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Electron tunneling in structurally engineered proteins

Gray, Harry B. and Winkler, Jay R. (1997) Electron tunneling in structurally engineered proteins. Journal of Electroanalytical Chemistry, 438 (1-2). pp. 43-47. ISSN 1572-6657. https://resolver.caltech.edu/CaltechAUTHORS:20170907-102343386

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Abstract

Photosynthesis, respiration, nitrogen fixation, drug metabolism, DNA synthesis, and immune response are among the scores of biological processes that rely heavily on long-range (10 to 25 Å) protein electron-transfer (ET) reactions. Semiclassical theory predicts that the rates of these reactions depend on the reaction driving force −ΔG°, a nuclear reorganization parameter λ, and the electronic-coupling strength H_(AB) between reactants and products at the transition state: ET rates (k°_(ET)) reach their maximum values when the nuclear factor is optimized (−ΔG° = λ); these k_(ET)° values are limited only by the strength (H_(AB)^2) of the electronic interaction between the donor (D) and acceptor (A). Coupling-limited Cu^+ to Ru^(3+) and Fe^(2+) to Ru^(3+) ET rates have been extracted from kinetic studies on several Ru-modified proteins. In azurin, a blue copper protein, the distant D/A pairs are relatively well coupled (k°_(ET) decreases exponentially with R(CuRu); the decay constant is 1.1 Å^(−1)). In contrast to the extended peptides found in azurin and other β-sheet proteins, helical structures have tortuous covalent pathways owing to the curvature of the peptide backbone. The decay constants estimated from ET rates for D/A pairs separated by long sections of the α helix in myoglobin and the photosynthetic reaction center are between 1.25 and 1.6 Å^(−1).


Item Type:Article
Related URLs:
URLURL TypeDescription
https://doi.org/10.1016/S0022-0728(96)05024-3DOIArticle
http://www.sciencedirect.com/science/article/pii/S0022072896050243PublisherArticle
ORCID:
AuthorORCID
Gray, Harry B.0000-0002-7937-7876
Winkler, Jay R.0000-0002-4453-9716
Additional Information:© 1997 Elsevier Science. Received 1 August 1996. Our work on electron transfer in proteins is supported by the National Science foundation, the National Institutes of Health, and the Arnold and Mabel Beckman Foundation.
Funders:
Funding AgencyGrant Number
NSFUNSPECIFIED
NIHUNSPECIFIED
Arnold and Mabel Beckman FoundationUNSPECIFIED
Subject Keywords:Electron tunneling; Proteins; Electron transfer rate; Decay constant
Issue or Number:1-2
Record Number:CaltechAUTHORS:20170907-102343386
Persistent URL:https://resolver.caltech.edu/CaltechAUTHORS:20170907-102343386
Official Citation:Harry B. Gray, Jay R. Winkler, Electron tunneling in structurally engineered proteins, Journal of Electroanalytical Chemistry, Volume 438, Issue 1, 1997, Pages 43-47, ISSN 1572-6657, http://dx.doi.org/10.1016/S0022-0728(96)05024-3. (http://www.sciencedirect.com/science/article/pii/S0022072896050243)
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:81241
Collection:CaltechAUTHORS
Deposited By: Ruth Sustaita
Deposited On:07 Sep 2017 20:16
Last Modified:22 Nov 2019 09:58

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