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The Active Sites of the Native Cytochrome‐c Oxidase from Bovine Heart Mitochondria: EXAFS‐Spectroscopic Characterization of a Novel Homobinuclear Copper Center (Cu<sub>A</sub>) and of the Heterobinuclear Fe<sub>a3</sub>‐Cu<sub>B</sub> Center
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Citations
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References
1995
Year
Bioorganic ChemistryActive SitesExafs InvestigationsMolecular BiologyCucu DistanceMitochondrial BiologyRedox BiologyOxidative StressProtein FoldingBioorganometallic ChemistryBiological Inorganic ChemistryBiochemistryCua CenterBovine Heart MitochondriaNative Cytochrome‐c OxidaseStructural BiologyMitochondrial FunctionNatural SciencesMetalloproteinMetabolismMedicine
A novel homobinuclear Cu2 complex describes best the CuA center of the cytochrome-c oxidase from bovine heart mitochondria according to EXAFS investigations. In this complex, which contains two terminal histidine residues, two cysteine sulfur bridges, and probably a bridging oxygen donor function, the CuCu distance of 2.46 Å is very short. The structure of the Fea3-CuB center was likewise determined.
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