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The nature of CuA in cytochrome c oxidase
P M Li1, B G Malmström, S I Chan
1Arthur Amos Noyes Laboratory of Chemical Physics, California Institute of Technology, Pasadena 91125.
FEBS Letters
|May 8, 1989
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.