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

Tadahiko Mashino, Shigeo Nakamura, Masaaki Hirobe

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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 heroin-Cl, mieroperoxidase-11 was an effective catalyst for sulfide oxidation, amine N-demethylation, and olefin oxidation in the presence of H2O2.

Original languageEnglish
Pages (from-to)3163-3166
Number of pages4
JournalTetrahedron Letters
Issue number22
Publication statusPublished - 1990


ASJC Scopus subject areas

  • Biochemistry
  • Drug Discovery
  • Organic Chemistry

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