FTIR study of conformational substates in the CO adduct of cytochrome c oxidase from Rhodobacter sphaeroides.

@article{Mitchell1996FTIRSO,
  title={FTIR study of conformational substates in the CO adduct of cytochrome c oxidase from Rhodobacter sphaeroides.},
  author={David M Mitchell and J. S. Bauer S. Virmani D. K. Mueller and Robert B Gennis and Gerd Ulrich Nienhaus},
  journal={Biochemistry},
  year={1996},
  volume={35 51},
  pages={16782-8}
}
Fourier transform infrared (FTIR) spectroscopy of cytochrome c oxidase from Rhodobacter sphaeroides reveals multiple CO stretch bands that are associated with different conformational substates of the enzyme. Here we report the temperature dependence of the infrared bands for the CO bound to the Fea3 heme iron and to CuB. We have also studied the kinetics of ligand return from Fea3 to CuB using temperature derivative spectroscopy (TDS). Two classes of substates (alpha/beta) can be distinguished… CONTINUE READING