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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Oxygen activation and reduction in respiration: involvement of redox-active tyrosine 244.

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.[1]

References

  1. Oxygen activation and reduction in respiration: involvement of redox-active tyrosine 244. Proshlyakov, D.A., Pressler, M.A., DeMaso, C., Leykam, J.F., DeWitt, D.L., Babcock, G.T. Science (2000) [Pubmed]
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