dx.doi.org/10.1107/s2053273319090508.

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31

Ogorzalek Loo, Rachel R., Brian E. Winger, and Richard D. Smith. "Proton transfer reaction studies of multiply charged proteins in a high mass-to-charge ratio quadrupole mass spectrometer." Journal of the American Society for Mass Spectrometry 5, no. 12 (December 1994): 1064–71. http://dx.doi.org/10.1016/1044-0305(94)85067-4.

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32

Rauk, A., G. Hamilton, and G. J. Moore. "Mechanistic consequences of charge transfer systems in serine proteases and angiotensin: Semiempirical computations." Biochemical and Biophysical Research Communications 145, no. 3 (June 1987): 1349–55. http://dx.doi.org/10.1016/0006-291x(87)91586-5.

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33

McDowell, Lynda M., Christine Kirmaier, and Dewey Holten. "Charge transfer and charge resonance states of the primary electron donor in wild-type and mutant bacterial reaction centers." Biochimica et Biophysica Acta (BBA) - Bioenergetics 1020, no. 3 (December 1990): 239–46. http://dx.doi.org/10.1016/0005-2728(90)90153-u.

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34

Hasan, S. Saif, Eiki Yamashita, and William A. Cramer. "Transmembrane signaling and assembly of the cytochrome b6f-lipidic charge transfer complex." Biochimica et Biophysica Acta (BBA) - Bioenergetics 1827, no. 11-12 (November 2013): 1295–308. http://dx.doi.org/10.1016/j.bbabio.2013.03.002.

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35

Kleinherenbrink, F. A. M., and J. Amesz. "Stoichiometries and rates of electron transfer and charge recombination in Heliobacterium chlorum." Biochimica et Biophysica Acta (BBA) - Bioenergetics 1143, no. 1 (June 1993): 77–83. http://dx.doi.org/10.1016/0005-2728(93)90218-5.

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36

Kruk, Jerzy, and Kazimierz Strzafka. "Charge-transfer complexes of plastoquinone and α-tocopherol quinone in phosphatidylcholine and octadecane." Chemistry and Physics of Lipids 70, no. 2 (April 1994): 199–204. http://dx.doi.org/10.1016/0009-3084(94)90087-6.

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37

Kufner, Corinna L., Wolfgang Zinth, and Dominik B. Bucher. "UV‐Induced Charge‐Transfer States in Short Guanosine‐Containing DNA Oligonucleotides." ChemBioChem 21, no. 16 (May 5, 2020): 2306–10. http://dx.doi.org/10.1002/cbic.202000103.

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38

Juretić, Davor, and Paško Županović. "Photosynthetic models with maximum entropy production in irreversible charge transfer steps." Computational Biology and Chemistry 27, no. 6 (December 2003): 541–53. http://dx.doi.org/10.1016/j.compbiolchem.2003.09.001.

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39

Wang, Donghui, Ji Tan, Hongqin Zhu, Yongfeng Mei, and Xuanyong Liu. "Biomedical Implants with Charge‐Transfer Monitoring and Regulating Abilities." Advanced Science 8, no. 16 (June 24, 2021): 2004393. http://dx.doi.org/10.1002/advs.202004393.

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40

Hoffmann, William D., and Glen P. Jackson. "Charge Transfer Dissociation (CTD) Mass Spectrometry of Peptide Cations Using Kiloelectronvolt Helium Cations." Journal of The American Society for Mass Spectrometry 25, no. 11 (September 18, 2014): 1939–43. http://dx.doi.org/10.1007/s13361-014-0989-6.

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41

Semenov, Alexey Yu, Mahir D. Mamedov, and Sergey K. Chamorovsky. "Photoelectric studies of the transmembrane charge transfer reactions in photosystem I pigment-protein complexes." FEBS Letters 553, no. 3 (September 25, 2003): 223–28. http://dx.doi.org/10.1016/s0014-5793(03)01032-9.

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42

Malojčić, Goran, Robin L. Owen, John P. A. Grimshaw, and Rudi Glockshuber. "Preparation and structure of the charge-transfer intermediate of the transmembrane redox catalyst DsbB." FEBS Letters 582, no. 23-24 (September 5, 2008): 3301–7. http://dx.doi.org/10.1016/j.febslet.2008.07.063.

