Structural analysis of myeloperoxidase by resonance Raman spectroscopy.

摘要: Soret excitation of canine myeloperoxidase (MPO) gives rise to a complex resonance Raman (RR) spectrum characterized by multiple bands in the core size and oxidation state marker regions. Relative intensities obtained 406- 454-nm laser were nearly identical temperature independent from 77 273 K. Spectra dithionite-reduced cyanide-coordinated derivatives are also reported. In native enzyme, there no detectable between 1620 1700 cm-1, indicating that hemes do not contain formyl substituents conjugation with macrocyclic ring. Excitation visible absorption band at 568 nm gave only very weakly resonance-enhanced spectra. The RR spectra interpreted within context other physical measurements indicate MPO contains two equivalent or chlorin prosthetic groups. Possible mechanistic consequences these structural features discussed.