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Raman characterization of human leukocyte myeloperoxidase ec 1.11.1.7 and bovine spleen green hemoprotein insight into chromophore structure and evidence that the chromophores of myeloperoxidase are equivalent



Raman characterization of human leukocyte myeloperoxidase ec 1.11.1.7 and bovine spleen green hemoprotein insight into chromophore structure and evidence that the chromophores of myeloperoxidase are equivalent



Biochimica et Biophysica Acta 828(1): 58-66



Soret excitation resonance Raman spectroscopy was used to characterize dimeric human leukocyte myeloperoxidase (donor:hydrogen peroxide oxidoreductase, EC 1.11.1.7) and monomeric bovine spleen green hemoprotein. The spectra of the 2 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 hemoproteins. It is possible, however, to assign the high-frequency vibrations and, from these assignments, to determine structural features of the Fe chromophores. In the resting protein, the Fe adopts a 6-coordinate high-spin configuration in both proteins; HCN addition produces 6-coordinate low-spin species, and ferrous enzymes the Fe appears to be 5-coordinate and high-spin. The proteins are stable to laser excitation and do not photoreduce under illumination. No evidence is found for unusual peripheral substituents, such as formyl or protonated Schiff's base group, in conjugation with the main chromophore in the native protein. The vibrational data are consistent with an iron chlorin chromophore, although outer electronic effects, in addition to those produced by porphyrin ring reduction, are necessary to account for the optical properties of the proteins. The similarity in Raman spectra for myeloperoxidase and green hemoprotein indicates that the 2 Fe sites in myeloperoxidase are equivalent.

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