18O incorporation from H2 18O2 in the oxidation of N-methylcarbazole and sulfides catalyzed by microperoxidase-11

Shigeo Nakamura, Tadahiko Mashino, Masaaki Hirobe

Research output: Contribution to journalArticle

34 Citations (Scopus)

Abstract

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 H2 18O2, 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
Volume33
Issue number37
DOIs
Publication statusPublished - 1992 Sep 8
Externally publishedYes

Fingerprint

Sulfides
Oxidation
Heme
Atoms
Pepsin A
Cytochromes c
Histidine
Cytochrome P-450 Enzyme System
Peroxidase
Digestion
Iron
Electrons
Oxygen
Ligands
N-methylcarbazole
microperoxidase
Substrates

ASJC Scopus subject areas

  • Biochemistry
  • Organic Chemistry
  • Drug Discovery

Cite this

18O incorporation from H2 18O2 in the oxidation of N-methylcarbazole and sulfides catalyzed by microperoxidase-11. / Nakamura, Shigeo; Mashino, Tadahiko; Hirobe, Masaaki.

In: Tetrahedron Letters, Vol. 33, No. 37, 08.09.1992, p. 5409-5412.

Research output: Contribution to journalArticle

@article{276fc5ba973f43ea9e6ca8bd2677f9aa,
title = "18O incorporation from H2 18O2 in the oxidation of N-methylcarbazole and sulfides catalyzed by microperoxidase-11",
abstract = "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 H2 18O2, 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.",
author = "Shigeo Nakamura and Tadahiko Mashino and Masaaki Hirobe",
year = "1992",
month = "9",
day = "8",
doi = "10.1016/S0040-4039(00)79107-6",
language = "English",
volume = "33",
pages = "5409--5412",
journal = "Tetrahedron Letters",
issn = "0040-4039",
publisher = "Elsevier Limited",
number = "37",

}

TY - JOUR

T1 - 18O incorporation from H2 18O2 in the oxidation of N-methylcarbazole and sulfides catalyzed by microperoxidase-11

AU - Nakamura, Shigeo

AU - Mashino, Tadahiko

AU - Hirobe, Masaaki

PY - 1992/9/8

Y1 - 1992/9/8

N2 - 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 H2 18O2, 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.

AB - 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 H2 18O2, 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.

UR - http://www.scopus.com/inward/record.url?scp=0026769003&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0026769003&partnerID=8YFLogxK

U2 - 10.1016/S0040-4039(00)79107-6

DO - 10.1016/S0040-4039(00)79107-6

M3 - Article

AN - SCOPUS:0026769003

VL - 33

SP - 5409

EP - 5412

JO - Tetrahedron Letters

JF - Tetrahedron Letters

SN - 0040-4039

IS - 37

ER -