Journal of Bioenergetics and Biomembranes

, Volume 30, Issue 1, pp 55–62

The Dinuclear Center of Cytochrome bo3 from Escherichia coli

  • Nicholas J. Watmough
  • Myles R. Cheesman
  • Clive S. Butler
  • Richard H. Little
  • Colin Greenwood
  • Andrew J. Thomson
Article

DOI: 10.1023/A:1020507511285

Cite this article as:
Watmough, N.J., Cheesman, M.R., Butler, C.S. et al. J Bioenerg Biomembr (1998) 30: 55. doi:10.1023/A:1020507511285

Abstract

For the study of the dinuclear center of heme-copper oxidases cytochrome bo3 from Escherichia coli offers several advantages over the extensively charactererized bovine cytochrome c oxidase. The availability of strains with enhanced levels of expression allows purification of the significant amounts of enzyme required for detailed spectroscopic studies. Cytochrome bo3 is readily prepared as the fast form, with a homogeneous dinuclear center which gives rise to characteristic broad EPR signals not seen in CcO. The absence of CuA and the incorporation of protohemes allows for a detailed interpretation of the MCD spectra arising from the dinuclear center heme o3. Careful analysis allows us to distinguish between small molecules that bind to heme o3, those which are ligands of CuB, and those which react to yield higher oxidation states of heme o3. Here we review results from our studies of the reactions of fast cytochrome bo3 with formate, fluoride, chloride, azide, cyanide, NO, and H2O2.

Escherichia coli Quinol oxidase cytochrome bocytochrome c oxidase nitric oxide reductase EPR spectroscopy MCD spectroscopy oxyferryl heme 

Copyright information

© Plenum Publishing Corporation 1998

Authors and Affiliations

  • Nicholas J. Watmough
    • 1
  • Myles R. Cheesman
    • 2
  • Clive S. Butler
    • 1
    • 2
  • Richard H. Little
    • 1
  • Colin Greenwood
    • 1
  • Andrew J. Thomson
    • 2
  1. 1.Centre for Metalloprotein Spectroscopy and Biology, School of Biological SciencesUniversity of East AngliaNorwichUnited Kingdom
  2. 2.Centre for Metalloprotein Spectroscopy and Biology, School of Chemical SciencesUniversity of East AngliaNorwichUnited Kingdom

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