Journal articles: 'Metalloproteins; Electron transfer'

1

Brunori, Maurizio. "Control of electron transfer in metalloproteins." Biosensors and Bioelectronics 9, no. 9-10 (1994): 633–36. http://dx.doi.org/10.1016/0956-5663(94)80059-6.

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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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Gray, Harry B., and Bo G. Malmstroem. "Long-range electron transfer in multisite metalloproteins." Biochemistry 28, no. 19 (September 19, 1989): 7499–505. http://dx.doi.org/10.1021/bi00445a001.

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4

De Jonge, N., H. K. Rau, and W. Haehnel. "Light-induced Electron Transfer in Synthetic Metalloproteins." Zeitschrift für Physikalische Chemie 1, no. 1 (January 1998): 375–80. http://dx.doi.org/10.1524/zpch.1998.1.1.375.

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De Jonge, N., H. K. Rau, and W. Haehnel. "Light-induced Electron Transfer in Synthetic Metalloproteins." Zeitschrift für Physikalische Chemie 213, Part_2 (January 1999): 175–80. http://dx.doi.org/10.1524/zpch.1999.213.part_2.175.

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Ogawa, Michael Y., Jiufeng Fan, Anna Fedorova, Jing Hong, Olesya A. Kharenko, Anna Y. Kornilova, Robin C. Lasey, and Fei Xie. "Electron-transfer functionality of synthetic coiled-coil metalloproteins." Journal of the Brazilian Chemical Society 17, no. 8 (December 2006): 1516–21. http://dx.doi.org/10.1590/s0103-50532006000800006.

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7

Malmstr�m, Bo G. "Structural control of electron-transfer properties in metalloproteins." Biology of Metals 3, no. 2 (1990): 64–66. http://dx.doi.org/10.1007/bf01179504.

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8

Elliott, Martin, and D. Dafydd Jones. "Approaches to single-molecule studies of metalloprotein electron transfer using scanning probe-based techniques." Biochemical Society Transactions 46, no. 1 (December 22, 2017): 1–9. http://dx.doi.org/10.1042/bst20170229.

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The single-molecule properties of metalloproteins have provided an intensely active research area in recent years. This brief review covers some of the techniques used to prepare, measure and analyse the electron transfer properties of metalloproteins, concentrating on scanning tunnelling microscopy-based techniques and advances in attachment of proteins to electrodes.

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Butler, Clive S. "Metals, non-metals and minerals: The complexity of bacterial selenate respiration." Biochemist 34, no. 5 (October 1, 2012): 23–27. http://dx.doi.org/10.1042/bio03405023.

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Metalloproteins and enzymes are an essential part of all respiratory electron-transfer chains and provide a pathway for electron transfer to terminal electron acceptors. Since bacteria can utilize a wide range of respiratory substrates, this variety of potential electron acceptors has facilitated the need for many different respiratory metalloproteins. Bacterial selenate respiration requires the sequential reduction of the selenium oxyanions selenate and selenite resulting in the precipitation of elemental selenium. The initial bioenergetic processes of selenate respiration are driven by metalloproteins utilizing cofactors containing iron and molybdenum. However, the assembly of the elemental selenium into selenium nanosphere crystals has shed light on a new family of proteins involved in selenium biomineralization. This article highlights some of the recent advances in our understanding of selenate respiration in the bacterium Thauera selenatis, with particular focus on the metalloproteins involved in selenate reduction and the novel proteins that function to deal with these insoluble selenium deposits. “As mineralogy constitutes a part of chemistry, it is clear that this arrangement of minerals must derive its principles from chemistry” Jöns Jacob Berzelius 1814

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Winkler, J. R., B. G. Malmström, and H. B. Gray. "Rapid electron injection into multisite metalloproteins: intramolecular electron transfer in cytochrome oxidase." Biophysical Chemistry 54, no. 3 (May 1995): 199–209. http://dx.doi.org/10.1016/0301-4622(94)00156-e.

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BARKER, Paul D., Kati GLERIA, H. Allen O. HILL, and Valerie J. LOWE. "Electron transfer reactions of metalloproteins at peptide-modified gold electrodes." European Journal of Biochemistry 190, no. 1 (May 1990): 171–75. http://dx.doi.org/10.1111/j.1432-1033.1990.tb15561.x.

