18O incorporation from H218O2 in the oxidation of N-methylcarbazole and sulfides catalyzed by microperoxidase-11

Shigeo Nakamura, Tadahiko Mashino, Masaaki Hirobe

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35 Citations (Scopus)


Microperoxidase-11 (MP-11), prepared by pepsin digestion of cytochrome c, contains protoheme IX and one proximal histidine ligand. MP-11 oxygenated N-methylcarbazole, methyl phenyl sulfide, and phenacyl phenyl sulfide with 80%, 100%, and 96% 18O atom incorporation from H218O2, respectively. These results indicate that the oxygen atom on heme iron of MP-11 immediately rebinds to one-electron-oxidized intermediates of the substrates and that MP-11 catalyzes N-demethylation through a cytochrome P-450-like mechanism rather than a peroxidase-like mechanism.

Original languageEnglish
Pages (from-to)5409-5412
Number of pages4
JournalTetrahedron Letters
Issue number37
Publication statusPublished - 1992 Sep 8
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Drug Discovery
  • Organic Chemistry


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