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Journal articles on the topic 'Electron Transfer'

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Published: 4 June 2021
Last updated: 25 May 2024

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1

Niki, Katsumi, and Takamasa Sagara. "Electron transfer reaction of electron transfer proteins." Kobunshi 39, no. 11 (1990): 830–33. http://dx.doi.org/10.1295/kobunshi.39.830.

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2

WILSON, ELIZABETH. "ELECTRON TRANSFER." Chemical & Engineering News Archive 82, no. 30 (July 26, 2004): 13. http://dx.doi.org/10.1021/cen-v082n030.p013a.

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3

Trammell, Scott A., John C. Wimbish, Fabrice Odobel, Laurie A. Gallagher, Poonam M. Narula, and Thomas J. Meyer. "Mechanisms of Surface Electron Transfer. Proton-Coupled Electron Transfer." Journal of the American Chemical Society 120, no. 50 (December 1998): 13248–49. http://dx.doi.org/10.1021/ja9821854.

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4

Tazuke, Shigeo, Noboru Kitamura, and Yuji Kawanishi. "Problems of back electron transfer in electron transfer sensitization." Journal of Photochemistry 29, no. 1-2 (May 1985): 123–38. http://dx.doi.org/10.1016/0047-2670(85)87065-9.

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5

Kato, Yuki, Ryo Nagao, and Takumi Noguchi. "Redox potential of the terminal quinone electron acceptor QB in photosystem II reveals the mechanism of electron transfer regulation." Proceedings of the National Academy of Sciences 113, no. 3 (December 29, 2015): 620–25. http://dx.doi.org/10.1073/pnas.1520211113.

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Photosystem II (PSII) extracts electrons from water at a Mn4CaO5 cluster using light energy and then transfers them to two plastoquinones, the primary quinone electron acceptor QA and the secondary quinone electron acceptor QB. This forward electron transfer is an essential process in light energy conversion. Meanwhile, backward electron transfer is also significant in photoprotection of PSII proteins. Modulation of the redox potential (Em) gap of QA and QB mainly regulates the forward and backward electron transfers in PSII. However, the full scheme of electron transfer regulation remains unresolved due to the unknown Em value of QB. Here, for the first time (to our knowledge), the Em value of QB reduction was measured directly using spectroelectrochemistry in combination with light-induced Fourier transform infrared difference spectroscopy. The Em(QB−/QB) was determined to be approximately +90 mV and was virtually unaffected by depletion of the Mn4CaO5 cluster. This insensitivity of Em(QB−/QB), in combination with the known large upshift of Em(QA−/QA), explains the mechanism of PSII photoprotection with an impaired Mn4CaO5 cluster, in which a large decrease in the Em gap between QA and QB promotes rapid charge recombination via QA−.
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6

Ekrami, Saeid, and Hamid Reza Shamlouei. "Ab initio study of C20 nanocluster effects on electrochemical properties of tetraphenylporphyrin." Journal of Porphyrins and Phthalocyanines 22, no. 08 (August 2018): 640–45. http://dx.doi.org/10.1142/s1088424618500773.

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The Density Functional Theory (DFT) method was employed to study the properties of the C[Formula: see text] complex with tetraphenylporphyrin (TPP). Calculations were performed in vacuum and in the presence of different solvents. Strong interaction between the C[Formula: see text] cluster and TPP molecule was observed. To understand the effect of C[Formula: see text] on electrochemical properties of TPP, electron transfers from and toward the porphyrin and C[Formula: see text]-TPP complex were studied. It was shown that the presence of C[Formula: see text] influences the electron transfer reaction toward the porphyrin molecule and causes transfer of one and two electrons to C[Formula: see text]-porphyrin, which is more favorable compared with porphyrin alone. However, C[Formula: see text] has slight effect on electron transfer from porphyrin and on positive ion formation. The effect of solvent type on electron transfer energy was studied for these reactions, and it was shown that solvents with higher permittivity have lower electron transfer reaction energy, which may be predicted from ionic character of the products.
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7

Martini, I. B. "Optical Control of Electrons During Electron Transfer." Science 293, no. 5529 (July 20, 2001): 462–65. http://dx.doi.org/10.1126/science.1061612.

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8

ArunaKumari, M. L., and L. Gomathi Devi. "New insights into the origin of the visible light photocatalytic activity of Fe(iii) porphyrin surface anchored TiO2." Environmental Science: Water Research & Technology 1, no. 2 (2015): 177–87. http://dx.doi.org/10.1039/c4ew00024b.

