Oxygen-linked equilibrium CuB-CO species in cytochrome ba3 oxidase from thermus thermophilus. Implications for an oxygen channel ar the CuB site.

@article{Koutsoupakis2003OxygenlinkedEC,
  title={Oxygen-linked equilibrium CuB-CO species in cytochrome ba3 oxidase from thermus thermophilus. Implications for an oxygen channel ar the CuB site.},
  author={Konstantinos Koutsoupakis and Stavros Stavrakis and Tewfik Soulimane and Constantinos Varotsis},
  journal={The Journal of biological chemistry},
  year={2003},
  volume={278 17},
  pages={14893-6}
}
We report the first study of O(2) migration in the putative O(2) channel of cytochrome ba(3) and its effect to the properties of the binuclear heme a(3)-Cu(B) center of cytochrome ba(3) from Thermus thermophilus. The Fourier transform infrared spectra of the ba(3)-CO complex demonstrate that in the presence of 60-80 micro m O(2), the nu(C-O) of Cu(B)1+-C-O at 2053 cm(-1) (complex A) shifts to 2045 cm(-1) and remains unchanged in H(2)O/D(2)O exchanges and in the pH 6.5-9.0 range. The frequencies… CONTINUE READING