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Zuo, Xiaolei, Shijiang He, Di Li, Cheng Peng, Qing Huang, Shiping Song, and Chunhai Fan. "Graphene Oxide-Facilitated Electron Transfer of Metalloproteins at Electrode Surfaces." Langmuir 26, no. 3 (February 2, 2010): 1936–39. http://dx.doi.org/10.1021/la902496u.

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13

Mutz, M. W., G. L. McLendon, J. F. Wishart, E. R. Gaillard, and A. F. Corin. "Conformational dependence of electron transfer across de novo designed metalloproteins." Proceedings of the National Academy of Sciences 93, no. 18 (September 3, 1996): 9521–26. http://dx.doi.org/10.1073/pnas.93.18.9521.

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14

Prytkova, Tatiana R., Igor V. Kurnikov, and David N. Beratan. "Ab Initio Based Calculations of Electron-Transfer Rates in Metalloproteins." Journal of Physical Chemistry B 109, no. 4 (February 2005): 1618–25. http://dx.doi.org/10.1021/jp0457491.

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15

Bernauer, Klaus, Simona Ghizdavu, and Luca Verardo. "Chiral metal complexes as probes in electron-transfer reactions involving metalloproteins." Coordination Chemistry Reviews 190-192 (September 1999): 357–69. http://dx.doi.org/10.1016/s0010-8545(99)00094-6.

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16

Durham, Bill, and Frank Millett. "Ruthenium(II) Polypyridine Complexes and the Electron-Transfer Reactions of Metalloproteins." Journal of Chemical Education 74, no. 6 (June 1997): 636. http://dx.doi.org/10.1021/ed074p636.

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Hong, Jing, Olesya A. Kharenko, and Michael Y. Ogawa. "Incorporating Electron-Transfer Functionality into Synthetic Metalloproteins from the Bottom-up." Inorganic Chemistry 45, no. 25 (December 2006): 9974–84. http://dx.doi.org/10.1021/ic060222j.

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18

Solomon, Edward I., David W. Randall, and Thorsten Glaser. "Electronic structures of active sites in electron transfer metalloproteins: contributions to reactivity." Coordination Chemistry Reviews 200-202 (May 2000): 595–632. http://dx.doi.org/10.1016/s0010-8545(00)00332-5.

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19

Itaya, A., H. Sugawara, M. Nakakomi, A. Nagasawa, T. Kohzuma, and S. Suzuki. "Kinetic study on the electron transfer reactions of metalloproteins with cobalt complexes." Journal of Inorganic Biochemistry 67, no. 1-4 (July 1997): 404. http://dx.doi.org/10.1016/s0162-0134(97)80267-x.

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20

Rau, H. K., N. DeJonge, and W. Haehnel. "Modular synthesis of de novo-designed metalloproteins for light-induced electron transfer." Proceedings of the National Academy of Sciences 95, no. 20 (September 29, 1998): 11526–31. http://dx.doi.org/10.1073/pnas.95.20.11526.

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21

Chi, Qijin, Jingdong Zhang, Palle S. Jensen, Hans E. M. Christensen, and Jens Ulstrup. "Long-range interfacial electron transfer of metalloproteins based on molecular wiring assemblies." Faraday Discuss. 131 (2006): 181–95. http://dx.doi.org/10.1039/b506136a.

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22

Taniguchi, Isao. "Probing Metalloproteins and Bioelectrochemical Systems (Rapid electron-transfer at functional electrode surfaces.)." Electrochemical Society Interface 6, no. 4 (December 1, 1997): 34–37. http://dx.doi.org/10.1149/2.f07974if.

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23

TANIGUCHI, Isao. "Electron-Transfer Reactions of Metalloproteins at Electrodes and Preparation of Electro-functional Devices." Seibutsu Butsuri 34, no. 2 (1994): 72–77. http://dx.doi.org/10.2142/biophys.34.72.

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24

Bernauer, Klaus, and Luca Verardo. "Selection of Different Reactive Sites by Enantiomers in Electron-Transfer Reactions Involving Metalloproteins." Angewandte Chemie International Edition in English 35, no. 15 (August 1996): 1716–17. http://dx.doi.org/10.1002/anie.199617161.

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25

Lam, Quan, Mallory Kato, and Lionel Cheruzel. "Ru(II)-diimine functionalized metalloproteins: From electron transfer studies to light-driven biocatalysis." Biochimica et Biophysica Acta (BBA) - Bioenergetics 1857, no. 5 (May 2016): 589–97. http://dx.doi.org/10.1016/j.bbabio.2015.09.004.

