A Caltech Library Service

Electron Transfer in Proteins

Gray, Harry B. and Winkler, Jay R. (1996) Electron Transfer in Proteins. Annual Review of Biochemistry, 65 . pp. 537-561. ISSN 0066-4154. doi:10.1146/

PDF - Published Version
See Usage Policy.


Use this Persistent URL to link to this item:


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 [lambda] energy (1) and the electronic-coupling strength (HAB). Studies of ET reactions in ruthenium-modified proteins have probed [lambda] and HAB 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: [beta]sheets appear to mediate coupling more efficiently than [alpha]-helical structures, and hydrogen bonds play a critical role in both.

Item Type:Article
Related URLs:
URLURL TypeDescription
Gray, Harry B.0000-0002-7937-7876
Winkler, Jay R.0000-0002-4453-9716
Additional Information:"Reprinted, with permission, from the Annual Review of Biochemistry, Volume 65 copyright 1996 by Annual Reviews," We thank BG Malmstrom, JN Onuchic, JJ Regan, MJ Therien, and K Warncke for helpful discussions. Our work on protein electron transfer is supported by the National Institutes of Health, the National Science Foundation, and the Arnold and Mabel Beckman Foundation.
Funding AgencyGrant Number
Arnold and Mabel Beckman FoundationUNSPECIFIED
Subject Keywords:electron tunneling, electronic coupling, reorganization energy, Cytochrome c, myoglobin, azurin, photosynthetic reaction center, cytochrome c oxidase
Record Number:CaltechAUTHORS:GRAarb96
Persistent URL:
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:1394
Deposited By: Archive Administrator
Deposited On:14 Jan 2006
Last Modified:08 Nov 2021 19:09

Repository Staff Only: item control page