The Active Sites of the Native Cytochrome-c Oxidase from Bovine Heart Mitochondria: EXAFS-Spectroscopic Characterization of a Novel Homobinuclear Copper Center (CuA) and of the Heterobinuclear Fea3-CuB Center

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  • Financial support from the Deutsche Forschungsgemeinschaft, the Bundesministerium für Forschung und Technologie, the European Union, and the Fonds der chemischen Industrie is gratefully acknowledged.

Abstract

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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 Cu[BOND]Cu distance of 2.46 Å is very short. The structure of the Fea3-CuB center was likewise determined.

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