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Long-range electron transfer in heme proteins

Mayo, Stephen L. and Ellis, Walther R., Jr. and Crutchley, Robert J. and Gray, Harry B. (1986) Long-range electron transfer in heme proteins. Science, 233 (4767). pp. 948-952. ISSN 0036-8075. doi:10.1126/science.3016897. https://resolver.caltech.edu/CaltechAUTHORS:20110620-160434289

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Abstract

Kinetic experiments have conclusively shown that electron transfer can take place over large distances (greater than 10 angstroms) through protein interiors. Current research focuses on the elucidation of the factors that determine the rates of long-range electron-transfer reactions in modified proteins and protein complexes. Factors receiving experimental and theoretical attention include the donor-acceptor distance, changes in geometry of the donor and acceptor upon electron transfer, and the thermodynamic driving force. Recent experimental work on heme proteins indicates that the electron-transfer rate falls off exponentially with donor-acceptor distance at long range. The rate is greatly enhanced in proteins in which the structural changes accompanying electron transfer are very small.


Item Type:Article
Related URLs:
URLURL TypeDescription
http://dx.doi.org/10.1126/science.3016897DOIArticle
http://www.sciencemag.org/content/233/4767/948PublisherArticle
ORCID:
AuthorORCID
Mayo, Stephen L.0000-0002-9785-5018
Gray, Harry B.0000-0002-7937-7876
Contact Email Address:hbgray@caltech.edu
Additional Information:© 1986 American Association for the Advancement of Science. Supported by grants from the National Science Foundation (CHE85-09637 and CHE85-18793). S.L.M. is an AT&T Bell Laboratories predoctoral fellow (1983 to the present). R.J.C. held a postdoctoral fellowship from the Natural Sciences and Engineering Research Council of Canada during 1982-84. H.B.G. was Visiting Miller Research Professor at the Department of Chemistry, University of California, Berkeley, when the manuscript was completed. We thank the following colleagues for helpful discussion: K. M. Yocom, J. R. Winkler, E. Bordignon, D. G. Nocera, J. B. Shelton, J. R. Shelton, W. A. Schroeder, J. N. Onuchic, G. Worosila, S. S. Isied, B. M. Hoffman, G. L. McLendon, R. A. Scott, A. G. Mauk, M. R. Mauk, N. S. Hush, R. A. Marcus, N. Sutin, J. J. Hopfield, D. N. Beratan, G. L. Closs, M. Smith, G. Pielak, B. D. Olafson, J. L. Campbell, J. H. Richards, W. A. Goddard III, I. Pecht, A. W. Axup, A. A. da Gama, M. Albin, J. H. Dawson, H. Taube, J. R. Miller, B. G. Malmstrom, W. R. Scheidt, and S. Larsson. Contribution 7334 from the Arthur Amos Noyes Laboratory.
Funders:
Funding AgencyGrant Number
NSFCHE85-18793
NSFCHE85-09637
AT&T Bell LaboratoriesUNSPECIFIED
Natural Sciences and Engineering Research Council of Canada (NSERC)UNSPECIFIED
Subject Keywords:Thermodynamics, Cytochrome c Group, Pseudomonas aeruginosa, Hemeproteins, Myoglobin, Electron Transport, Metalloporphyrins, Animals, Horses
Other Numbering System:
Other Numbering System NameOther Numbering System ID
Caltech Arthur Amos Noyes Laboratory7334
Issue or Number:4767
DOI:10.1126/science.3016897
Record Number:CaltechAUTHORS:20110620-160434289
Persistent URL:https://resolver.caltech.edu/CaltechAUTHORS:20110620-160434289
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:24127
Collection:CaltechAUTHORS
Deposited By: Marie Ary
Deposited On:26 Sep 2011 22:33
Last Modified:09 Nov 2021 16:20

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