Structure and Function of Cytochrome c Oxidase

Structure and Function of Cytochrome c Oxidase Few enzymes have commanded as much attention or are the subject of as much study as cytochrome c oxidase (EC 1.9.3.1). A book has been dedicated 569 0066-4154/90/0701-0569$02.00 CAPALDI entirely to the structure and functioning of the enzyme (1), and meetings have been organized to discuss this protein alone (2). Cytochrome c oxidase is a complex metalloprotein that provides a critical function in cellular respiration in both prokaryotes and eukaryotes. The enzyme catalyzes the reaction 4H+ + 4e- + O2;;= 2 H20. Energy released in this exogonic reaction is conserved as a pH gradient and membrane potential across the membrane barrier, generated in part by H+ consumption and also by proton translocation through the protein complex. This review focuses on aartype cytochrome c oxidase, as opposed to ab- or ao-type oxidases, which are found in some bacteria (3) , and considers the structure-function rela­ tionships that are emerging from studies on the enzyme from a variety of organisms, including bacteria such as Paracoccus denitrificans, and eu­ karyotes as various as slime mold, yeast, and human. Characterization of cytochrome c oxidase from yeast has opened the way for studying the biogenesis of the enzyme. Cytochrome c oxidase in eu­ http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Annual Review of Biochemistry Annual Reviews

Structure and Function of Cytochrome c Oxidase

Annual Review of Biochemistry, Volume 59 (1) – Jul 1, 1990

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Publisher
Annual Reviews
Copyright
Copyright 1990 Annual Reviews. All rights reserved
Subject
Review Articles
ISSN
0066-4154
eISSN
1545-4509
D.O.I.
10.1146/annurev.bi.59.070190.003033
Publisher site
See Article on Publisher Site

Abstract

Few enzymes have commanded as much attention or are the subject of as much study as cytochrome c oxidase (EC 1.9.3.1). A book has been dedicated 569 0066-4154/90/0701-0569$02.00 CAPALDI entirely to the structure and functioning of the enzyme (1), and meetings have been organized to discuss this protein alone (2). Cytochrome c oxidase is a complex metalloprotein that provides a critical function in cellular respiration in both prokaryotes and eukaryotes. The enzyme catalyzes the reaction 4H+ + 4e- + O2;;= 2 H20. Energy released in this exogonic reaction is conserved as a pH gradient and membrane potential across the membrane barrier, generated in part by H+ consumption and also by proton translocation through the protein complex. This review focuses on aartype cytochrome c oxidase, as opposed to ab- or ao-type oxidases, which are found in some bacteria (3) , and considers the structure-function rela­ tionships that are emerging from studies on the enzyme from a variety of organisms, including bacteria such as Paracoccus denitrificans, and eu­ karyotes as various as slime mold, yeast, and human. Characterization of cytochrome c oxidase from yeast has opened the way for studying the biogenesis of the enzyme. Cytochrome c oxidase in eu­

Journal

Annual Review of BiochemistryAnnual Reviews

Published: Jul 1, 1990

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