Cytochrome cbb(3) oxidase and bacterial microaerobic metabolism.
Cytochrome cbb(3) 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 cbb(3) 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 (E(m)<+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.
Pitcher
R S
RS
Centre for Metalloprotein Spectroscopy and Biology, School of Biological Sciences, University of East Anglia, Norwich NR4 7TJ, UK. r.pitcher@uea.ac.uk
Brittain
T
T
Watmough
N J
NJ
D000332:Aerobiosis; D001419:Bacteria / Q000201:enzymology*; D002248:Carbon Monoxide / Q000378:metabolism; D003576:Electron Transport Complex IV / Q000235:genetics / Q000378:metabolism*; D009876:Operon; D010101:Oxygen Consumption; D011485:Protein Binding; D011549:Pseudomonas / Q000201:enzymology*
D002248:Carbon Monoxide; C414443:cbb3 oxidase; D003576:Electron Transport Complex IV