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The chemisorbed Hemin molecule acts as a sensitizer under visible light and transfers photogenerated electrons to the TiO2 conduction band through OC–O–Ti bonds which can act as electron transfer channels. The oxidized Hemin molecule is regenerated by triethanolamine a sacrificial electron donor.
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9

Maran, Flavio, and Mark Workentin. "Dissociative Electron Transfer." Electrochemical Society Interface 11, no. 4 (December 1, 2002): 44–49. http://dx.doi.org/10.1149/2.f07024if.

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10

Fox, Marye Anne. "PHOTOINDUCED ELECTRON TRANSFER." Photochemistry and Photobiology 52, no. 3 (September 1990): 617–27. http://dx.doi.org/10.1111/j.1751-1097.1990.tb01808.x.

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11

Mager, H. I. X., and R. Addink. "Electron transfer-II." Tetrahedron 41, no. 1 (January 1985): 183–90. http://dx.doi.org/10.1016/s0040-4020(01)83484-0.

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12

Beratan, DN, and SS Skourtis. "Electron transfer mechanisms." Current Opinion in Chemical Biology 2, no. 2 (April 1998): 235–43. http://dx.doi.org/10.1016/s1367-5931(98)80065-3.

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13

Borah, D., and M. K. Baruah. "Electron transfer process." Fuel 78, no. 9 (July 1999): 1083–88. http://dx.doi.org/10.1016/s0016-2361(99)00021-6.

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14

McLendon, G., and R. Hake. "Interprotein electron transfer." Chemical Reviews 92, no. 3 (May 1992): 481–90. http://dx.doi.org/10.1021/cr00011a007.

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15

Banaji, Murad, and Stephen Baigent. "Electron transfer networks." Journal of Mathematical Chemistry 43, no. 4 (July 6, 2007): 1355–70. http://dx.doi.org/10.1007/s10910-007-9257-3.

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16

Jortner, Joshua, M. Bixon, and Mark A. Ratner. "Electron transfer dynamics." Journal of Chemical Sciences 109, no. 6 (December 1997): 365–77. http://dx.doi.org/10.1007/bf02869199.

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17

Hernandez, M. E., and D. K. Newman. "Extracellular electron transfer." Cellular and Molecular Life Sciences 58, no. 11 (October 2001): 1562–71. http://dx.doi.org/10.1007/pl00000796.

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18

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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19

Nozik, A. J. "Electron transfer dynamics." Solar Energy Materials and Solar Cells 38, no. 1-4 (January 1995): 327–29. http://dx.doi.org/10.1016/0927-0248(95)00007-0.

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20

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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21

Rosen, Brad M., and Virgil Percec. "Single-Electron Transfer and Single-Electron Transfer Degenerative Chain Transfer Living Radical Polymerization." Chemical Reviews 109, no. 11 (November 11, 2009): 5069–119. http://dx.doi.org/10.1021/cr900024j.

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22

Devadoss, Chelladurai, P. Bharathi, and Jeffrey S. Moore. "Photoinduced Electron Transfer in Dendritic Macromolecules. 1. Intermolecular Electron Transfer." Macromolecules 31, no. 23 (November 1998): 8091–99. http://dx.doi.org/10.1021/ma980225i.

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23

Kebarle, Paul, and Swapan Chowdhury. "Electron affinities and electron-transfer reactions." Chemical Reviews 87, no. 3 (June 1987): 513–34. http://dx.doi.org/10.1021/cr00079a003.

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24

Neff, Diane, Sylwia Smuczynska, and Jack Simons. "Electron shuttling in electron transfer dissociation." International Journal of Mass Spectrometry 283, no. 1-3 (June 2009): 122–34. http://dx.doi.org/10.1016/j.ijms.2009.02.021.

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25

Zhang, Wenyan, Chao Kong, Wei Gao, and Gongxuan Lu. "Intrinsic magnetic characteristics-dependent charge transfer and visible photo-catalytic H2 evolution reaction (HER) properties of a Fe3O4@PPy@Pt catalyst." Chemical Communications 52, no. 14 (2016): 3038–41. http://dx.doi.org/10.1039/c5cc09017b.

