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Long-Range Electron Transfer in Heme Proteins Porphyrin-Ruthenium Electronic Couplings in Three Ru(His)Cytochromes c

Therien, Michael J. and Bowler, Bruce E. and Selman, Mary A. and Gray, Harry B. and Chang, I-Jy and Winkler, Jay R. (1991) Long-Range Electron Transfer in Heme Proteins Porphyrin-Ruthenium Electronic Couplings in Three Ru(His)Cytochromes c. In: Electron Transfer in Inorganic, Organic, and Biological Systems. ACS Symposium Series. No.228. American Chemical Society , Washington, DC, pp. 191-199. ISBN 9780841218468. https://resolver.caltech.edu/CaltechAUTHORS:20180405-131938655

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Abstract

The kinetics of long-range electron transfer (ET) have been measured in Ru(NH_3)_4L(His 39) derivatives (L is NH_3, pyridine, or isonicotinamide) of Zn-substituted Candida krusei cytochrome c and Ru(NH_3)_4L(His 62) derivatives (L is NH_3 or pyridine) of Zn-substituted Saccharomyces cerevisiae cytochrome c. The rates of both excited-state electron transfer and thermal recombination are approximately 3 times greater in Ru(His 39)cytochrome c (Zn) than the rates of the corresponding reactions in Ru(His 33)cytochrome c (Zn), but analogous ET reactions in Ru(His 62)cytochrome c (Zn) are roughly 2 orders of magnitude slower than in the His 33-modified protein. Analysis of driving-force dependences establishes that the large variations in the ET rates are due to differences in donor-acceptor electronic couplings. Examination of potential ET pathways indicates that hydrogen bonds could be responsible for the enhanced electronic couplings in the Ru(His 39) and Ru(His 33) proteins.


Item Type:Book Section
Related URLs:
URLURL TypeDescription
http://dx.doi.org/10.1021/ba-1991-0228.ch012DOIArticle
https://pubs.acs.org/doi/abs/10.1021/ba-1991-0228.ch012PublisherArticle
ORCID:
AuthorORCID
Winkler, Jay R.0000-0002-4453-9716
Additional Information:© 1991 American Chemical Society. Received for review April 27, 1990. Accepted revised manuscript August 29, 1990. Published in print 5 May 1991. We thank David Beratan for helpful discussions. Both M. J. Therien (National Institutes of Health) and Β. E. Bowler (Medical Research Council of Canada) acknowledge postdoctoral fellowships. Research at the California Institute of Technology was suported by the National Science Foundation (CHE88-22988) and the National Institutes of Health (DK19038). Research performed at Brookhaven National Laboratory was carried out under Contract DE-AC02-CH00016 with the U.S. Department of Energy and supported by its Division of Chemical Sciences, Office of Basic Energy Sciences.
Funders:
Funding AgencyGrant Number
NSFCHE88-22988
NIHDK19038
Department of Energy (DOE)DE-AC02-CH00016
Series Name:ACS Symposium Series
Issue or Number:228
Record Number:CaltechAUTHORS:20180405-131938655
Persistent URL:https://resolver.caltech.edu/CaltechAUTHORS:20180405-131938655
Official Citation:Long-Range Electron Transfer in Heme Proteins Michael J. Therien, Bruce E. Bowler, Mary A. Selman, Harry B. Gray, I-Jy Chang, and Jay R. Winkler Electron Transfer in Inorganic, Organic, and Biological Systems. May 5, 1991, 191-199 DOI:10.1021/ba-1991-0228.ch012
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:85643
Collection:CaltechAUTHORS
Deposited By: Ruth Sustaita
Deposited On:05 Apr 2018 20:57
Last Modified:03 Oct 2019 19:33

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