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Abstract:

Most of the biochemical and biophysical processes of proteins take place at membranes, and are thus under the influence of strong local electric fields, which are likely to affect the structure as well as the reaction mechanism and dynamics. To analyse such electric field effects, biomimetic interfaces may be employed that consist of membrane models deposited on nanostructured metal electrodes. For such devices, surface-enhanced resonance Raman and IR absorption spectroscopy are powerful techniques to disentangle the complex interfacial processes of proteins in terms of rotational diffusion, electron transfer, and protein and cofactor structural changes. The present article reviews the results obtained for the haem protein cytochrome c, which is widely used as a model protein for studying the various reaction steps of interfacial redox processes in general. In addition, it is shown that electric field effects may be functional for the natural redox processes of cytochrome c in the respiratory chain, as well as for the switch from the redox to the peroxidase function, one of the key events preceding apoptosis. The review focuses on the effects of local electric fields on cytochrome c bound to coated electrodes. For such devices that mimic the electrostatic properties of biological membranes surface-sensitive spectroelectrochemicals allow for an in-depth analysis of the molecular processes of the immobilised cytochrome c, contributing to a better understanding of the potential electric-field dependent control of the protein's function. © 2011 The Authors Journal compilation © 2011 FEBS.

Registro:

Documento: Artículo
Título:Surface-enhanced vibrational spectroscopy for probing transient interactions of proteins with biomimetic interfaces: Electric field effects on structure, dynamics and function of cytochrome c
Autor:Khoa Ly, H.; Sezer, M.; Wisitruangsakul, N.; Feng, J.-J.; Kranich, A.; Millo, D.; Weidinger, I.M.; Zebger, I.; Murgida, D.H.; Hildebrandt, P.
Filiación:Technische Universität Berlin, Institut für Chemie, Sekr. PC 14, Straße des 17 Juni 135, D-10623 Berlin, Germany
Iron and Steel Institute of Thailand, Bangkok, Thailand
School of Chemistry and Environmental Science, Henan Normal University, Xinxiang, China
Departamento de Química Inorgánica, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Argentina
Palabras clave:apoptosis; cytochrome c; electric field; electron transfer; protein dynamics; surface-enhanced infrared spectroscopy; surface-enhanced resonance Raman spectroscopy; cytochrome c; hemoprotein; nanomaterial; absorption spectroscopy; apoptosis; artificial membrane; biomimetic interface; controlled study; device; diffusion; electric field; electrode; electron transport; enzyme immobilization; membrane model; oxidation reduction reaction; priority journal; protein function; protein interaction; protein structure; respiratory chain; review; spectroscopy; surface enhanced infrared absorption; surface enhanced resonance Raman; surface enhanced vibrational spectroscopy; transient interaction; Biomimetics; Cytochromes c; Electrons; Molecular Probes; Molecular Structure; Oxidation-Reduction; Protein Binding; Proteins; Spectrum Analysis; Vibration
Año:2011
Volumen:278
Número:9
Página de inicio:1382
Página de fin:1390
DOI: http://dx.doi.org/10.1111/j.1742-4658.2011.08064.x
Título revista:FEBS Journal
Título revista abreviado:FEBS J.
ISSN:1742464X
CAS:cytochrome c, 9007-43-6, 9064-84-0; Cytochromes c, 9007-43-6; Molecular Probes; Proteins
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_1742464X_v278_n9_p1382_KhoaLy

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Citas:

---------- APA ----------
Khoa Ly, H., Sezer, M., Wisitruangsakul, N., Feng, J.-J., Kranich, A., Millo, D., Weidinger, I.M.,..., Hildebrandt, P. (2011) . Surface-enhanced vibrational spectroscopy for probing transient interactions of proteins with biomimetic interfaces: Electric field effects on structure, dynamics and function of cytochrome c. FEBS Journal, 278(9), 1382-1390.
http://dx.doi.org/10.1111/j.1742-4658.2011.08064.x
---------- CHICAGO ----------
Khoa Ly, H., Sezer, M., Wisitruangsakul, N., Feng, J.-J., Kranich, A., Millo, D., et al. "Surface-enhanced vibrational spectroscopy for probing transient interactions of proteins with biomimetic interfaces: Electric field effects on structure, dynamics and function of cytochrome c" . FEBS Journal 278, no. 9 (2011) : 1382-1390.
http://dx.doi.org/10.1111/j.1742-4658.2011.08064.x
---------- MLA ----------
Khoa Ly, H., Sezer, M., Wisitruangsakul, N., Feng, J.-J., Kranich, A., Millo, D., et al. "Surface-enhanced vibrational spectroscopy for probing transient interactions of proteins with biomimetic interfaces: Electric field effects on structure, dynamics and function of cytochrome c" . FEBS Journal, vol. 278, no. 9, 2011, pp. 1382-1390.
http://dx.doi.org/10.1111/j.1742-4658.2011.08064.x
---------- VANCOUVER ----------
Khoa Ly, H., Sezer, M., Wisitruangsakul, N., Feng, J.-J., Kranich, A., Millo, D., et al. Surface-enhanced vibrational spectroscopy for probing transient interactions of proteins with biomimetic interfaces: Electric field effects on structure, dynamics and function of cytochrome c. FEBS J. 2011;278(9):1382-1390.
http://dx.doi.org/10.1111/j.1742-4658.2011.08064.x