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.
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Conference Article|
August 01 2002
Cytochrome cbb3 oxidase and bacterial microaerobic metabolism
R. S. Pitcher;
R. S. Pitcher
1
*Centre for Metalloprotein Spectroscopy and Biology, School of Biological Sciences, University of East Anglia, Norwich NR4 7TJ, U.K.
1To whom correspondence should be addressed (e-mail r.pitcher@uea.ac.uk)
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T. Brittain;
T. Brittain
†School of Biological Sciences, University of Auckland, Private Bag 92019, Auckland, New Zealand
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N. J. Watmugh
N. J. Watmugh
*Centre for Metalloprotein Spectroscopy and Biology, School of Biological Sciences, University of East Anglia, Norwich NR4 7TJ, U.K.
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Publisher: Portland Press Ltd
Received:
March 28 2002
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© 2002 Biochemical Society
2002
Biochem Soc Trans (2002) 30 (4): 653–658.
Article history
Received:
March 28 2002
Citation
R. S. Pitcher, T. Brittain, N. J. Watmugh; Cytochrome cbb3 oxidase and bacterial microaerobic metabolism. Biochem Soc Trans 1 August 2002; 30 (4): 653–658. doi: https://doi.org/10.1042/bst0300653
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