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• W2069276518 startingPage "769" @default.
• W2069276518 abstract "Cytochrome c oxidase (CcO) is the terminal enzyme of the respiratory chain. By reducing oxygen to water, it generates a proton gradient across the mitochondrial or bacterial membrane. Recently, two independent X-ray crystallographic studies ((Aoyama et al. Proc. Natl. Acad. Sci. USA 106 (2009) 2165–2169) and (Koepke et al. Biochim. Biophys. Acta 1787 (2009) 635–645)), suggested that a peroxide dianion might be bound to the active site of oxidized CcO. We have investigated this hypothesis by combining quantum chemical calculations with a re-refinement of the X-ray crystallographic data and optical spectroscopic measurements. Our data suggest that dianionic peroxide, superoxide, and dioxygen all form a similar superoxide species when inserted into a fully oxidized ferric/cupric binuclear site (BNC). We argue that stable peroxides are unlikely to be confined within the oxidized BNC since that would be expected to lead to bond splitting and formation of the catalytic P intermediate. Somewhat surprisingly, we find that binding of dioxygen to the oxidized binuclear site is weakly exergonic, and hence, the observed structure might have resulted from dioxygen itself or from superoxide generated from O2 by the X-ray beam. We show that the presence of O2 is consistent with the X-ray data. We also discuss how other structures, such as a mixture of the aqueous species (H2O + OH− and H2O) and chloride fit the experimental data." @default.
• W2069276518 created "2016-06-24" @default.
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• W2069276518 date "2011-07-01" @default.
• W2069276518 modified "2023-10-02" @default.
• W2069276518 title "A combined quantum chemical and crystallographic study on the oxidized binuclear center of cytochrome c oxidase" @default.
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• W2069276518 doi "https://doi.org/10.1016/j.bbabio.2010.12.016" @default.
• W2069276518 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/21211513" @default.
• W2069276518 hasPublicationYear "2011" @default.
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