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26

Arnesano, Fabio, Lucia Banci, and Mario Piccioli. "NMR structures of paramagnetic metalloproteins." Quarterly Reviews of Biophysics 38, no. 2 (May 2005): 167–219. http://dx.doi.org/10.1017/s0033583506004161.

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1. Introduction 1681.1 Genomic annotation of metalloproteins 1681.2 Why NMR structures? 1681.3 Why paramagnetic metalloproteins? 1692. General theory 1702.1 Nuclear and electron spins 1702.2 Hyperfine coupling 1712.3 The effect of the hyperfine coupling on the NMR shift: the hyperfine shift 1732.4 The effect of the hyperfine coupling on nuclear relaxation 1742.5 Interplay between electron spin properties and features of the NMR spectra 1783. Paramagnetism-based structural restraints 1803.1 Contact shifts and relaxation rates as restraints 1813.2 Locating the metal ion within the protein frame: pseudocontact shifts 1843.3 Cross-correlation rates 1863.4 Residual dipolar couplings 1883.5 Interplay between different restraints 1904. NMR without1H detection 1914.1 The protocol for 13C-detected protonless assignment of backbone and side-chains 1944.2 Protonless heteronuclear NMR experiments tailored to paramagnetic systems 1965. The use of lanthanides as paramagnetic probes 1986. The case of Cu(II) proteins 2027. Perspectives 2088. Acknowledgments 2099. References 209Metalloproteins represent a large share of the proteome and many of them contain paramagnetic metal ions. The knowledge, at atomic resolution, of their structure in solution is important to understand processes in which they are involved, such as electron transfer mechanisms, enzymatic reactions, metal homeostasis and metal trafficking, as well as interactions with their partners. Formerly considered as unfeasible, the first structure in solution by nuclear magnetic resonance (NMR) of a paramagnetic protein was obtained in 1994. Methodological and instrumental advancements pursued over the last decade are such that NMR structure of paramagnetic proteins may be now routinely obtained. We focus here on approaches and problems related to the structure determination of paramagnetic proteins in solution through NMR spectroscopy. After a survey of the background theory, we show how the effects produced by the presence of a paramagnetic metal ion on the NMR parameters, which are in many cases deleterious for the detection of NMR spectra, can be overcome and turned into an additional source of structural restraints. We also briefly address features and perspectives given by the use of 13C-detected protonless NMR spectroscopy for proteins in solution. The structural information obtained through the exploitation of a paramagnetic center are discussed for some Cu2+-binding proteins and for Ca2+-binding proteins, where the replacement of a diamagnetic metal ion with suitable paramagnetic metal ions suggests novel approaches to the structural characterization of proteins containing diamagnetic and NMR-silent metal ions.

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27

Armstrong, F. A., J. N. Butt, and A. Sucheta. "Electrochemical studies of the kinetics and thermodynamics of gated electron-transfer reactions in metalloproteins." Journal of Inorganic Biochemistry 51, no. 1-2 (July 1993): 9. http://dx.doi.org/10.1016/0162-0134(93)85047-c.

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28

Hosseinzadeh, Parisa, and Yi Lu. "Design and fine-tuning redox potentials of metalloproteins involved in electron transfer in bioenergetics." Biochimica et Biophysica Acta (BBA) - Bioenergetics 1857, no. 5 (May 2016): 557–81. http://dx.doi.org/10.1016/j.bbabio.2015.08.006.

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29

Chuev, G. N. "Influence of the protein medium on the electronic state and electron transfer in metalloproteins." Theoretical and Experimental Chemistry 28, no. 2 (1993): 157–60. http://dx.doi.org/10.1007/bf00573930.

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30

Fereiro, Jerry A., Xi Yu, Israel Pecht, Mordechai Sheves, Juan Carlos Cuevas, and David Cahen. "Tunneling explains efficient electron transport via protein junctions." Proceedings of the National Academy of Sciences 115, no. 20 (April 30, 2018): E4577—E4583. http://dx.doi.org/10.1073/pnas.1719867115.

