Insight into the active-site structure and function of cytochrome oxidase by analysis of site-directed mutants of bacterial cytochrome aa3 and cytochrome bo

Jonathan P. Hosler, Shelagh Ferguson-Miller, Melissa W. Calhoun, Jeffrey W. Thomas, John Hill, Laura Lemieux, Jixiang Ma, Christos Georgiou, John Fetter, James Shapleigh, Mary M.J. Tecklenburg, Gerald T. Babcock, Robert B. Gennis

Research output: Contribution to journalArticlepeer-review

Abstract

Cytochrome aa3 of Rhodobacter sphaeroides and cytochrome bo of E. coli are useful models of the more complex cytochrome c oxidase of eukaryotes, as demonstrated by the genetic, spectroscopic, and functional studies reviewed here. A summary of site-directed mutants of conserved residues in these two enzymes is presented and discussed in terms of a current model of the structure of the metal centers and evidence for regions of the protein likely to be involved in proton transfer. The model of ligation of the heme a3 (or o)-CuB center, in which both hemes are bound to helix X of subunit I, has important implications for the pathways and control of electron transfer.

Original languageEnglish (US)
Pages (from-to)121-136
Number of pages16
JournalJournal of Bioenergetics and Biomembranes
Volume25
Issue number2
DOIs
StatePublished - Apr 1993

Keywords

  • COFTIR
  • Cu ligands
  • Heme ligands
  • mitochondrial cytochrome c oxidase
  • oxidase superfamily
  • proton pumping

ASJC Scopus subject areas

  • Physiology
  • Cell Biology

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