Raman characterization of human leukocyte myeloperoxidase and bovine spleen green haemoprotein. Insight into chromophore structure and evidence that the chromophores of myeloperoxidase are equivalent.

@article{Babcock1985RamanCO,
  title={Raman characterization of human leukocyte myeloperoxidase and bovine spleen green haemoprotein. Insight into chromophore structure and evidence that the chromophores of myeloperoxidase are equivalent.},
  author={Gerald T. Babcock and Ronald Ingle and W Anthony Oertling and James Ch. Davis and Bruce A. Averill and C L Hulse and D J Stufkens and B G Bolscher and Ron Wever},
  journal={Biochimica et biophysica acta},
  year={1985},
  volume={828 1},
  pages={58-66}
}
Soret excitation resonance Raman spectroscopy has been used to characterize dimeric human leukocyte myeloperoxidase (donor:hydrogen peroxide oxidoreductase, EC 1.11.1.7) and monomeric bovine spleen green haemoprotein. The spectra of the two proteins, under the same conditions of iron valence and ligation, are essentially identical. Owing to strong symmetry reduction effects, the spectra are more complex than usually observed for haemoproteins. It is possible, however, to assign the high… CONTINUE READING