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

Gerhard Buse, Tewfik Soulimane, Manfred Dewor, Helmut E. Meyer, Martin Blüggel

Research output: Contribution to journalArticlepeer-review

Abstract

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 copper(B)-coordinated His240-Tyr244) cross- link at the O2-activating Heme Fea3-Cu(B) center in the catalytic subunit I of the enzyme. The early evolutionary invention of this unusual structure may have prevented demaging ·OH-radical release at e--transfer to dioxygen and thus have enabled O2 respiration.

Original languageEnglish
Pages (from-to)985-990
Number of pages6
JournalProtein Science
Volume8
Issue number5
DOIs
Publication statusPublished - 1999
Externally publishedYes

Keywords

  • Cell respiration
  • Cytochrome-c oxidase
  • Histidine-tyrosine cross-link
  • O activation
  • Oxygen radicals

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