Spectroscopic characterization of cytochrome ba3, a terminal oxidase from Thermus thermophilus: comparison of the a3/CuB site to that of bovine cytochrome aa3.

@article{Oertling1994SpectroscopicCO,
  title={Spectroscopic characterization of cytochrome ba3, a terminal oxidase from Thermus thermophilus: comparison of the a3/CuB site to that of bovine cytochrome aa3.},
  author={W Anthony Oertling and Kristene K. Surerus and {\'O}l{\"o}f Einarsd{\'o}ttir and James A. Fee and R. Brian Dyer and William H. Woodruff},
  journal={Biochemistry},
  year={1994},
  volume={33 10},
  pages={3128-41}
}
Unliganded and cyano derivatives of cytochrome ba3 from Thermus thermophilus have been examined by UV-vis, EPR, and resonance Raman spectroscopies. Species of cytochrome ba3 investigated include its resting, as-isolated, fully oxidized state, the fully reduced, unliganded enzyme, the one-electron-reduced cyano complex, the three-electron-reduced cyano complex, and the fully reduced cyano complex. Results are compared to those obtained from similar adducts of bovine cytochrome aa3, in particular… CONTINUE READING