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Title: The nature of CuA in cytochrome c oxidase. Author: Li PM, Malmström BG, Chan SI. Journal: FEBS Lett; 1989 May 08; 248(1-2):210-1. PubMed ID: 2542086. 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.[Abstract] [Full Text] [Related] [New Search]