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Cited by 1,039

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

ELECTRON TRANSFER IN PROTEINS

Gray, Harry B., Winkler, Jay R.·1996·Annual Review of Biochemistry

Abstract

Electron-transfer (ET) reactions are key steps in a diverse array of biological transformations ranging from photosynthesis to aerobic respiration. A powerful theoretical formalism has been developed that describes ET rates in terms of two parameters: the nuclear reorganization energy (γ) and the electroniccoupling strength (H AB). Studies of ET reactions in ruthenium-modified proteins have probed γ and H AB in several metalloproteins (cytochrome c, myoglobin, azurin). This work has shown that protein reorganization energies are sensitive to the medium surrounding the redox sites and that an aqueous environment, in particular, leads to large reorganization energies. Analyses of electronic-coupling strengths suggest that the efficiency of long-range ET depends on the protein secondary structure: β sheets appear to mediate coupling more efficiently than α-helical structures, and hydrogen bonds play a critical role in both.

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Crossref · 10.1146/annurev.bi.65.070196.002541

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Metadata

Authors
Gray, H. B., & Winkler, J. R.
Venue
Annual Review of Biochemistry
Published
1996-06
Volume
65
Issue
1
Pages
537-561
ISSN
  • 0066-4154 (ISSN-L)
  • 1545-4509
OpenAlex
W2124540342
Cited by
1,039
References
1
FWCI
25.58
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: ELECTRON TRANSFER IN PROTEINS. https://app.cochat.ai/papers/10.1146/annurev.bi.65.070196.002541
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Gray, H. B., & Winkler, J. R. (1996). ELECTRON TRANSFER IN PROTEINS. Annual Review of Biochemistry. https://doi.org/10.1146/annurev.bi.65.070196.002541

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.