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The electron transfer and visible-light-driven hydrogen evolution of a ternary nano-architecture could be regulated effectively by electro-magnetic interaction between the magnetic catalysts and photo-generated electrons.
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26

Ishimori, Koichiro. "Regulation Mechanism of Electron Transfer Reaction from Cytochrome C to Cytochrome C Oxidase." ECS Meeting Abstracts MA2023-01, no. 15 (August 28, 2023): 1420. http://dx.doi.org/10.1149/ma2023-01151420mtgabs.

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The respiratory chain in mitochondria is quite essential for the energy generation in cells, effectively producing “the energy currency in living organisms”, ATP. The driving force for this system is a series of electron transfers form Complex I (NADH:quinone oxidoreductase) to Complex IV (Cytochrome c Oxidase; CcO) in inner mitochondria membrane, and these electron transfer reactions promote the proton pumping from the matrix to the intermembrane space in mitochondria, and, by use of the resulting proton concentration gradient across the membrane, Complex V (ATP synthase) produces ATP. These series of electron transfer reactions terminate at CcO to reduce molecular oxygen to water molecules. The electrons required for this four-electron reduction of molecular oxygen in CcO are donated from a small soluble electron transfer hemoprotein, Cytochrome c (Cyt c), and this electron transfer is also associated with the proton pumping for the ATP generation in the respiratory chain. To examine the molecular regulation mechanism of the electron transfer reaction to terminate the electron transport chain for four-electron reduction of molecular oxygen and proton pumping for the ATP generation, we kinetically followed the electron transfer reaction and analyzed the electron transfer reaction by the Michaelis-Menten equation. By utilizing the Cyt c mutants, we identified the amino acid residues to regulate the electron transfer reactions (Biochem. J., 2020, 477,1565). The kinetic analysis of the electron transfer reaction also revealed that the apparent rate for the electron transfer reaction determined by the steady-state kinetics is much slower than the intramolecular electron transfer rate in the Cyt c – CcO complex. On the other hand, we successfully determined the interaction site between Cyt c and CcO by using NMR (Proc. Natl. Acad. Sci., 2011, 108, 12271) and protein-protein docking simulation (J. Biol. Chem., 2016, 291, 15320). The Cyt c – CcO complex structure estimated from the NMR and protein-protein docking simulation clearly showed that the two redox centers, heme iron in Cyt c and CuA in subunit II of CcO, were located more than 20 Å apart, and the complexes exhibiting shorter redox center distances were energetically unstable. Combined with the results from kinetic and structural studies, we proposed a “conformationally gated electron transfer mechanism”, where the thermal fluctuation of the protein structure controls the electron transfer rate. However, direct experimental evidence that protein conformational fluctuations regulate electron transfer reactions has not been obtained. In this study, we focused on the viscosity of the protein solution as a factor to regulate the conformational fluctuation of the proteins, based on the assumption that high viscosity of the solution suppresses the conformational fluctuation. The electron transfer reaction from Cyt c to CcO was examined in the high viscosity solution and NMR relaxation measurements under high viscosity were also performed to identify the local structural fluctuation responsible for the regulation of the electron transfer rate. Together with the transient complex structures between Cyt c and CcO estimated by the MD simulation, the regulation mechanism of the electron transfer from Cyt c to CcO based on the “conformational gating” will be discussed.
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27

Armstrong, Fraser A., H. Allen O. Hill, and Nicholas J. Walton. "Reactions of electron-transfer proteins at electrodes." Quarterly Reviews of Biophysics 18, no. 3 (August 1985): 261–322. http://dx.doi.org/10.1017/s0033583500000366.

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Studies of electron-transfer reactions of redox proteins have, in recent years, attracted widespread interest and attention. Progress has been evident from both physical and biological standpoints, with the increasing availability of three-dimensional structural data for many small electron-transfer proteins prompting a variety of systematic investigations (Isied, 1985). Most recently, attention has been directed towards questions concerning the elementary transfer of electrons between spatially remote redox sites, and the nature of protein–protein interactions which, for intermolecular processes, stabilize specific precursor complexes which may be optimally juxtaposed for electron-transfer. These and other issues, including the necessary reversibility of protein interfacial interactions and the dynamic properties of proteins as carriers of electrons in biological electron-transport systems, are now being addressed in the rapidly emerging field of direct (unmediated) protein electrochemistry. It is our intention in this article to discuss developments made in this area and highlight points which we believe to have the most bearing on our current understanding of diffusion-dominated, protein-mediated electron transport at electrode surfaces. First we shall outline some basic considerations which are best considered with reference to homogeneous systems.
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28

Larsson, Sven, and Manuel Braga. "Pathways and mobile ? electrons in biological electron transfer." International Journal of Quantum Chemistry 48, S20 (March 13, 1993): 65–76. http://dx.doi.org/10.1002/qua.560480710.

