title: Cytochrome c oxidase metal centers: location and function.
abstract: Cytochrome c oxidase of Paracoccus denitrificans is spectroscopically and functionally very similar to the mammalian enzyme. However, it has a very much simpler quaternary structure, consisting of only three subunits instead of the 13 of the bovine enzyme. The known primary structure of the Paracoccus denitrificans subunits, the knowledge of a large number of sequences from other species, and data on the controlled proteolytic digestion of the enzyme allow structural restrictions to be placed on the models describing the binding of the active metal centers to the polypeptide structure.
authors.affiliation: Institut für Biochemie und Molekularbiologie der Universität Bern, Switzerland.
authors.forename: M
authors.initials: M
authors.lastname: Müller
authors.forename: A
authors.initials: A
authors.lastname: Azzi
mesh_terms: D000595:Amino Acid Sequence; D003300:Copper / Q000737:chemistry; D003576:Electron Transport Complex IV / Q000737:chemistry / Q000378:metabolism*; D006418:Heme / Q000737:chemistry; D008670:Metals / Q000737:chemistry*; D008969:Molecular Sequence Data; D010231:Paracoccus denitrificans / Q000201:enzymology*; D011487:Protein Conformation
chemical_list: D008670:Metals; D006418:Heme; D003300:Copper; D003576:Electron Transport Complex IV