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Protein electron transfer rates set by the bridging secondary and tertiary structure

Beratan, D. N. and Betts, J. N. and Onuchic, J. N. (1991) Protein electron transfer rates set by the bridging secondary and tertiary structure. Science, 252 (5010). pp. 1285-1288. ISSN 0036-8075. https://resolver.caltech.edu/CaltechAUTHORS:20141205-132010841

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Abstract

The rate of long-distance electron transfer in proteins rapidly decreases with distance, which is indicative of an electron tunneling process. Calculations predict that the distance dependence of electron transfer in native proteins is controlled by the protein's structural motif. The helix and sheet content of a protein and the tertiary arrangement of these secondary structural units define the distance dependence of electronic coupling in that protein. The calculations use a tunneling pathway model applied previously with success to ruthenated proteins. The analysis ranks the average distance decay constant for electronic coupling in electron transfer proteins and identifies the amino acids that are coupled to the charge localization site more strongly or weakly than average for their distance.


Item Type:Article
Related URLs:
URLURL TypeDescription
http://dx.doi.org/10.1126/science.1656523 DOIArticle
http://www.sciencemag.org/content/252/5010/1285PublisherArticle
http://www.jstor.org/stable/2875960JSTORArticle
Additional Information:© 1991 American Association for the Advancement of Science. Received 19 November 1990; accepted 14 March 1991. This work was performed in part at the Jet Propulsion Laboratory, California Institute of Technology, and was sponsored by the Department of Energy's Catalysis/Biocatalysis Program (Advanced Industrial Concepts Division) through an agreement with the National Aeronautics and Space Administration. We thank the National Science Foundation and the Conselho Nacional de Des envolvimento Científico e Tecnológico (Brazil) for a binational research grant that allowed international visits during which this work was initiated. Work in San Diego was funded by a research contract from the Jet Propulsion Laboratory, supported by the Department of Energy's Catalysis/Biocatalysis Program and the National Science Foundation (grant DMB-9018768). The pathway search software, written in FORTRAN for Silicon Graphics IRIS computers, is available from D.N.B. at the Beckman Institute address. J.N.O. is in residence at the Instituto de Física e Química de São Carlos, Universidade de São Paulo, 13560, São Carlos, São Paulo, Brazil during the summers.
Funders:
Funding AgencyGrant Number
Department of Energy (DOE)UNSPECIFIED
NASAUNSPECIFIED
NSFUNSPECIFIED
Conselho Nacional de Des envolvimento Científico e Tecnológico (Brazil)UNSPECIFIED
JPLUNSPECIFIED
NSFDMB-9018768
Issue or Number:5010
Record Number:CaltechAUTHORS:20141205-132010841
Persistent URL:https://resolver.caltech.edu/CaltechAUTHORS:20141205-132010841
Official Citation:Protein electron transfer rates set by the bridging secondary and tertiary structure DN Beratan, JN Betts, and JN Onuchic Science 31 May 1991: 252 (5010), 1285-1288. [DOI:10.1126/science.1656523]
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:52438
Collection:CaltechAUTHORS
Deposited By: Tony Diaz
Deposited On:09 Dec 2014 22:43
Last Modified:03 Oct 2019 07:42

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