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29

Ramsay, R. R., D. J. Steenkamp, and M. Husain. "Reactions of electron-transfer flavoprotein and electron-transfer flavoprotein: ubiquinone oxidoreductase." Biochemical Journal 241, no. 3 (February 1, 1987): 883–92. http://dx.doi.org/10.1042/bj2410883.

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Electron-transfer flavoprotein:ubiquinone oxidoreductase (ETF-Q oxidoreductase) catalyses the re-oxidation of reduced electron-transfer flavoprotein (ETF) with ubiquinone-1 (Q-1) as the electron acceptor. A kinetic assay for the enzyme was devised in which glutaryl-CoA in the presence of glutaryl-CoA dehydrogenase was used to reduce ETFox. and the reduction of Q-1 was monitored at 275 nm. The partial reactions involved in the overall assay system were examined. Glutaryl-CoA dehydrogenase catalyses the rapid reduction of ETFox. to the anionic semiquinone (ETF.-), but reduces ETF.- to the fully reduced form (ETFhq) at a rate that is about 6-fold lower. ETF.-, but not ETFhq, is directly re-oxidized by Q-1 at a rate that, depending on the steady-state concentration of ETF.-, may contribute significantly to the overall reaction. ETF-Q oxidoreductase catalyses rapid disproportionation of ETF.- with an equilibrium constant of about 1.0 at pH 7.8. In the presence of Q-1 it also catalyses the re-oxidation of ETFhq at a rate that is faster than that of the overall reaction. Rapid-scan experiments indicated the formation of ETF.-, but its fractional concentration in the early stages of the re-oxidation of ETFhq is low. The data indicate that the re-oxidation of ETFhq proceeds at a rate that is adequate to account for the overall rate of electron transfer from glutaryl-CoA to Q-1. An unusual property of ETF-Q oxidoreductase seems to be that it not only catalyses the re-oxidation of the reduced forms of ETF but also facilitates the complete reduction of ETFox. to ETFhq by disproportionation of the radical.
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30

Beckmann, Joe D., and Frank E. Frerman. "Reaction of electron-transfer flavoprotein with electron transfer flavoprotein-ubiquinone oxidoreductase." Biochemistry 24, no. 15 (July 1985): 3922–25. http://dx.doi.org/10.1021/bi00336a017.

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31

FRERMAN, FRANK E. "Acyl-CoA dehydrogenases, electron transfer flavoprotein and electron transfer flavoprotein dehydrogenase." Biochemical Society Transactions 16, no. 3 (June 1, 1988): 416–18. http://dx.doi.org/10.1042/bst0160416.

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32

Kittler, L. "Photoinduced Electron Transfer. Part C. Photoinduced Electron Transfer Reactions: Organic Substrates." Journal of Electroanalytical Chemistry and Interfacial Electrochemistry 276, no. 2 (October 1989): 170–71. http://dx.doi.org/10.1016/0022-0728(89)87310-3.

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33

Kittler, L. "Photoinduced Electron Transfer. Part C. Photoinduced Electron Transfer Reactions: Organic Substrates." Bioelectrochemistry and Bioenergetics 22, no. 2 (October 1989): 170–71. http://dx.doi.org/10.1016/0302-4598(89)80051-0.

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34

Haselbach, Edwin, Denis Pilloud, and Paul Suppan. "Orbital-Symmetry Effects in Bimolecular Electron-Transfer Reactions: Back Electron Transfer." Helvetica Chimica Acta 81, no. 3-4 (1998): 670–75. http://dx.doi.org/10.1002/hlca.19980810317.

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35

Chen, Xiaohua, and Yuxiang Bu. "Cation-Modulated Electron-Transfer Channel: H-Atom Transfer vs Proton-Coupled Electron Transfer with a Variable Electron-Transfer Channel in Acylamide Units." Journal of the American Chemical Society 129, no. 31 (August 2007): 9713–20. http://dx.doi.org/10.1021/ja071194m.

