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Electrostatic Influence on the Energetics of Electron Transfer Reactions

Rees, D. C. (1985) Electrostatic Influence on the Energetics of Electron Transfer Reactions. Proceedings of the National Academy of Sciences of the United States of America, 82 (10). pp. 3082-3085. ISSN 0027-8424. PMCID PMC397718. doi:10.1073/pnas.82.10.3082.

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Electron transfer chains in biological systems must operate efficiently to satisfy metabolic energetic requirements. The component proteins in these chains are expected to exhibit characteristic structural features that facilitate electron transfer to the appropriate donor and acceptor proteins. A survey of soluble one-electron carrier proteins indicates a significant tendency for lower potential proteins to be more negatively charged than higher potential proteins. Consideration of the electrostatic consequences of this pattern of charge asymmetry suggests that the reduction potential difference between the two proteins will be minimized in the precursor complex associated with electron transfer. An equivalent statement is that the change in free energy accompanying electron transfer in the complex will approach zero. This behavior is consistent with theoretical arguments advanced by Albery and Knowles [Albery, W. J. & Knowles, J. R. (1976) Biochemistry 15, 5631-5640], which suggest that for the most efficient enzymes, the free energy difference between enzyme-bound species should approach zero. A more general derivation of this prediction is provided. The observed charge asymmetry in electron transfer proteins provides a structural mechanism for satisfying this requirement, thus accelerating the overall rate of electron transfer.

Item Type:Article
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URLURL TypeDescription CentralArticle
Rees, D. C.0000-0003-4073-1185
Additional Information:© 1985 National Academy of Sciences. Communicated by Paul D. Boyer, December 26, 1984. Discussions with J.B. Howard, T. Yeates, and the University of California at Los Angeles Structural Molecular Biology group are gratefully appreciated. This work was supported by National Institutes of Health Grant GM 31875, the Dreyfus Foundation, and the Chicago Community Trust/Searle Scholars Program. The publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. §1734 solely to indicate this fact.
Funding AgencyGrant Number
NIHGM 31875
Camille and Henry Dreyfus FoundationUNSPECIFIED
Chicago Community TrustUNSPECIFIED
Searle Scholars ProgramUNSPECIFIED
Subject Keywords:enzyme mechanisms; metalloproteins; protein electrostatics; perfect enzymes
Issue or Number:10
PubMed Central ID:PMC397718
Record Number:CaltechAUTHORS:20150210-094548615
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Official Citation:D C Rees Electrostatic influence on energetics of electron transfer reactions PNAS 1985 82 (10) 3082-3085
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:54638
Deposited By: SWORD User
Deposited On:11 Feb 2015 01:00
Last Modified:10 Nov 2021 20:36

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