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Metalloproteins, proteins containing a transition metal ion cofactor, are electron transfer agents that perform key functions in cells. Inspired by this fact, electron transport across these proteins has been widely studied in solid-state settings, triggering the interest in examining potential use of proteins as building blocks in bioelectronic devices. Here, we report results of low-temperature (10 K) electron transport measurements via monolayer junctions based on the blue copper protein azurin (Az), which strongly suggest quantum tunneling of electrons as the dominant charge transport mechanism. Specifically, we show that, weakening the protein–electrode coupling by introducing a spacer, one can switch the electron transport from off-resonant to resonant tunneling. This is a consequence of reducing the electrode’s perturbation of the Cu(II)-localized electronic state, a pattern that has not been observed before in protein-based junctions. Moreover, we identify vibronic features of the Cu(II) coordination sphere in transport characteristics that show directly the active role of the metal ion in resonance tunneling. Our results illustrate how quantum mechanical effects may dominate electron transport via protein-based junctions.

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31

Lin, Ying-Wu. "Rational Design of Artificial Metalloproteins and Metalloenzymes with Metal Clusters." Molecules 24, no. 15 (July 29, 2019): 2743. http://dx.doi.org/10.3390/molecules24152743.

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Metalloproteins and metalloenzymes play important roles in biological systems by using the limited metal ions, complexes, and clusters that are associated with the protein matrix. The design of artificial metalloproteins and metalloenzymes not only reveals the structure and function relationship of natural proteins, but also enables the synthesis of artificial proteins and enzymes with improved properties and functions. Acknowledging the progress in rational design from single to multiple active sites, this review focuses on recent achievements in the design of artificial metalloproteins and metalloenzymes with metal clusters, including zinc clusters, cadmium clusters, iron–sulfur clusters, and copper–sulfur clusters, as well as noble metal clusters and others. These metal clusters were designed in both native and de novo protein scaffolds for structural roles, electron transfer, or catalysis. Some synthetic metal clusters as functional models of native enzymes are also discussed. These achievements provide valuable insights for deep understanding of the natural proteins and enzymes, and practical clues for the further design of artificial enzymes with functions comparable or even beyond those of natural counterparts.

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32

Bernauer, K. "Stereo- and site selection by enantiomers in electron-transfer reactions involving native and recombinant metalloproteins." Journal of Inorganic Biochemistry 67, no. 1-4 (July 1997): 400. http://dx.doi.org/10.1016/s0162-0134(97)80263-2.

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33

Bernauer, K., P. Schürmann, C. Nusbaumer, L. Verardo, and Simona Ghizdavu. "Stereo- and site selection by enantiomers in electron-transfer reactions involving native and recombinant metalloproteins." Pure and Applied Chemistry 70, no. 4 (January 1, 1998): 985–91. http://dx.doi.org/10.1351/pac199870040985.

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34

Bond, A. M. "Chemical and electrochemical approaches to the investigation of redox reactions of simple electron transfer metalloproteins." Inorganica Chimica Acta 226, no. 1-2 (November 1994): 293–340. http://dx.doi.org/10.1016/0020-1693(94)04082-6.

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35

Kornilova, Anna Y., James F. Wishart, and Michael Y. Ogawa. "Effect of Surface Charges on the Rates of Intermolecular Electron-Transfer between de Novo Designed Metalloproteins†." Biochemistry 40, no. 40 (October 2001): 12186–92. http://dx.doi.org/10.1021/bi011156u.

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36

Silveira, Célia M., Lidia Zuccarello, Catarina Barbosa, Giorgio Caserta, Ingo Zebger, Peter Hildebrandt, and Smilja Todorovic. "Molecular Details on Multiple Cofactor Containing Redox Metalloproteins Revealed by Infrared and Resonance Raman Spectroscopies." Molecules 26, no. 16 (August 11, 2021): 4852. http://dx.doi.org/10.3390/molecules26164852.

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Vibrational spectroscopy and in particular, resonance Raman (RR) spectroscopy, can provide molecular details on metalloproteins containing multiple cofactors, which are often challenging for other spectroscopies. Due to distinct spectroscopic fingerprints, RR spectroscopy has a unique capacity to monitor simultaneously and independently different metal cofactors that can have particular roles in metalloproteins. These include e.g., (i) different types of hemes, for instance hemes c, a and a3 in caa3-type oxygen reductases, (ii) distinct spin populations, such as electron transfer (ET) low-spin (LS) and catalytic high-spin (HS) hemes in nitrite reductases, (iii) different types of Fe-S clusters, such as 3Fe-4S and 4Fe-4S centers in di-cluster ferredoxins, and (iv) bi-metallic center and ET Fe-S clusters in hydrogenases. IR spectroscopy can provide unmatched molecular details on specific enzymes like hydrogenases that possess catalytic centers coordinated by CO and CN− ligands, which exhibit spectrally well separated IR bands. This article reviews the work on metalloproteins for which vibrational spectroscopy has ensured advances in understanding structural and mechanistic properties, including multiple heme-containing proteins, such as nitrite reductases that house a notable total of 28 hemes in a functional unit, respiratory chain complexes, and hydrogenases that carry out the most fundamental functions in cells.

