HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Hill, B. C. Search for Related Content PubMed PubMed Citation Articles by Hill, B. C. Social Bookmarking                      What's this?

J. Biol. Chem., Vol. 269, Issue 4, 2419-2425, Jan, 1994

Modeling the sequence of electron transfer reactions in the single turnover of reduced, mammalian cytochrome c oxidase with oxygen

BC Hill
Department of Biological Sciences, University of Calgary, Alberta, Canada.

Single-turnover studies of the reaction of reduced cytochrome oxidase with oxygen has led to a mechanistic model that specifies a linear sequence of electron transfer from cytochrome c to O2 via the four redox active metals of mitochondrial cytochrome oxidase. Fully reduced oxidase initially forms a dioxygen adduct within which two electrons are transferred at a rate of 6 x 10(4) s-1 to form a peroxy adduct. This two-electron step results in single-electron oxidation of cytochrome alpha 3 and cytochrome alpha. Cytochrome alpha is then re- reduced by CuA in an intramolecular reaction. Subsequent reoxidation of cytochrome alpha occurs at a rate nearly 100-fold slower than its initial oxidation. Oxidation of CuB in this sequence has been the most difficult to determine and here is specified as the third electron transfer step. This reaction sequence is unchanged in the presence of tightly bound cytochrome c, although cytochrome c is rapidly oxidized via CuA and cytochrome alpha. The linear model advanced here has CuA as the acceptor of electrons from cytochrome c, with cytochrome alpha serving as a bridge to deliver electrons from CuA (and cytochrome c) to the binuclear center, cytochrome alpha 3-CuB.
CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				E. A. Gorbikova, I. Belevich, M. Wikstrom, and M. I. Verkhovsky The proton donor for OO bond scission by cytochrome c oxidase PNAS, August 5, 2008; 105(31): 10733 - 10737. [Abstract] [Full Text] [PDF]

				I. Belevich, V. B. Borisov, and M. I. Verkhovsky Discovery of the True Peroxy Intermediate in the Catalytic Cycle of Terminal Oxidases by Real-time Measurement J. Biol. Chem., September 28, 2007; 282(39): 28514 - 28519. [Abstract] [Full Text] [PDF]

				O. Farver, E. Grell, B. Ludwig, H. Michel, and I. Pecht Rates and Equilibrium of CuA to Heme a Electron Transfer in Paracoccus denitrificans Cytochrome c Oxidase Biophys. J., March 15, 2006; 90(6): 2131 - 2137. [Abstract] [Full Text] [PDF]

				I. Belevich, V. B. Borisov, J. Zhang, K. Yang, A. A. Konstantinov, R. B. Gennis, and M. I. Verkhovsky Time-resolved electrometric and optical studies on cytochrome bd suggest a mechanism of electron-proton coupling in the di-heme active site PNAS, March 8, 2005; 102(10): 3657 - 3662. [Abstract] [Full Text] [PDF]

				T. Tsukihara, K. Shimokata, Y. Katayama, H. Shimada, K. Muramoto, H. Aoyama, M. Mochizuki, K. Shinzawa-Itoh, E. Yamashita, M. Yao, et al. The low-spin heme of cytochrome c oxidase as the driving element of the proton-pumping process PNAS, December 23, 2003; 100(26): 15304 - 15309. [Abstract] [Full Text] [PDF]

				A.-X. Song, L.-Z. Li, T. Yu, S.-M. Chen, and Z.-X. Huang Role of tryptophan 121 in the soluble CuA domain of cytochrome c oxidase: structure and electron transfer studies Protein Eng. Des. Sel., June 1, 2003; 16(6): 435 - 441. [Abstract] [Full Text] [PDF]

				S. Han, S. Takahashi, and D. L. Rousseau Time Dependence of the Catalytic Intermediates in Cytochrome c Oxidase J. Biol. Chem., January 21, 2000; 275(3): 1910 - 1919. [Abstract] [Full Text] [PDF]

				A. Kannt, U. Pfitzner, M. Ruitenberg, P. Hellwig, B. Ludwig, W. Mantele, K. Fendler, and H. Michel Mutation of Arg-54 Strongly Influences Heme Composition and Rate and Directionality of Electron Transfer in Paracoccus denitrificans Cytochrome c Oxidase J. Biol. Chem., December 31, 1999; 274(53): 37974 - 37981. [Abstract] [Full Text] [PDF]

				T. K. Das, C. M. Gomes, M. Teixeira, and D. L. Rousseau Redox-linked transient deprotonation at the binuclear site in the aa3-type quinol oxidase from Acidianus ambivalens: Implications for proton translocation PNAS, August 17, 1999; 96(17): 9591 - 9596. [Abstract] [Full Text] [PDF]

				N. S. Chandel, G.R. S. Budinger, and P. T. Schumacker Molecular Oxygen Modulates Cytochrome c Oxidase Function J. Biol. Chem., August 2, 1996; 271(31): 18672 - 18677. [Abstract] [Full Text] [PDF]

				M. H. Overholtzer, P. S. Yakowec, and V. Cameron The Effect of Amino Acid Substitutions in the Conserved Aromatic Region of Subunit II of Cytochrome c Oxidase in Saccharomyces cerevisiae J. Biol. Chem., March 29, 1996; 271(13): 7719 - 7724. [Abstract] [Full Text] [PDF]

				S. Yoshikawa, M. Mochizuki, X.-J. Zhao, and W. S. Caughey Effects of Overall Oxidation State on Infrared Spectra of Heme a(3) Cyanide in Bovine Heart Cytochrome c Oxidase J. Biol. Chem., March 3, 1995; 270(9): 4270 - 4279. [Abstract] [Full Text] [PDF]