Cytochrome cbb3 oxidase and bacterial microaerobic metabolism

R. S. Pitcher, T. Brittain, N. J. Watmough

Research output: Contribution to journalArticlepeer-review

57 Citations (Scopus)

Abstract

Cytochrome cbb3 oxidase is a member of the haem-copper oxidase superfamily. It is characterized by its high oxygen affinity, while retaining the ability to pump protons. These attributes are central to its proposed role in bacterial microaerobic metabolism. Recent spectroscopic characterization of both the cytochrome cbb3 oxidase complex from Pseudomonas stutzeri and the dihaem ccoP subunit expressed separately in Escherichia coli has revealed the presence of a low-spin His/His co-ordinated c-type cytochrome. The low midpoint reduction potential of this haem (Em < + 100 mV), together with its unexpected ability to bind CO in the reduced state at the expense of the distal histidine ligand, raises questions about the role of the ccoP subunit in the delivery of electrons to the active site.
Original languageEnglish
Pages (from-to)653-658
Number of pages6
JournalBiochemical Society Transactions
Volume30
DOIs
Publication statusPublished - 2002

Cite this