Electron-Transfer Processes of Cytochrome c at Interfaces. New Insights by Surface-Enhanced Resonance Raman Spectroscopy
- 8 September 2004
- journal article
- research article
- Published by American Chemical Society (ACS) in Accounts of Chemical Research
- Vol. 37 (11) , 854-861
- https://doi.org/10.1021/ar0400443
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.Keywords
This publication has 20 references indexed in Scilit:
- Surface-Enhanced Resonance Raman Spectroscopic and Electrochemical Study of Cytochrome c Bound on Electrodes through Coordination with Pyridinyl-Terminated Self-Assembled MonolayersThe Journal of Physical Chemistry B, 2004
- Electrostatic-Field Dependent Activation Energies Modulate Electron Transfer of CytochromecThe Journal of Physical Chemistry B, 2002
- Conformational and Redox Equilibria and Dynamics of Cytochrome c Immobilized on Electrodes via Hydrophobic InteractionsThe Journal of Physical Chemistry B, 2002
- Proton-Coupled Electron Transfer of Cytochrome cJournal of the American Chemical Society, 2001
- Active-Site Structure and Dynamics of Cytochrome c Immobilized on Self-Assembled Monolayers-A Time-Resolved Surface Enhanced Resonance Raman Spectroscopic StudyAngewandte Chemie International Edition in English, 2001
- Heterogeneous Electron Transfer of Cytochrome c on Coated Silver Electrodes. Electric Field Effects on Structure and Redox PotentialThe Journal of Physical Chemistry B, 2001
- The structural and functional role of lysine residues in the binding domain of cytochrome c in the electron transfer to cytochrome c oxidaseEuropean Journal of Biochemistry, 1999
- Novel Time-Resolved Surface-Enhanced (Resonance) Raman Spectroscopic Technique for Studying the Dynamics of Interfacial Processes: Application to the Electron Transfer Reaction of Cytochrome c at a Silver ElectrodeApplied Spectroscopy, 1999
- Time-Resolved Surface-Enhanced Resonance Raman Spectroscopy for Studying Electron-Transfer Dynamics of Heme ProteinsJournal of the American Chemical Society, 1998
- Tryptophan 121 of Subunit II Is the Electron Entry Site to Cytochrome-c Oxidase in Paracoccus denitrificansPublished by Elsevier ,1998