Academic literature on the topic 'Metalloproteins; Electron transfer'

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Journal articles on the topic "Metalloproteins; Electron transfer"

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

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De Jonge, N., H. K. Rau, and W. Haehnel. "Light-induced Electron Transfer in Synthetic Metalloproteins." Zeitschrift für Physikalische Chemie 1, no. 1 (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 (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, et al. "Electron-transfer functionality of synthetic coiled-coil metalloproteins." Journal of the Brazilian Chemical Society 17, no. 8 (2006): 1516–21. http://dx.doi.org/10.1590/s0103-50532006000800006.

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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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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 (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 (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 metal
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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 (1995): 199–209. http://dx.doi.org/10.1016/0301-4622(94)00156-e.

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Dissertations / Theses on the topic "Metalloproteins; Electron transfer"

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Taiwo, Fatai Adetokunbo. "Electron transfer effects in metalloproteins : an ESR study." Thesis, University of Leicester, 1988. http://hdl.handle.net/2381/33944.

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The metal chromophore in metalloproteins is identified as a high affinity site for dry electrons in conformity with previous studies. Relative electron affinities for such centres in a physiologically probable valence hybrid haemoglobin have been determined. A ratio of ca. 2.5 for the electron affinity of oxyhaemog1obin over methaemog1obin is explained in terms of structural differences in the constituent forms. The phenomenon of intersubunit electron transfer in similar systems is considered in terms of haem edge-to-edge minimum separation. The hydrogen peroxide complex of iron haemoproteins
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Hong, Jing. "DESIGN, CHARACTERIZATION, AND ELECTRON TRANSFER PROPERTIES OF SYNTHETIC METALLOPROTEINS." Bowling Green State University / OhioLINK, 2006. http://rave.ohiolink.edu/etdc/view?acc_num=bgsu1149775101.

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Worrall, Jonathan A. R. "Studies on electron-transfer reactions of Fe and Cu metalloproteins." Thesis, University of Newcastle Upon Tyne, 1999. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.246711.

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Pershad, Harsh R. "Studies of redox proteins and enzymes using protein-film voltammetry." Thesis, University of Oxford, 2000. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.325777.

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Jackman, M. P. "Kinetics of electron transfer in some metalloproteins and their Ru-modified derivatives." Thesis, University of Newcastle Upon Tyne, 1987. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.379765.

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Fan, Jiufeng. "Bottom-Up Design of Synthetic Photoactive Metalloproteins." Bowling Green State University / OhioLINK, 2009. http://rave.ohiolink.edu/etdc/view?acc_num=bgsu1256410648.

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Wang, Xie. "Biochemical and electrochemical studies of metalloproteins involved in oxygen reduction pathway in Acidithiobacillus ferrooxidans." Thesis, Aix-Marseille, 2018. http://www.theses.fr/2018AIXM0579.

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Acidithiobacillus ferrooxidans (A. f.) est un modèle bactérien parfaitement adapté à l’étude de la survie en milieu acide. Si plusieurs métalloprotéines ont été identifiées et caractérisées d’un point de vue biochimique, le fonctionnement de la chaîne respiratoire couplant l’oxydation du Fe(II) à la réduction de l’oxygène dans cet organisme n’est pas élucidée. Au cours de ce travail de thèse, après avoir optimisé les conditions de croissance de la bactérie et de production des protéines redox impliquées, nous avons reconstitué sur interface électrochimique une partie de la chaîne respiratoire
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Chaussade, Marc. "Étude par RMN à haute résolution en solide de modèles synthétiques des sites actifs des protéines à {4Fe-4S}." Grenoble 1, 1998. http://www.theses.fr/1998GRE10139.

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Les ferredoxines a 4fe-4s constituent une categorie de metalloproteines particulierement etudiee depuis leur decouverte dans les annees 1960 en raison de leur fonction clef de transfert electronique dans les metabolismes essentiels de la vie. Le cluster de type pseudo-cubane 4fe-4s opere entre les deux etats redox fe#4s#4#2#+(2+) et fe#4s#4#1#+(1+) et est responsable du transfert electronique. Il est possible d'en synthetiser chimiquement des analogues afin d'en simplifier l'etude. Ses proprietes magnetiques font l'objet de beaucoup d'investigations car il presente des couplages magnetiques co
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HUBERT, JEAN-GASPARD. "Rmn de proteines 4fe-4s : proprietes structurales et transfert electronique intramoleculaire." Université Joseph Fourier (Grenoble), 1996. http://www.theses.fr/1996GRE10175.

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Les proprietes de deplacement chimique et de relaxation des spins nucleaires, surtout quand elles sont influencees par le paramagnetisme de centres polymetalliques, apportent de nouvelles informations sur la structure atomique, electronique et magnetiques des proteines 4fe-4s et sur la vitesse d'echange electronique entre clusters
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Brouquisse, Renaud. "Etude des protéines fer-soufre des mitochondries végétales : caractérisation et purification de l'aconitase." Grenoble 1, 1987. http://www.theses.fr/1987GRE10088.