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37

Kharkats, Yurij I., and Jens Ulstrup. "A simple approach to the solvent reorganization Gibbs free energy in electron transfer reactions of redox metalloproteins." Chemical Physics Letters 303, no. 3-4 (April 1999): 320–24. http://dx.doi.org/10.1016/s0009-2614(99)00231-6.

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38

Bâldea, Ioan. "Important Insight into Electron Transfer in Single-Molecule Junctions Based on Redox Metalloproteins from Transition Voltage Spectroscopy." Journal of Physical Chemistry C 117, no. 48 (November 22, 2013): 25798–804. http://dx.doi.org/10.1021/jp408873c.

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39

Gupta, Sanju, and Aline Irihamye. "Probing the nature of electron transfer in metalloproteins on graphene-family materials as nanobiocatalytic scaffold using electrochemistry." AIP Advances 5, no. 3 (March 2015): 037106. http://dx.doi.org/10.1063/1.4914186.

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40

Brunori, M., R. Santucci, L. Campanella, and G. Tranchida. "Membrane-entrapped microperoxidase as a ‘solid-state’ promoter in the electrochemistry of soluble metalloproteins." Biochemical Journal 264, no. 1 (November 15, 1989): 301–4. http://dx.doi.org/10.1042/bj2640301.

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Immobilization of biological systems in solid matrices is presently of great interest, in view of the many potential advantages associated with both the higher stability of the immobilized macromolecules and the potential utilization for biotechnology. In the present paper the electrochemical behaviour of the undecapeptide from cytochrome c (called microperoxidase) tightly entrapped in cellulose triacetate membrane is reported; its utilization as ‘solid-state’ promoter in the electrochemistry of soluble metalloproteins is presented. The results obtained indicate that: (i) membrane-entrapped microperoxidase undergoes rapid reversible electron transfer at a glassy carbon electrode; (ii) the electrochemical process is diffusion-controlled; (iii) entrapped microperoxidase acts as ‘solid-state’ promoter in the electrochemistry of soluble cytochrome c and of azurin.

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41

SUZUKI, Masato, Kenichi MURATA, Nobuhumi NAKAMURA, and Hiroyuki OHNO. "The Effect of Particle Size on the Direct Electron Transfer Reactions of Metalloproteins Using Au Nanoparticle-Modified Electrodes." Electrochemistry 80, no. 5 (2012): 337–39. http://dx.doi.org/10.5796/electrochemistry.80.337.

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42

Friis, E. P., J. E. T. Andersen, Y. I. Kharkats, A. M. Kuznetsov, R. J. Nichols, J. D. Zhang, and J. Ulstrup. "An approach to long-range electron transfer mechanisms in metalloproteins: In situ scanning tunneling microscopy with submolecular resolution." Proceedings of the National Academy of Sciences 96, no. 4 (February 16, 1999): 1379–84. http://dx.doi.org/10.1073/pnas.96.4.1379.

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43

Rees, Douglas C., F. Akif Tezcan, Chad A. Haynes, Mika Y. Walton, Susana Andrade, Oliver Einsle, and James B. Howard. "Structural basis of biological nitrogen fixation." Philosophical Transactions of the Royal Society A: Mathematical, Physical and Engineering Sciences 363, no. 1829 (April 5, 2005): 971–84. http://dx.doi.org/10.1098/rsta.2004.1539.

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Biological nitrogen fixation is mediated by the nitrogenase enzyme system that catalyses the ATP dependent reduction of atmospheric dinitrogen to ammonia. Nitrogenase consists of two component metalloproteins, the MoFe-protein with the FeMo-cofactor that provides the active site for substrate reduction, and the Fe-protein that couples ATP hydrolysis to electron transfer. An overview of the nitrogenase system is presented that emphasizes the structural organization of the proteins and associated metalloclusters that have the remarkable ability to catalyse nitrogen fixation under ambient conditions. Although the mechanism of ammonia formation by nitrogenase remains enigmatic, mechanistic inferences motivated by recent developments in the areas of nitrogenase biochemistry, spectroscopy, model chemistry and computational studies are discussed within this structural framework.

