Cytochrome cbb3 oxidase and bacterial microaerobic metabolism

Pitcher, R. S., Brittain, T. and Watmough, N. J. (2002) Cytochrome cbb3 oxidase and bacterial microaerobic metabolism. Biochemical Society Transactions, 30. pp. 653-658. ISSN 1470-8752

Full text not available from this repository.


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.

Item Type: Article
Faculty \ School: Faculty of Science > School of Biological Sciences
UEA Research Groups: Faculty of Science > Research Centres > Centre for Molecular and Structural Biochemistry
Faculty of Science > Research Groups > Molecular Microbiology
Depositing User: EPrints Services
Date Deposited: 01 Oct 2010 13:36
Last Modified: 21 Jul 2024 00:16
DOI: 10.1042/BST0300653

Actions (login required)

View Item View Item