The bacterial cytochrome cbb3 oxidases

Robert S. Pitcher, Nicholas J. Watmough

Research output: Contribution to journalArticlepeer-review

240 Citations (Scopus)

Abstract

Cytochrome cbb3 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 cbb3 oxidase allows human pathogens to colonise anoxic tissues and agronomically important diazotrophs to sustain N2 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.
Original languageEnglish
Pages (from-to)388-399
Number of pages12
JournalBiochimica Et Biophysica Acta-Bioenergetics
Volume1655
DOIs
Publication statusPublished - 2004

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