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Electron-transfer processes of cytochrome c at interfaces. New insights by surface-enhanced resonance Raman spectroscopy
Citation key ISI:000226361400004
Author Murgida, D H and Hildebrandt, P
Pages 854-861
Year 2004
ISSN 0001-4842
DOI 10.1021/ar0400443
Address 1155 16TH ST, NW, WASHINGTON, DC 20036 USA
Journal Acc. Chem. Res.
Volume 37
Number 11
Month NOV
Publisher AMER CHEMICAL SOC
Abstract 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.
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