Structural characterization of cytochrome c peroxidase by resonance Raman scattering.

@article{Dasgupta1989StructuralCO,
  title={Structural characterization of cytochrome c peroxidase by resonance Raman scattering.},
  author={Siddharth Dasgupta and Denis L. Rousseau and H Anni and Takashi Yonetani},
  journal={The Journal of biological chemistry},
  year={1989},
  volume={264 1},
  pages={654-62}
}
Resonance Raman scattering studies are reported on freshly prepared and aged ferric, ligand-free ferrous, and CO-bound ferrous cytochrome c peroxidase. The ferric form of the fresh enzyme has a heme which is penta-coordinate high spin, independent of buffer over the pH range 4.3-7, as determined by well established Raman marker lines. The aged enzyme displays a mixture of spin and coordination states, but it can be stabilized in the penta-coordinate high spin form in the presence of phosphate… CONTINUE READING