ChemBioChem · 2001 · 37 citations · 20 references
Natural SciencesBiochemistryChemistryBiocatalysisCatalysisRedox BiochemistryCatalytic MechanismsOxidation ReactionsOxidation-reduction ReactionsRedox ChemistryRedox EnzymesRedox ProcessesActive Site AnalysisCatalyst MechanismsCatalytic ActivityCatalytic Activity EnhancementOxidase CatalysisOxygen Reduction ReactionPorphyrin Redox ChemistryStructured Catalysts
Functional analogues of the so-called Fea3–CuB active site of cytochrome c oxidase were synthesized to elucidate the mechanism of the reduction of O2 to H2O. The role of each individual structural component, especially the CuB center, for catalytic activity was investigated. These quinolinoyl picket iron porphyrins (see picture) were shown to be efficient catalysts for the 4 e− reduction of dioxygen to water with or without a Cu ion in their distal site, clearly demonstrating that the Cu center is not essential for the catalytic activity.
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The Whole Structure of the 13-Subunit Oxidized Cytochrome c Oxidase at 2.8 Å
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Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans
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Structures of Metal Sites of Oxidized Bovine Heart Cytochrome c Oxidase at 2.8 Å
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