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

✍ Scribed by Tadahiko Mashino; Shigeo Nakamura; Masaaki Hirobe

• Publisher: Elsevier Science
• Year: 1990
• Tongue: French
• Weight: 270 KB
• Volume: 31
• Category: Article
• ISSN: 0040-4039
• DOI: 10.1016/s0040-4039(00)94722-1

✦ Synopsis

Snmmary : Heme-undecapeptide, microperoxidase-11, prepared from cyto&rome c by pepsin digestion, retains the proximal 6th 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 HzOz. Microperoxidase, MP-11, heme-undecapeptide, is easily prepared by the enzymatic hydrolysis of cytochrome c .i.z) MP-11 retains amino-acid residues 11 -21, including the proximal His-18 and two thioether bonds between iron-protoporphyrin M and two Cys residues.