SULFIDE OXIDATION, AMINE N-DEMETHYLATION, AND OLEFIN OXIDATION BY HEME-UNDECAPEPTIDE, MICROPEROXIDASE-11, IN THE PRESENCE OF HYDROGEN-PEROXIDE

被引：32

作者：

MASHINO, T

NAKAMURA, S

HIROBE, M

机构：

[1] Faculty of Pharmaceutical Sciences, University of Tokyo, Hongo, Bunkyo-ku, Tokyo

来源：

TETRAHEDRON LETTERS | 1990年 / 31卷 / 22期

关键词：

D O I：

10.1016/S0040-4039(00)94722-1

中图分类号：

O62 [有机化学];

学科分类号：

070303 ; 081704 ;

摘要：

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. © 1990.

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页码：3163 / 3166

页数：4

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