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Science 24 November 2000:
Vol. 290. no. 5496, pp. 1588 - 1591
DOI: 10.1126/science.290.5496.1588
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Reports

Oxygen Activation and Reduction in Respiration: Involvement of Redox-Active Tyrosine 244 

Denis A. Proshlyakov,1 Michelle A. Pressler,1 Catherine DeMaso,1 Joseph F. Leykam,2 David L. DeWitt,2 Gerald T. Babcock1*

Cytochrome oxidase activates and reduces O2 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 O2-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 FeIV&cjs0811;O/CuB2+-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.

1 Department of Chemistry and
2 Department of Biochemistry, Michigan State University, East Lansing, MI 48824, USA.
*   To whom correspondence should be addressed. E-mail: babcock{at}cem.msu.edu

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