The bacterial cytochrome cbb3 oxidases

Biochim Biophys Acta. 2004 Apr 12;1655(1-3):388-99. doi: 10.1016/j.bbabio.2003.09.017.

Abstract

Cytochrome cbb(3) oxidases are found almost exclusively in Proteobacteria, and represent a distinctive class of proton-pumping respiratory heme-copper oxidases (HCO) that lack many of the key structural features that contribute to the reaction cycle of the intensely studied mitochondrial cytochrome c oxidase (CcO). Expression of cytochrome cbb(3) oxidase allows human pathogens to colonise anoxic tissues and agronomically important diazotrophs to sustain N(2) fixation. We review recent progress in the biochemical characterisation of these distinctive oxidases that lays the foundation for understanding the basis of their proposed high affinity for oxygen, an apparent degeneracy in their electron input pathways and whether or not they acquired the ability to pump protons independently of other HCOs.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Bacteria / enzymology*
  • Bacteria / genetics
  • Carbon Monoxide / metabolism
  • Electrochemistry
  • Electron Spin Resonance Spectroscopy
  • Electron Transport Complex IV / chemistry*
  • Electron Transport Complex IV / genetics
  • Electron Transport Complex IV / metabolism*
  • Gene Expression
  • Genes, Bacterial
  • Heme / chemistry
  • Kinetics
  • Ligands
  • Proton Pumps / chemistry
  • Proton Pumps / metabolism
  • Pseudomonas stutzeri / enzymology
  • Pseudomonas stutzeri / genetics

Substances

  • Ligands
  • Proton Pumps
  • Heme
  • Carbon Monoxide
  • cbb3 oxidase
  • Electron Transport Complex IV