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44

Hervás, M., J. A. Navarro, A. Díaz, H. Bottin, and M. A. De la Rosa. "Kinetic models for the reaction mechanism of electron transfer from the metalloproteins cytochrome C6 and plastocyanin to photosystem I." Journal of Inorganic Biochemistry 59, no. 2-3 (August 1995): 272. http://dx.doi.org/10.1016/0162-0134(95)97375-z.

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45

Chang, I. Jy, Harry B. Gray, and Jay R. Winkler. "High-driving-force electron transfer in metalloproteins: intramolecular oxidation of ferrocytochrome c by Ru(2,2'-bpy)2(im)(his-33)3+." Journal of the American Chemical Society 113, no. 18 (August 1991): 7056–57. http://dx.doi.org/10.1021/ja00018a064.

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46

Chi, Qijin, Jingdong Zhang, Palle S. Jensen, Renat R. Nazmudtinov, and Jens Ulstrup. "Surface-induced intramolecular electron transfer in multi-centre redox metalloproteins: the di-haem protein cytochromec4in homogeneous solution and at electrochemical surfaces." Journal of Physics: Condensed Matter 20, no. 37 (August 26, 2008): 374124. http://dx.doi.org/10.1088/0953-8984/20/37/374124.

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47

Roger, Magali, Cindy Castelle, Marianne Guiral, Pascale Infossi, Elisabeth Lojou, Marie-Thérèse Giudici-Orticoni, and Marianne Ilbert. "Mineral respiration under extreme acidic conditions: from a supramolecular organization to a molecular adaptation in Acidithiobacillus ferrooxidans." Biochemical Society Transactions 40, no. 6 (November 21, 2012): 1324–29. http://dx.doi.org/10.1042/bst20120141.

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Acidithiobacillus ferrooxidans is an acidophilic chemolithoautotrophic Gram-negative bacterium that can derive energy from the oxidation of ferrous iron at pH 2 using oxygen as electron acceptor. The study of this bacterium has economic and fundamental biological interest because of its use in the industrial extraction of copper and uranium from ores. For this reason, its respiratory chain has been analysed in detail in recent years. Studies have shown the presence of a functional supercomplex that spans the outer and the inner membranes and allows a direct electron transfer from the extracellular Fe2+ ions to the inner membrane cytochrome c oxidase. Iron induces the expression of two operons encoding proteins implicated in this complex as well as in the regeneration of the reducing power. Most of these are metalloproteins that have been characterized biochemically, structurally and biophysically. For some of them, the molecular basis of their adaptation to the periplasmic acidic environment has been described. Modifications in the metal surroundings have been highlighted for cytochrome c and rusticyanin, whereas, for the cytochrome c oxidase, an additional partner that maintains its stability and activity has been demonstrated recently.

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48

Fedurco, Milan. "Redox reactions of heme-containing metalloproteins: dynamic effects of self-assembled monolayers on thermodynamics and kinetics of cytochrome c electron-transfer reactions." Coordination Chemistry Reviews 209, no. 1 (November 2000): 263–331. http://dx.doi.org/10.1016/s0010-8545(00)00292-7.

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49

Zhou, Jian S., and Nenad M. Kostic. "Kinetics of static and diffusive electron transfer between zinc-substituted cytochrome c and plastocyanin. Indications of nonelectrostatic interactions between highly charged metalloproteins." Journal of the American Chemical Society 113, no. 16 (July 1991): 6067–73. http://dx.doi.org/10.1021/ja00016a021.

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50

Govindaraju, K., Hans E. M. Christensen, Emma Lloyd, Marianne Olsen, G. Arthur Salmon, Nicholas P. Tomkinson, and A. Geoffrey Sykes. "A new approach to the study of intramolecular electron-transfer reactions of metalloproteins: pulse radiolysis of nitrogen dioxide-modified tyrosine derivatives of plastocyanin." Inorganic Chemistry 32, no. 1 (January 1993): 40–46. http://dx.doi.org/10.1021/ic00053a007.

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Journal articles on the topic 'Metalloproteins; Electron transfer'

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