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36

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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37

Sayyar Muhammad, Sayyar Muhammad, Ummul Banin Zahra Ummul Banin Zahra, Aneela Ahmad Aneela Ahmad, and Luqman Ali Shah and Akhtar Muhammad Luqman Ali Shah and Akhtar Muhammad. "Understanding the Basics of Electron Transfer and Cyclic Voltammetry of Potassium Ferricyanide - An Outer Sphere Heterogeneous Electrode Reaction." Journal of the chemical society of pakistan 42, no. 6 (2020): 813. http://dx.doi.org/10.52568/000705.

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Understanding and controlling the processes occurring at electrode/electrolyte interface are very important in optimizing energy conversion devices. Cyclic voltammetry is a very sophisticated and accurate electroanalytical method enables us to explore the mechanism of such electrode reactions. In this work, electrochemical experiments using cyclic voltammetry were performed in aqueous KCl solution containing potassium ferricyanide, K3[Fe(CN)6] at a glassy carbon disc working electrode and the mechanism of the reactions is highlighted. The CV measurements shows that the ferricyanide [Fe(CN)6]3− reduction to ferrocyanide [Fe(CN)6]4− and the reverse oxidation process follows an outer sphere electrode reaction mechanism. Voltammetry analysis further indicates that the reaction is reversible and diffusion controlled one electron transfer electrochemical process. The peak currents due to [Fe(CN)6]4− oxidation and the peak current due to [Fe(CN)6]3− reduction increase with increase of concentration and scan rate increase. The diffusion co-efficient was determined by applying Randles-Sevcik equation. The report could be helpful for university students to understand the basics of electron transfer in redox processes and cyclic voltammetry.
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38

Sayyar Muhammad, Sayyar Muhammad, Ummul Banin Zahra Ummul Banin Zahra, Aneela Ahmad Aneela Ahmad, and Luqman Ali Shah and Akhtar Muhammad Luqman Ali Shah and Akhtar Muhammad. "Understanding the Basics of Electron Transfer and Cyclic Voltammetry of Potassium Ferricyanide - An Outer Sphere Heterogeneous Electrode Reaction." Journal of the chemical society of pakistan 42, no. 6 (2020): 813. http://dx.doi.org/10.52568/000705/jcsp/42.06.2020.

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Understanding and controlling the processes occurring at electrode/electrolyte interface are very important in optimizing energy conversion devices. Cyclic voltammetry is a very sophisticated and accurate electroanalytical method enables us to explore the mechanism of such electrode reactions. In this work, electrochemical experiments using cyclic voltammetry were performed in aqueous KCl solution containing potassium ferricyanide, K3[Fe(CN)6] at a glassy carbon disc working electrode and the mechanism of the reactions is highlighted. The CV measurements shows that the ferricyanide [Fe(CN)6]3− reduction to ferrocyanide [Fe(CN)6]4− and the reverse oxidation process follows an outer sphere electrode reaction mechanism. Voltammetry analysis further indicates that the reaction is reversible and diffusion controlled one electron transfer electrochemical process. The peak currents due to [Fe(CN)6]4− oxidation and the peak current due to [Fe(CN)6]3− reduction increase with increase of concentration and scan rate increase. The diffusion co-efficient was determined by applying Randles-Sevcik equation. The report could be helpful for university students to understand the basics of electron transfer in redox processes and cyclic voltammetry.
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39

Sobczyk, Monika, and Jack Simons. "Distance dependence of through-bond electron transfer rates in electron-capture and electron-transfer dissociation." International Journal of Mass Spectrometry 253, no. 3 (July 2006): 274–80. http://dx.doi.org/10.1016/j.ijms.2006.05.003.

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40

Fukuzumi, Shunichi, Toshiaki Kitano, Masashi Ishikawa, and Yoshiharu Matsuda. "Electron transfer chemistry of hydride and carbanion donors. Hydride and carbanion transfer via electron transfer." Chemical Physics 176, no. 2-3 (October 1993): 337–47. http://dx.doi.org/10.1016/0301-0104(93)80244-4.

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41

Rosen, Brad M., and Virgil Percec. "ChemInform Abstract: Single-Electron Transfer and Single-Electron Transfer Degenerative Chain Transfer Living Radical Polymerization." ChemInform 41, no. 11 (February 19, 2010): no. http://dx.doi.org/10.1002/chin.201011273.