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43

Wang, Shi, Wenrui He, and Wei Huang. "Synthesis and Crystal Structure of Charge-Transfer Salt (TTF)[Pt(mnt)2]." Journal of Chemical Crystallography 41, no. 3 (January 19, 2011): 430–33. http://dx.doi.org/10.1007/s10870-010-9975-4.

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44

Permentier, Hjalmar P., Sieglinde Neerken, Kristiane A. Schmidt, Jörg Overmann, and Jan Amesz. "Energy transfer and charge separation in the purple non-sulfur bacterium Roseospirillum parvum." Biochimica et Biophysica Acta (BBA) - Bioenergetics 1460, no. 2-3 (November 2000): 338–45. http://dx.doi.org/10.1016/s0005-2728(00)00200-0.

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45

Björck, Markus L., and Peter Brzezinski. "Control of transmembrane charge transfer in cytochrome c oxidase by the membrane potential." Biochimica et Biophysica Acta (BBA) - Bioenergetics 1859 (September 2018): e70. http://dx.doi.org/10.1016/j.bbabio.2018.09.209.

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46

Han, Yulun, Sergei Tretiak, and Dmitri Kilin. "Dynamics of charge transfer at Au/Si metal-semiconductor nano-interface." Molecular Physics 112, no. 3-4 (October 14, 2013): 474–84. http://dx.doi.org/10.1080/00268976.2013.842007.

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47

KELEMEN, MARC, CHRISTOPH WACHTER, HUBERT WINTER, ELMAR DORMANN, RUDOLF GOMPPER, and DOMINIK HERMANN. "Magnetic properties of new charge-transfer complexes based on manganese porphyrins." Molecular Physics 90, no. 3 (February 20, 1997): 407–13. http://dx.doi.org/10.1080/00268979709482621.

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48

Lee, Sebok, Myungsam Jen, and Yoonsoo Pang. "Twisted Intramolecular Charge Transfer State of a “Push-Pull” Emitter." International Journal of Molecular Sciences 21, no. 21 (October 27, 2020): 7999. http://dx.doi.org/10.3390/ijms21217999.

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The excited state Raman spectra of 4-dicyanomethylene-2-methyl-6-(p-dimethylaminostyryl)-4H-pyran (DCM) in the locally-excited (LE) and the intramolecular charge transfer (ICT) states have been separately measured by time-resolved stimulated Raman spectroscopy. In a polar dimethylsulfoxide solution, the ultrafast ICT of DCM with a time constant of 1.0 ps was observed in addition to the vibrational relaxation in the ICT state of 4–7 ps. On the other hand, the energy of the ICT state of DCM becomes higher than that of the LE state in a less polar chloroform solution, where the initially-photoexcited ICT state with the LE state shows the ultrafast internal conversion to the LE state with a time constant of 300 fs. The excited-state Raman spectra of the LE and ICT state of DCM showed several major vibrational modes of DCM in the LE and ICT conformer states coexisting in the excited state. Comparing to the time-dependent density functional theory simulations and the experimental results of similar push-pull type molecules, a twisted geometry of the dimethylamino group is suggested for the structure of DCM in the S1/ICT state.

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49

Avenson, Thomas J., Tae Kyu Ahn, Krishna K. Niyogi, Matteo Ballottari, Roberto Bassi, and Graham R. Fleming. "Lutein Can Act as a Switchable Charge Transfer Quencher in the CP26 Light-harvesting Complex." Journal of Biological Chemistry 284, no. 5 (November 6, 2008): 2830–35. http://dx.doi.org/10.1074/jbc.m807192200.

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50

Young, Meggie N., and Christian Bleiholder. "Molecular Structures and Momentum Transfer Cross Sections: The Influence of the Analyte Charge Distribution." Journal of The American Society for Mass Spectrometry 28, no. 4 (March 1, 2017): 619–27. http://dx.doi.org/10.1007/s13361-017-1605-3.

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