The nature of CuA in cytochrome c oxidase.
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.
Li
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PM
Arthur Amos Noyes Laboratory of Chemical Physics, California Institute of Technology, Pasadena 91125.
Malmström
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Chan
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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
D007093:Imidazoles; D013455:Sulfur; D003300:Copper; C029899:imidazole; D010088:Oxidoreductases; C022763:nitrous oxide reductase; D003576:Electron Transport Complex IV; D003545:Cysteine