title: The nature of CuA in cytochrome c oxidase.
abstract: Kroneck et al. [(1988) FEBS Lett. 242, 70-74] have recently suggested, on the basis of a comparison with the EPR properties of nitrous oxide reductase, that cytochrome c oxidase contains a mixed-valence binuclear copper site, and that this is responsible for the EPR spectrum generally ascribed to CuA. Here we question this hypothesis in view of a multitude of analytical and spectroscopic data available. We maintain that a mononuclear Cu site with two cysteine sulfur and two imidazole nitrogen atoms as ligands is consistent with the current experimental information on the CuA site.
authors.affiliation: Arthur Amos Noyes Laboratory of Chemical Physics, California Institute of Technology, Pasadena 91125.
authors.forename: P M
authors.initials: PM
authors.lastname: Li
authors.forename: B G
authors.initials: BG
authors.lastname: Malmström
authors.forename: S I
authors.initials: SI
authors.lastname: Chan
mesh_terms: D001665:Binding Sites; D003300:Copper / Q000032:analysis*; D003545:Cysteine / Q000032:analysis; D004578:Electron Spin Resonance Spectroscopy; D003576:Electron Transport Complex IV / Q000032:analysis*; D007093:Imidazoles / Q000032:analysis; D010088:Oxidoreductases / Q000032:analysis; D013455:Sulfur / Q000032:analysis
chemical_list: D007093:Imidazoles; D013455:Sulfur; D003300:Copper; C029899:imidazole; D010088:Oxidoreductases; C022763:nitrous oxide reductase; D003576:Electron Transport Complex IV; D003545:Cysteine