TY - JOUR
T1 - Sulfide oxidation, amine N-demethylation, and olefin oxidation by heme-undecapeptide, microperoxidase-11, in the presence of hydrogen peroxide
AU - Mashino, Tadahiko
AU - Nakamura, Shigeo
AU - Hirobe, Masaaki
N1 - Copyright:
Copyright 2014 Elsevier B.V., All rights reserved.
PY - 1990
Y1 - 1990
N2 - 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.
AB - 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.
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U2 - 10.1016/S0040-4039(00)94722-1
DO - 10.1016/S0040-4039(00)94722-1
M3 - Article
AN - SCOPUS:0025288760
SN - 0040-4039
VL - 31
SP - 3163
EP - 3166
JO - Tetrahedron Letters
JF - Tetrahedron Letters
IS - 22
ER -