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42

Hembree, G. G., Luo Chuan Hong, P. A. Bennett, and J. A. Venables. "Transfer optics for high spatial resolution electron spectroscopy." Proceedings, annual meeting, Electron Microscopy Society of America 46 (1988): 666–67. http://dx.doi.org/10.1017/s0424820100105394.

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A new field emission scanning transmission electron microscope has been constructed for the NSF HREM facility at Arizona State University. The microscope is to be used for studies of surfaces, and incorporates several surface-related features, including provision for analysis of secondary and Auger electrons; these electrons are collected through the objective lens from either side of the sample, using the parallelizing action of the magnetic field. This collimates all the low energy electrons, which spiral in the high magnetic field. Given an initial field Bi∼1T, and a final (parallelizing) field Bf∼0.01T, all electrons emerge into a cone of semi-angle θf≤6°. The main practical problem in the way of using this well collimated beam of low energy (0-2keV) electrons is that it is travelling along the path of the (100keV) probing electron beam. To collect and analyze them, they must be deflected off the beam path with minimal effect on the probe position.
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43

Lian, Tianquan. "(Invited) Efficient Hot Electron Transfer By Plasmon Induced Interfacial Charge Transfer Transitio." ECS Meeting Abstracts MA2018-01, no. 31 (April 13, 2018): 1867. http://dx.doi.org/10.1149/ma2018-01/31/1867.

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Surface plasmon resonance in metal nanostructures has been widely used to enhance the efficiency of semiconductors and/or molecular chromophore based solar energy conversion devices by increasing absorption or energy transfer rates through the enhanced local field strength. In more recent years, it has been shown that excitation of plasmons in metal nanostructures can also lead to the injection of hot electrons into semiconductors and enhanced photochemistry. This novel mechanism suggests that plasmonic nanostructures can potentially function as a new class of widely tunable and robust light harvesting materials for solar energy conversion. More importantly, it provide a novel approach to access highly energetic and reactive states of metals that is difficult to utilize with thermal chemistry. However, plasmon-induced hot electron injections from metal to semiconductor or molecules are still inefficient because of the competing ultrafast hot electron relaxation processes within the metallic domain. In this talk, I will discuss a recent study on the key factors that limit the efficiency of plasmon induced hot electron transfer in colloidal quantum-confined semiconductor-gold nanorod heterostructures. These heterostructures provide a well-defined and systematically tunable model system for studying the mechanism of hot electron transfer. In CdSe NRs with Au tips, the distinct plasmon band of the Au nanoparticles was completely damped due to strong interaction with the CdSe domain. Using transient absorption spectroscopy, we show that optical excitation of plasmons in the Au tip leads to efficient hot electron injection into the semiconductor nanorod. In the presence of sacrificial electron donors, this plasmon induced hot electron transfer process can be utilized to drive photoreduction reactions under continuous illumination. We propose that the strong metal/semiconductor coupling in CdSe/Au hetersostructures leads to a new pathway for this surprising efficient hot electron transfer. In this plasmon induced interfacial charge transfer transition (PICTT) the a plasmon decay by direct excitation of an electron from the metal to semiconductor, bypassing the competition with hot electron transfer in metal. Ongoing studies are examining the generality of this mechanism and exploring possible approaches for improving its efficiency through controlling the size and shape of the plasmonic and excitonic domains. Reference [1]. Kaifeng Wu, Jinquan Chen, James R. McBride, Tianquan Lian, “Efficient hot-electron transfer by a plasmon-induced interfacial charge-transfer transition”, Science (2015), 349 (6248): 632. DOI: 10.1126/science.aac5443 [2]. Kaifeng Wu, William E. Rodríguez-Córdoba, Ye Yang, and Tianquan Lian, “Plasmon-Induced Hot Electron Transfer from the Au Tip to CdS Rod in CdS-Au Nanoheterostructures”, Nano Lett. (2013), 13(11), 5255-5263. DOI: 10.1021/nl402730m
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44

El-Khouly, Mohamed E., and Shunichi Fukuzumi. "Light harvesting phthalocyanine/subphthalocyanine system: intermolecular electron-transfer and energy-transfer reactions via the triplet subphthalocyanine." Journal of Porphyrins and Phthalocyanines 15, no. 02 (February 2011): 111–17. http://dx.doi.org/10.1142/s1088424611003070.

