Interactions of sulphide and other ligands with cytochrome c oxidase. An electron-paramagnetic-resonance study.

@article{Hill1984InteractionsOS,
  title={Interactions of sulphide and other ligands with cytochrome c oxidase. An electron-paramagnetic-resonance study.},
  author={Bruce C Hill and Tai Chin Woon and Peter Nicholls and Jim Peterson and C. Greenwood and Andrew James Thomson},
  journal={The Biochemical journal},
  year={1984},
  volume={224 2},
  pages={591-600}
}
The effect of sulphide on resting oxidized cytochrome c oxidase was studied by both e.p.r. and optical-absorption spectroscopy. Excess sulphide causes some reduction of cytochrome a, CuA and CuB, and the formation of the cytochrome a3-SH complex after about 1 min. After several hours in the presence of excess sulphide only the e.p.r. signals due to low-spin ferricytochrome a3-SH persist, giving a partially reduced species. Re-oxidation of this partially reduced sulphide-bound enzyme by… CONTINUE READING

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