title: Comparative studies in series of cytochrome c oxidase models.
abstract: This study compares the behavior as cytochrome c oxidase (CcO) functional and structural models of a series of reported and unreported ligands that provide either a binding site for copper without a built-in proximal base, or both a flexible binding site for copper and a built-in proximal base, or a fixed binding site for copper with a built-in proximal base. The comparisons of the models show that the relative position of the two metal sites is not only a crucial parameter in the control of the catalytic behavior but also essential in mimicking other features of the enzyme such as CO exchange between the ferrous heme a(3) and the cuprous Cu(B) center.
authors.affiliation: Spectroscopie vibrationnelle et électrochimie des biomolécules, Institut de Chimie de Strasbourg, UMR 7177 CNRS, Université de Strasbourg, Strasbourg, France. fmelin@unistra.fr
authors.forename: F
authors.initials: F
authors.lastname: Melin
authors.forename: A
authors.initials: A
authors.lastname: Trivella
authors.forename: M
authors.initials: M
authors.lastname: Lo
authors.forename: C
authors.initials: C
authors.lastname: Ruzié
authors.forename: I
authors.initials: I
authors.lastname: Hijazi
authors.forename: N
authors.initials: N
authors.lastname: Oueslati
authors.forename: J A
authors.initials: JA
authors.lastname: Wytko
authors.forename: B
authors.initials: B
authors.lastname: Boitrel
authors.forename: C
authors.initials: C
authors.lastname: Boudon
authors.forename: P
authors.initials: P
authors.lastname: Hellwig
authors.forename: J
authors.initials: J
authors.lastname: Weiss
mesh_terms: D001665:Binding Sites; D003300:Copper / Q000737:chemistry; D004563:Electrochemistry / Q000379:methods; D003576:Electron Transport Complex IV / Q000737:chemistry* / Q000378:metabolism*; D006418:Heme / Q000737:chemistry; D008670:Metals / Q000737:chemistry
chemical_list: D008670:Metals; D006418:Heme; D003300:Copper; D003576:Electron Transport Complex IV