Gray, Harry B. and Winkler, Jay R. (1996) Electron Transfer in Proteins. Annual Review of Biochemistry, 65 . pp. 537-561. ISSN 0066-4154 http://resolver.caltech.edu/CaltechAUTHORS:GRAarb96
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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.
|Additional Information:||"Reprinted, with permission, from the Annual Review of Biochemistry, Volume 65 copyright 1996 by Annual Reviews, www.annualreviews.org" 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.|
|Subject Keywords:||electron tunneling, electronic coupling, reorganization energy, Cytochrome c, myoglobin, azurin, photosynthetic reaction center, cytochrome c oxidase|
|Usage Policy:||No commercial reproduction, distribution, display or performance rights in this work are provided.|
|Deposited By:||Archive Administrator|
|Deposited On:||14 Jan 2006|
|Last Modified:||26 Dec 2012 08:44|
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