Interfacial redox processes of cytochrome b562

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The anionic soluble heme protein cytochrome b562 was electrostatically immobilised on Ag electrodes coated with positively charged self-assembled monolayers of amino-terminated alkanethiols. The structure of the heme pocket, the redox equilibria, and the electron transfer dynamics were studied by st...

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Autor principal: Zuo, P.
Otros Autores: Albrecht, T., Barker, P.D, Murgida, D.H, Hildebrandt, P.
Formato: Capítulo de libro
Lenguaje:Inglés
Publicado: 2009
Acceso en línea:Registro en Scopus
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024 7 |2 cas  |a cytochrome b, 9035-37-4; silver, 7440-22-4; Cytochrome b Group; Enzymes, Immobilized; Escherichia coli Proteins; Silver, 7440-22-4; cytochrome b562, E coli, 9064-79-3 
040 |a Scopus  |b spa  |c AR-BaUEN  |d AR-BaUEN 
030 |a PPCPF 
100 1 |a Zuo, P. 
245 1 0 |a Interfacial redox processes of cytochrome b562 
260 |c 2009 
270 1 0 |m Murgida, D. H.; Departamento de Química Inorgánica, Analítica y Química Física, INQUIMAE-CONICET, Ciudad Universitaria, Pab. 2 piso 1, C1428EHA-Buenos Aires, Argentina; email: dhmurgida@qi.fcen.uba.ar 
506 |2 openaire  |e Política editorial 
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520 3 |a The anionic soluble heme protein cytochrome b562 was electrostatically immobilised on Ag electrodes coated with positively charged self-assembled monolayers of amino-terminated alkanethiols. The structure of the heme pocket, the redox equilibria, and the electron transfer dynamics were studied by stationary and time-resolved surface enhanced resonance Raman spectroscopy, complemented by cyclic voltammetry measurements of the interfacial redox process. The conformational and redox equilibria of the immobilised protein are compared to those of the cationic heme protein cytochrome c immobilised on negatively charged electrode coatings. Similarities and differences can be rationalised in terms of the respective electric fields at the interfaces of amino- and carboxyl-terminated electrode coatings. The heterogeneous electron transfer rate of cytochrome b562 only slightly increases with decreasing thickness from ca. 20 to 11 Å, implying that the electron tunneling is not the rate-limiting step. In contrast to cytochrome c on carboxyl-terminated monolayers, this behaviour cannot be attributed to protein re-orientation gating the heterogeneous electron transfer. Instead, it may reflect the interplay between interprotein electron transfer and heterogeneous electron transfer via protein orientations exhibiting particularly high tunneling probabilities for the electron exchange with the electrode. © 2009 the Owner Societies.  |l eng 
593 |a Technische Universität Berlin, Institut für Chemie, Sekr. PC14 Straße des 17. Juni 135, D-10623 Berlin, Germany 
593 |a Imperial College London, Department of Chemistry, South Kensington Campus, London SW7 2AZ, United Kingdom 
593 |a University of Cambridge, Department of Chemistry, Lensfield Road, Cambridge CB2 1EW, United Kingdom 
593 |a Departamento de Química Inorgánica, Analítica y Química Física, INQUIMAE-CONICET, Ciudad Universitaria, Pab. 2 piso 1, C1428EHA-Buenos Aires, Argentina 
593 |a Chemical Dynamics Lab, RIKEN, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan 
690 1 0 |a CYTOCHROME B 
690 1 0 |a CYTOCHROME B562, E COLI 
690 1 0 |a ESCHERICHIA COLI PROTEIN 
690 1 0 |a IMMOBILIZED ENZYME 
690 1 0 |a SILVER 
690 1 0 |a ARTICLE 
690 1 0 |a CHEMISTRY 
690 1 0 |a ELECTRODE 
690 1 0 |a OXIDATION REDUCTION REACTION 
690 1 0 |a STATIC ELECTRICITY 
690 1 0 |a THERMODYNAMICS 
690 1 0 |a CYTOCHROME B GROUP 
690 1 0 |a ELECTRODES 
690 1 0 |a ENZYMES, IMMOBILIZED 
690 1 0 |a ESCHERICHIA COLI PROTEINS 
690 1 0 |a OXIDATION-REDUCTION 
690 1 0 |a SILVER 
690 1 0 |a STATIC ELECTRICITY 
690 1 0 |a THERMODYNAMICS 
700 1 |a Albrecht, T. 
700 1 |a Barker, P.D. 
700 1 |a Murgida, D.H. 
700 1 |a Hildebrandt, P. 
773 0 |d 2009  |g v. 11  |h pp. 7430-7436  |k n. 34  |p Phys. Chem. Chem. Phys.  |x 14639076  |t Physical Chemistry Chemical Physics 
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