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

Protein Sci. 1999 May;8(5):985-90. doi: 10.1110/ps.8.5.985.

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 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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Cattle
  • Copper / chemistry*
  • Electron Transport Complex IV / chemistry*
  • Histidine / chemistry*
  • Mass Spectrometry
  • Models, Chemical
  • Models, Molecular
  • Molecular Sequence Data
  • Oxygen Consumption
  • Paracoccus denitrificans / chemistry
  • Tyrosine / chemistry*

Substances

  • Tyrosine
  • Histidine
  • Copper
  • Electron Transport Complex IV