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Electron-transfer processes of cytochrome c at interfaces. New insights by surface-enhanced resonance Raman spectroscopy
Zitatschlüssel ISI:000226361400004
Autor Murgida, D H and Hildebrandt, P
Seiten 854-861
Jahr 2004
ISSN 0001-4842
DOI 10.1021/ar0400443
Adresse 1155 16TH ST, NW, WASHINGTON, DC 20036 USA
Journal Acc. Chem. Res.
Jahrgang 37
Nummer 11
Monat NOV
Verlag AMER CHEMICAL SOC
Zusammenfassung The heme protein cytochrome c acts as an electron carrier at the mitochondrial-membrane interface and thus exerts its function under the influence of strong electric fields. To assess possible consequences of electric fields on the redox processes of cytochrome c, the protein can be immobilized to self-assembled monolayers on electrodes and studied by surface-enhanced resonance Raman spectroscopy. Such model systems may mimic some essential features of biological interfaces including local electric field strengths. It is shown that physiologically relevant electric field strengths can effectively modulate the electron-transfer dynamics and induce conformational transitions.
Typ der Publikation Review
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