title: Electron transfer and ligand binding in terminal oxidases. Impact of recent structural information.
abstract: A consensus structure for the active site of terminal oxidases has been recently proposed by Hosler et al. [(1993) J. Bioenerg. Biomem. 25, 121-135]. We exploit the novel structural information to propose a hypothesis for the large difference in the rate of internal electron transfer found when experiments are started either with the reduced or with the oxidized enzyme. This rationale also allows us to discuss the oxidation state of the prevailing oxygen reacting species with reference to the concentration of the two substrates (oxygen and cytochrome c) and to the structural state of the oxidase.
authors.affiliation: Department of Biochemical Sciences, Universities of Rome La Sapienza, Italy.
authors.forename: M
authors.initials: M
authors.lastname: Brunori
authors.forename: G
authors.initials: G
authors.lastname: Antonini
authors.forename: A
authors.initials: A
authors.lastname: Giuffre
authors.forename: F
authors.initials: F
authors.lastname: Malatesta
authors.forename: F
authors.initials: F
authors.lastname: Nicoletti
authors.forename: P
authors.initials: P
authors.lastname: Sarti
authors.forename: M T
authors.initials: MT
authors.lastname: Wilson
mesh_terms: D000595:Amino Acid Sequence; D001665:Binding Sites; D004579:Electron Transport; D003576:Electron Transport Complex IV / Q000737:chemistry*; D008024:Ligands; D008969:Molecular Sequence Data; D010084:Oxidation-Reduction
chemical_list: D008024:Ligands; D003576:Electron Transport Complex IV