The haem b558 component of the cytochrome bd quinol oxidase complex from Escherichia coli has histidine-methionine axial ligation.

@article{Spinner1995TheHB,
  title={The haem b558 component of the cytochrome bd quinol oxidase complex from Escherichia coli has histidine-methionine axial ligation.},
  author={F Spinner and Myles R. Cheesman and Andrew James Thomson and T M Kaysser and Robert B Gennis and Qiu-he Peng and Jim Peterson},
  journal={The Biochemical journal},
  year={1995},
  volume={308 ( Pt 2)},
  pages={641-4}
}
The cytochrome bd ubiquinol oxidase from Escherichia coli is induced when the bacteria are cultured under microaerophilic or low-aeration conditions. This membrane-bound respiratory oxidase catalyses the two-electron oxidation of ubiquinol and the four-electron reduction of dioxygen to water. The oxidase contains three haem prosthetic groups: haem b558, haem b595 and haem d. Haem d is the oxygen binding site, and it is likely that haem d and b595 form a bimetallic site in the enzyme. Haem b558… CONTINUE READING
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