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Photoinduced electron transfer from the electron-donating zinc tetra-tert-butylphthalocyanine, ZnTBPc , to the electron-accepting dodecafluorosubphthalocyanine, SubPcF12 , in the polar benzonitrile has been investigated with nanosecond laser photolysis method. The examined ZnTBPc/SubPcF12 mixture absorbs the light in a wide section of the UV/vis/NIR spectra. Owing to the particular electronic properties of both entities, such combination seems to be perfectly suited for the study of intermolecular electron-transfer process in the polar solvents via the triplet-excited state of SubPcF12 . Upon excitation of SubPcF12 with 570 nm laser light in polar benzonitrile (εs = 25.2), the electron transfer from ZnTBPc to the triplet-excited state of SubPcF12 was confirmed by observing the transient absorption bands of ZnTBPc radical cation and SubPcF12 radical anion in the visible and near-IR region. On addition of an appropriate electron acceptor with excellent electron-accepting properties, namely dicyanoperylene-3,4,9,10-bis(dicarboximide) ( PDICN2 ), the anion radical of SubPcF12 transfers to the PDICN2 yielding the PDICN2 radical anion. These observations confirm the photosensitized electron-transfer/electron-mediating cycle of ZnTBPc/SubPcF12/PDICN2 system. In non-polar toluene (εs = 2.2), the energy-transfer process from the triplet-excited state of SubPcF12 to the low-lying triplet state of ZnTBPc was confirmed by the consecutive appearance of the triplet ZnTBPc .
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45

Zhu, Lixia, Qi Li, Yongfeng Wan, Meilin Guo, Lu Yan, Hang Yin, and Ying Shi. "Short-Range Charge Transfer in DNA Base Triplets: Real-Time Tracking of Coherent Fluctuation Electron Transfer." Molecules 28, no. 19 (September 25, 2023): 6802. http://dx.doi.org/10.3390/molecules28196802.

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The short-range charge transfer of DNA base triplets has wide application prospects in bioelectronic devices for identifying DNA bases and clinical diagnostics, and the key to its development is to understand the mechanisms of short-range electron dynamics. However, tracing how electrons are transferred during the short-range charge transfer of DNA base triplets remains a great challenge. Here, by means of ab initio molecular dynamics and Ehrenfest dynamics, the nuclear–electron interaction in the thymine-adenine-thymine (TAT) charge transfer process is successfully simulated. The results show that the electron transfer of TAT has an oscillating phenomenon with a period of 10 fs. The charge density difference proves that the charge transfer proportion is as high as 59.817% at 50 fs. The peak position of the hydrogen bond fluctuates regularly between −0.040 and −0.056. The time-dependent Marcus–Levich–Jortner theory proves that the vibrational coupling between nucleus and electron induces coherent electron transfer in TAT. This work provides a real-time demonstration of the short-range coherent electron transfer of DNA base triplets and establishes a theoretical basis for the design and development of novel biological probe molecules.
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46

IWAKI, Masayo. "Electron Transfer in Photosynthesis." Seibutsu Butsuri 39, no. 2 (1999): 65–69. http://dx.doi.org/10.2142/biophys.39.65.

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47

Matyushov, Dmitry V., and Marshall D. Newton. "Electron-Induced Proton Transfer." Journal of Physical Chemistry B 125, no. 44 (October 29, 2021): 12264–73. http://dx.doi.org/10.1021/acs.jpcb.1c06949.

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48

Gray, Harry B., and Jay R. Winkler. "Electron Transfer in Proteins." Annual Review of Biochemistry 65, no. 1 (June 1996): 537–61. http://dx.doi.org/10.1146/annurev.bi.65.070196.002541.

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49

Peluso, Andrea, Méziane Brahimi, Maurizio Carotenuto, and Giuseppe Del Re. "Proton-Assisted Electron Transfer." Journal of Physical Chemistry A 102, no. 50 (December 1998): 10333–39. http://dx.doi.org/10.1021/jp981845o.

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50

Shah, Afzal, Bimalendu Adhikari, Sanela Martic, Azeema Munir, Suniya Shahzad, Khurshid Ahmad, and Heinz-Bernhard Kraatz. "Electron transfer in peptides." Chemical Society Reviews 44, no. 4 (2015): 1015–27. http://dx.doi.org/10.1039/c4cs00297k.

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