Could CuB be the site of redox linkage in cytochrome c oxidase?

Creators: Larsen, Randy W.; Pan, Lian-Ping; Musser, Siegfried M.; Li, Zhuyin; Chan, Sunney I.

Abstract

This paper explores the proton pumping function of cytochrome c oxidase [ferrocytochrome-c:oxygen oxidoreductase (EC 1.9.3.1)] based upon redox linkage at the "high-potential" CU(B) center. A model is proposed that is derived from a redox-linked ligand exchange mechanism previously described for the Cu(A) site. Qualitative analysis of this mechanism indicates that such a mechanism is feasible. However, the relatively short distance between Cu(B) and cytochrome a3 implies that the uncoupling electron transfers are quite facile. In addition, the position of the Cu(B) center with respect to the inner mitochondrial membrane argues against redox linkage at the Cu(B) site.

Additional Information

© 1992 by the National Academy of Sciences. Communicated by Fred Anson, August 5, 1991 (received for review May 30, 1991). This is contribution no. 8443 from the Arthur Amos Noyes Laboratory of Chemical Physics, California Institute of Technology. This work was supported by Grant GM 22432 from the National Institute of General Medical Sciences, U.S. Public Health Service, and Grant PRF#19671-AC3 from the Petroleum Research Fund of the American Chemical Society. 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.

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