Donor—Acceptor Electronic Coupling in Ruthenium-Modified Heme Proteins
Abstract
The rates of electron transfer (ET) in six Ru-modified cytochrome c derivatives were analyzed in terms of four theoretical models describing donor-acceptor electronic coupling. The simplest model, which treats the protein as a homogeneous medium, fails to describe the variations in ET rates with changes in donor-acceptor separation. The three other models explicitly account for the inhomogeneity of the polypeptide matrix and are more successful in describing the electronic couplings. Calculations of relative coupling strengths give results within an order of magnitude of experimentally determined values for cytochrome c. The homogeneousmedium model is more successful in describing ET in Ru-modified myoglobin, and two of the inhomogeneous-medium models suggest that multiple pathways are important in mediating the electronic coupling.
Additional Information
© 1995 American Chemical Society. Received for review July 19, 1993. Accepted revised manuscript December 10, 1993. Published in print 5 May 1996. We thank A. Kuki and R. A. Marcus for preprints of references 13 and 43, respectively. This research was supported by the National Science Foundation, the National Institutes of Health, the Department of Energy, and the Arnold and Mabel Beckman Foundation.Additional details
- Eprint ID
- 85673
- Resolver ID
- CaltechAUTHORS:20180406-080326896
- NSF
- NIH
- Department of Energy (DOE)
- Arnold and Mabel Beckman Foundation
- Created
-
2018-04-06Created from EPrint's datestamp field
- Updated
-
2021-11-15Created from EPrint's last_modified field
- Series Name
- Advances in Chemistry
- Series Volume or Issue Number
- 246