FTIR studies of the CO and cyanide adducts of fully reduced bovine cytochrome c oxidase.

@article{Rich2001FTIRSO,
  title={FTIR studies of the CO and cyanide adducts of fully reduced bovine cytochrome c oxidase.},
  author={Peter J. Rich and Jacques Breton},
  journal={Biochemistry},
  year={2001},
  volume={40 21},
  pages={6441-9}
}
Photolysis spectra of the CO and cyanide adducts of reduced bovine cytochrome c oxidase have been studied by FTIR difference spectroscopy. Bound CO is predominantly in a single 1963 cm(-1) form whereas cyanide is bound in at least two forms (2058/2045 cm(-1)). These forms are pH-independent between pH 6.5 and 8.5, indicating that there is no titratable protonatable group that influences significantly their binding in this pH range. Photolysis spectra of the cyanide adduct have a positive band… CONTINUE READING

From This Paper

Figures, tables, results, connections, and topics extracted from this paper.