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Thermodynamics of electron transfer in Escherichia coli cytochrome bo(3)

Schultz, Brian E. and Chan, Sunney I. (1998) Thermodynamics of electron transfer in Escherichia coli cytochrome bo(3). Proceedings of the National Academy of Sciences of the United States of America, 95 (20). pp. 11643-11648. ISSN 0027-8424. http://resolver.caltech.edu/CaltechAUTHORS:SCHpnas98

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Abstract

The proton translocation mechanism of the Escherichia coli cytochrome bo(3) complex is intimately tied to the electron transfers within the enzyme. Herein we evaluate two models of proton translocation in this enzyme, a cytochrome c oxidase-type ion-pump and a Q-cycle mechanism, on the basis of the thermodynamics of electron transfer. We conclude that from a thermodynamic standpoint, a Q-cycle is the more favorable mechanism for proton translocation and is likely occurring in the enzyme.


Item Type:Article
Additional Information:Copyright © 1998 by the National Academy of Sciences. Communicated by Fred C. Anson, California Institute of Technology, Pasadena, CA, July 27, 1998 (received for review May 10, 1998). This work was supported by Grant GM22432 from the National Institutes of Health. The publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. §1734 solely to indicate this fact.
Subject Keywords:QUINONE-BINDING SITE, C TERMINAL OXIDASES, UBIQUINOL OXIDASE, BO COMPLEX, SUBUNIT-I, PROTON TRANSLOCATION, 2.8 ANGSTROM, HEME-COPPER, DIOXYGEN, OXYGEN
Record Number:CaltechAUTHORS:SCHpnas98
Persistent URL:http://resolver.caltech.edu/CaltechAUTHORS:SCHpnas98
Alternative URL:http://www.pnas.org/cgi/content/abstract/95/20/11643
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:922
Collection:CaltechAUTHORS
Deposited By: Tony Diaz
Deposited On:09 Nov 2005
Last Modified:26 Dec 2012 08:42

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