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Electron-Transfer Processes of Cytochrome c at Interfaces. New Insights by Surface-Enhanced Resonance Raman Spectroscopy
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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Cited by
Using Raman spectroscopy to characterize biological materials
Butler, H. J., Ashton, L., Bird, B., Cinque, G., Curtis, K., Dorney, J., Esmonde-White, K., Fullwood, N. J., Gardner, B., Martin-Hirsch, P. L., et al. (2016) · Nature Protocols · doi:10.1038/nprot.2016.036 · Cited by 1,309
Multiplex in vitro detection using SERS
Laing, S., Gracie, K., & Faulds, K. (2016) · Chemical Society Reviews · doi:10.1039/c5cs00644a · Cited by 361
Wu, D.-Y., Liu, X.-M., Huang, Y.-F., Ren, B., Xu, X., & Tian, Z.-Q. (2009) · The Journal of Physical Chemistry C · doi:10.1021/jp9050929 · Cited by 311
A DyP-type peroxidase at a bio-compatible interface: structural and mechanistic insights
Sezer, M., Genebra, T., Mendes, S., Martins, L. O., & Todorovic, S. (2012) · Soft Matter · doi:10.1039/c2sm26310f · Cited by 23
Metadata
- Authors
- Murgida, D. H., & Hildebrandt, P.
- Venue
- Accounts of Chemical Research
- Publisher
- American Chemical Society (ACS)
- Published
- 2004-09-08
- Volume
- 37
- Issue
- 11
- Pages
- 854-861
- ISSN
- 0001-4842 (ISSN-L)
- 1520-4898
- OpenAlex
- W2163702232
- Cited by
- 236
- References
- 0
- FWCI
- 4.15
- Type
- journal article
- Language
- en
- Open access
- closed
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