Artículo

Zuo, P.; Albrecht, T.; Barker, P.D.; Murgida, D.H.; Hildebrandt, P. "Interfacial redox processes of cytochrome b562" (2009) Physical Chemistry Chemical Physics. 11(34):7430-7436
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Abstract:

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.

Registro:

Documento: Artículo
Título:Interfacial redox processes of cytochrome b562
Autor:Zuo, P.; Albrecht, T.; Barker, P.D.; Murgida, D.H.; Hildebrandt, P.
Filiación:Technische Universität Berlin, Institut für Chemie, Sekr. PC14 Straße des 17. Juni 135, D-10623 Berlin, Germany
Imperial College London, Department of Chemistry, South Kensington Campus, London SW7 2AZ, United Kingdom
University of Cambridge, Department of Chemistry, Lensfield Road, Cambridge CB2 1EW, United Kingdom
Departamento de Química Inorgánica, Analítica y Química Física, INQUIMAE-CONICET, Ciudad Universitaria, Pab. 2 piso 1, C1428EHA-Buenos Aires, Argentina
Chemical Dynamics Lab, RIKEN, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan
Palabras clave:cytochrome b; cytochrome b562, E coli; Escherichia coli protein; immobilized enzyme; silver; article; chemistry; electrode; oxidation reduction reaction; static electricity; thermodynamics; Cytochrome b Group; Electrodes; Enzymes, Immobilized; Escherichia coli Proteins; Oxidation-Reduction; Silver; Static Electricity; Thermodynamics
Año:2009
Volumen:11
Número:34
Página de inicio:7430
Página de fin:7436
DOI: http://dx.doi.org/10.1039/b904926f
Título revista:Physical Chemistry Chemical Physics
Título revista abreviado:Phys. Chem. Chem. Phys.
ISSN:14639076
CODEN:PPCPF
CAS: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
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_14639076_v11_n34_p7430_Zuo

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Citas:

---------- APA ----------
Zuo, P., Albrecht, T., Barker, P.D., Murgida, D.H. & Hildebrandt, P. (2009) . Interfacial redox processes of cytochrome b562. Physical Chemistry Chemical Physics, 11(34), 7430-7436.
http://dx.doi.org/10.1039/b904926f
---------- CHICAGO ----------
Zuo, P., Albrecht, T., Barker, P.D., Murgida, D.H., Hildebrandt, P. "Interfacial redox processes of cytochrome b562" . Physical Chemistry Chemical Physics 11, no. 34 (2009) : 7430-7436.
http://dx.doi.org/10.1039/b904926f
---------- MLA ----------
Zuo, P., Albrecht, T., Barker, P.D., Murgida, D.H., Hildebrandt, P. "Interfacial redox processes of cytochrome b562" . Physical Chemistry Chemical Physics, vol. 11, no. 34, 2009, pp. 7430-7436.
http://dx.doi.org/10.1039/b904926f
---------- VANCOUVER ----------
Zuo, P., Albrecht, T., Barker, P.D., Murgida, D.H., Hildebrandt, P. Interfacial redox processes of cytochrome b562. Phys. Chem. Chem. Phys. 2009;11(34):7430-7436.
http://dx.doi.org/10.1039/b904926f