Escherichia coli flavohaemoglobin (Hmp) reduces cytochrome c and Fe(III)-hydroxamate K by electron transfer from NADH via FAD: sensitivity of oxidoreductase activity to haem-bound dioxygen.

@article{Poole1997EscherichiaCF,
  title={Escherichia coli flavohaemoglobin (Hmp) reduces cytochrome c and Fe(III)-hydroxamate K by electron transfer from NADH via FAD: sensitivity of oxidoreductase activity to haem-bound dioxygen.},
  author={Robert K. Poole and Nicola J. Rogers and R A D'mello and Martin N. Hughes and Yutaka Orii},
  journal={Microbiology},
  year={1997},
  volume={143 ( Pt 5)},
  pages={1557-65}
}
Escherichia coli flavohaemoglobin (Hmp) reduced purified mitochondrial cytochrome c aerobically in a reaction that was not substantially inhibited by superoxide dismutase, demonstrating that superoxide anion, the product of O2 reduction by Hmp, did not contribute markedly to cytochrome c reduction. Cytochrome c was reduced by Hmp even in the presence of 0.5 mM CO, when the haem B was locked in the ferrous, low-spin state, demonstrating that electron transfer to cytochrome c from NADH was via… CONTINUE READING

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Respiration

  • R. B. Gennis, V. Stewart
  • Escherichia coli and Salmonella : Cellular and…
  • 1996
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