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Abstract:

Heterogeneous electron transfer of proteins at biomimetic interfaces is characterized by unusual distance dependences of the electron-transfer rates, whose origin has been elusive and controversial. Using a two-color, time-resolved, surface-enhanced resonance Raman spectroelectrochemical approach, we have been able to monitor simultaneously and in real time the structure, electron-transfer kinetics, and configurational fluctuations of cytochrome c electrostatically adsorbed to electrodes coated with self-assembled monolayers. Our results show that the overall electron-transfer kinetics is determined by protein dynamics rather than by tunnelling probabilities and that the protein dynamics in turn is controlled by the interfacial electric field. Implications for interprotein electron transfer at biological membranes are discussed. © 2008 American Chemical Society.

Registro:

Documento: Artículo
Título:Direct observation of the gating step in protein electron transfer: Electric-field-controlled protein dynamics
Autor:Kranich, A.; Ly, H.K.; Hildebrandt, P.; Murgida, D.H.
Filiación:Institut für Chemie, Technische Universität Berlin, Str. des 17. Juni 135, D10623 Berlin, Germany
Departamento de Química Inorgánica, Analítica Y Química Física, INQUIMAE-CONICET, Pab. 2, C1428EHA Buenos Aires, Argentina
Palabras clave:American Chemical Society (ACS); Biomimetic interfaces; Cytochrome c (Cyt c); Direct observation; Electron transfer (ET); Electron transfer kinetics; Electron transfer rates; Heterogeneous electron transfer (HET); Monitor (CO); Protein dynamics; Real time; Self assembled monolayers (SAMs); Spectroelectrochemical; Surface-Enhanced Resonance; Time-resolved; Two-color; Biological membranes; Biomimetics; Dynamics; Electric fields; Electromagnetic field theory; Electromagnetic fields; Electron transitions; Metallizing; Self assembled monolayers; Electrons; cytochrome c; article; electric field; electricity; electrochemical analysis; electrode; electron transport; protein analysis; protein assembly; Raman spectrometry; Cytochromes c; Electrochemistry; Electrodes; Electrons; Kinetics; Protein Conformation; Silver; Spectrum Analysis, Raman; Sulfhydryl Compounds
Año:2008
Volumen:130
Número:30
Página de inicio:9844
Página de fin:9848
DOI: http://dx.doi.org/10.1021/ja8016895
Título revista:Journal of the American Chemical Society
Título revista abreviado:J. Am. Chem. Soc.
ISSN:00027863
CODEN:JACSA
CAS:cytochrome c, 9007-43-6, 9064-84-0; Cytochromes c, 9007-43-6; Silver, 7440-22-4; Sulfhydryl Compounds
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00027863_v130_n30_p9844_Kranich

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Citas:

---------- APA ----------
Kranich, A., Ly, H.K., Hildebrandt, P. & Murgida, D.H. (2008) . Direct observation of the gating step in protein electron transfer: Electric-field-controlled protein dynamics. Journal of the American Chemical Society, 130(30), 9844-9848.
http://dx.doi.org/10.1021/ja8016895
---------- CHICAGO ----------
Kranich, A., Ly, H.K., Hildebrandt, P., Murgida, D.H. "Direct observation of the gating step in protein electron transfer: Electric-field-controlled protein dynamics" . Journal of the American Chemical Society 130, no. 30 (2008) : 9844-9848.
http://dx.doi.org/10.1021/ja8016895
---------- MLA ----------
Kranich, A., Ly, H.K., Hildebrandt, P., Murgida, D.H. "Direct observation of the gating step in protein electron transfer: Electric-field-controlled protein dynamics" . Journal of the American Chemical Society, vol. 130, no. 30, 2008, pp. 9844-9848.
http://dx.doi.org/10.1021/ja8016895
---------- VANCOUVER ----------
Kranich, A., Ly, H.K., Hildebrandt, P., Murgida, D.H. Direct observation of the gating step in protein electron transfer: Electric-field-controlled protein dynamics. J. Am. Chem. Soc. 2008;130(30):9844-9848.
http://dx.doi.org/10.1021/ja8016895