EPR spectra of intestinal peroxidase are reported for the first time. The resting state of intestinal peroxidase exhibits only a high spin EPR spectrum with pH-dependent rhombicity. Addition of chloride shifts the equilibrium between an acidic and a neutral form of the enzyme. In contrast, resting lactoperoxidase shows EPR spectra of both low spin and high spin species, indicating a different heme environment between these two peroxidases. The high spin signal of lactoperoxidase consists of multiple components; the major component exhibits pH-dependent rhombicity similar to intestinal peroxidase and the equilibrium between the acidic and the neutral forms is also shifted by chloride ion. EPR features of the low spin cyanide complex of intestinal peroxidase and lactoperoxidase are compared with those of other hemeproteins, whose proximal axial ligands are known to be histidine residues. The g-values of the cyanide adducts of the mammalian peroxidases are similar. The relationship between the g-value anisotropy and imidazolate character of the proximal histidine is discussed.
ASJC Scopus subject areas
- Molecular Biology