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Les proteines a centre (fe-s) des mitochondries vegetales sont etudiees par resonance para magnetique (rpe), cette etude a permis de caracteriser les centres (fe-s) impliques dans la chaine respiratoire de la membrane interne puis d'etudier et de purifier l'aconitase matricielle. L'activite aconitase dans les cellules d'erable est associee a deux fractions proteique. L'une est presente dans le cytosol alors que la seconde est d'origine mitochondriale. La presence de l'aconitase et de l'isocitrate deshydrogenase nadp-dependante dans le cytosol permet de penser que ces enzymes pourraient avoir u
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Books on the topic "Metalloproteins; Electron transfer"

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Helmut, Sigel, and Sigel Astrid, eds. Electron transfer reactions in metalloproteins. M. Dekker, 1991.

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1947-, Bertrand P., ed. Long-range electron transfer in biology. Springer-Verlag, 1991.

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A, Nicolini Claudio, ed. Biophysics of electron transfer and molecular bioelectronics. Plenum Press, 1998.

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Nicolini, C. Biophysics of Electron Transfer and Molecular Bioelectronics (Electronics and Biotechnology Advanced (Elba) Forum Series). Springer, 1999.

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1953-, Johnson Michael K., American Chemical Society. Division of Inorganic Chemistry., and Inorganic Chemistry Symposium (1989 : Athens, Ga.), eds. Electron transfer in biology and the solid state: Inorganic compounds with unusual properties. American Chemical Society, 1990.

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Electron Transfer in Biology and the Solid State: Inorganic Compounds with Unusual Properties (Advances in Chemistry Series). Oxford University Press, USA, 1989.

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Book chapters on the topic "Metalloproteins; Electron transfer"

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Therien, Michael J., Jeffrey Chang, Adrienne L. Raphael, Bruce E. Bowler, and Harry B. Gray. "Long-range electron transfer in metalloproteins." In Long-Range Electron Transfer in Biology. Springer Berlin Heidelberg, 1991. http://dx.doi.org/10.1007/3-540-53260-9_4.

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Yang, Xin, Xue-Bin Wang, You-Jun Fu, and Lai-Sheng Wang. "Probing the Electronic Structure of FeS Clusters: Ubiquitous Electron Transfer Centers in Metalloproteins Using Anion Photoelectron Spectroscopy in the Gas Phase." In Principles of Mass Spectrometry Applied to Biomolecules. John Wiley & Sons, Inc., 2006. http://dx.doi.org/10.1002/047005042x.ch2.

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Palma, P. Nuno, Jean Legall, John E. Wampler, and José J. G. Moura. "Molecular Interactions Between Metalloproteins Involved in Electron Transfer Processes: Tetraheme Cytochrome c 3 and Flavodoxin. Nmr and Molecular Modeling Studies." In Transition Metals in Supramolecular Chemistry. Springer Netherlands, 1994. http://dx.doi.org/10.1007/978-94-015-8380-0_15.

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Nicolini, Claudio. "Metalloprotein Engineering for New Materials, Drugs and Nanodevices." In Biophysics of Electron Transfer and Molecular Bioelectronics. Springer US, 1998. http://dx.doi.org/10.1007/978-1-4757-9516-5_1.

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Kostić, Nenad M. "Dynamic Aspects of Electron-Transfer Reactions in Metalloprotein Complexes." In Metal-Containing Polymeric Materials. Springer US, 1996. http://dx.doi.org/10.1007/978-1-4613-0365-7_37.

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Kuznetsov, Aleksandr M., Jens Ulstrup, and Merab G. Zakaraya. "Protein Configurational Fluctuation Dependence of the Electronic Tunnel Factor of Modified Metalloprotein Electron Transfer Systems and in Fast Direct and Superexchange Separation and Recombination in Bacterial Photosynthesis." In The Jerusalem Symposia on Quantum Chemistry and Biochemistry. Springer Netherlands, 1990. http://dx.doi.org/10.1007/978-94-009-0489-7_19.

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"Electron Transfer." In Encyclopedia of Metalloproteins. Springer New York, 2013. http://dx.doi.org/10.1007/978-1-4614-1533-6_100472.

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"Electron Transfer Shuttles." In Encyclopedia of Metalloproteins. Springer New York, 2013. http://dx.doi.org/10.1007/978-1-4614-1533-6_100473.

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Bizzarri, A. R., and S. Cannistraro. "Metalloproteins, Electron Transfer in." In Encyclopedia of Condensed Matter Physics. Elsevier, 2005. http://dx.doi.org/10.1016/b0-12-369401-9/00379-x.

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Bizzarri, A. R., and S. Cannistraro. "Biophysics: Electron Transfer in Metalloproteins." In Reference Module in Materials Science and Materials Engineering. Elsevier, 2016. http://dx.doi.org/10.1016/b978-0-12-803581-8.00993-0.

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Reports on the topic "Metalloproteins; Electron transfer"

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Peerey, L. Cross-linked metalloproteins: Novel systems for the study of intraprotein electron-transfer reactions. Office of Scientific and Technical Information (OSTI), 1990. http://dx.doi.org/10.2172/7118554.

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