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• W1997160871 endingPage "1591" @default.
• W1997160871 startingPage "1588" @default.
• W1997160871 abstract "Cytochrome oxidase activates and reduces O(2) to water to sustain respiration and uses the energy released to drive proton translocation and adenosine 5'-triphosphate synthesis. A key intermediate in this process, P, lies at the junction of the O(2)-reducing and proton-pumping functions. We used radioactive iodide labeling followed by peptide mapping to gain insight into the structure of P. We show that the cross-linked histidine 240-tyrosine 244 (His240-Tyr244) species is redox active in P formation, which establishes its structure as Fe(IV) = O/Cu(B)2+-H240-Y244. Thus, energy transfer from O2 to the protein moiety is used as a strategy to avoid toxic intermediates and to control energy utilization in subsequent proton-pumping events." @default.
• W1997160871 created "2016-06-24" @default.
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• W1997160871 date "2000-11-24" @default.
• W1997160871 modified "2023-10-18" @default.
• W1997160871 title "Oxygen Activation and Reduction in Respiration: Involvement of Redox-Active Tyrosine 244" @default.
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• W1997160871 doi "https://doi.org/10.1126/science.290.5496.1588" @default.
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