The steady-state mechanism of cytochrome c oxidase: redox interactions between metal centres.

@article{Mason2009TheSM,
  title={The steady-state mechanism of cytochrome c oxidase: redox interactions between metal centres.},
  author={Maria G. Mason and Peter Nicholls and Chris E. Cooper},
  journal={The Biochemical journal},
  year={2009},
  volume={422 2},
  pages={237-46}
}
The steady-state behaviour of isolated mammalian cytochrome c oxidase was examined by increasing the rate of reduction of cytochrome c. Under these conditions the enzyme's 605 (haem a), 655 (haem a3/CuB) and 830 (CuA) nm spectral features behaved as if they were at near equilibrium with cytochrome c (550 nm). This has implications for non-invasive tissue measurements using visible (550, 605 and 655 nm) and near-IR (830 nm) light. The oxidized species represented by the 655 nm band is bleached… CONTINUE READING
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237–246 (Printed in Great Britain) doi:10.1042/BJ20082220 SUPPLEMENTARY ONLINE DATA The steady-state mechanism of cytochrome c oxidase: redox interactions between metal centres

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