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    Protein Sci. 1999 May;8(5):985-90.

    Evidence for a copper-coordinated histidine-tyrosine cross-link in the active site of cytochrome oxidase.

    Buse G, Soulimane T, Dewor M, Meyer HE, Blüggel M.

    Institut für Biochemie, Rheinisch-Westfälische Technische Hochschule Aachen, Germany. GerhardBuse@post.rwth-aachen.de

    Following hints from X-ray data (Ostermeier C et al., 1997, Proc Natl Acad Sci USA 94:10547-10553; Yoshikawa S et al., 1998, Science 280: 1723-1729), chemical evidence is presented from four distantly related cytochrome-c oxidases for the existence of a copperB-coordinated His240-Tyr244) cross-link at the O2-activating Heme Fea3-CuB center in the catalytic subunit 1 of the enzyme. The early evolutionary invention of this unusual structure may have prevented damaging *OH-radical release at e(-)-transfer to dioxygen and thus have enabled O2 respiration.

    PMID: 10338009 [PubMed - indexed for MEDLINE]

    PMCID: 2144334

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