Few enzymes have commanded as much attention or are the subject of as much study as cytochrome c oxidase (EC 184.108.40.206). 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 relaÂ tionships that are emerging from studies on the enzyme from a variety of organisms, including bacteria such as Paracoccus denitrificans, and euÂ 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 euÂ
Annual Review of Biochemistry – Annual Reviews
Published: Jul 1, 1990
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