Sulfide oxidation, amine N-demethylation, and olefin oxidation by heme-undecapeptide, microperoxidase-11, in the presence of hydrogen peroxide

Article abstract of DOI:10.1016/S0040-4039(00)94722-1

Heme-undecapeptide, microperoxidase-11, prepared from cytochrome c by pepsin digestion, retains the proximal 5th His-18 ligand. Microperoxidase is thought to be a unique peroxidase which does not have a substrate binding site. Compared with hemin-Cl, microperoxidase-11 was an effective catalyst for sulfide oxidation, amine N-demethylation, and olefin oxidation in the presence of H₂O₂.