TY - JOUR
T1 - Effective oxygen transfer reaction catalyzed by microperoxidase-11 during sulfur oxidation of dibenzothiophene
AU - Ichinose, Hirofumi
AU - Wariishi, Hiroyuki
AU - Tanaka, Hiroo
N1 - Funding Information:
This research was supported from the New Energy and Industrial Technology Development Organization (NEDO) of Japan (to H. W. and H. T.) and the Regional Science Promoter Program from the FUKUOKA Industry, Science & Technology Foundation (to H. W.). H.I. was supported by Research Fellowships of the Japan Society for the Promotion of Science for Young Scientists.
PY - 2002/3/13
Y1 - 2002/3/13
N2 - The catalytic conversion of dibenzothiophenen (DBT) to DBT-5-oxide was examined using microperoxidase-11 (MP-11) as well as a series of heme peroxidases such as horseradish, lignin and manganese peroxidases. MP-11 is a heme-containing oligopeptide obtained by enzymatic hydrolysis of horse heart cytochrome c. Among the catalysts examined, only MP-11 effectively oxidizes DBT to its oxide with an expense of hydrogen peroxide. The maximal oxidation rate was obtained in the aqueous media containing 30% methanol. During MP-11 catalyzed oxidation of DBT to DBT-5-oxide by phenylperacetic acid, phenylacetic acid was formed but not benzyl alcohol. This observation strongly suggested that MP-11 first reacts with peroxide to form compound I species. DBT oxidation by the MP-11/H2O2 system was then carried out either with H218O2 or under 18O2 atmosphere, indicating that the oxygen atom of DBT-5-oxide was derived from hydrogen peroxide but not from molecular oxygen or water. These results indicated that MP-11 oxidized DBT via the peroxygenation reaction, where the oxygen was transferred from the ferryl-oxy complex of the heme to DBT forming DBT-5-oxide.
AB - The catalytic conversion of dibenzothiophenen (DBT) to DBT-5-oxide was examined using microperoxidase-11 (MP-11) as well as a series of heme peroxidases such as horseradish, lignin and manganese peroxidases. MP-11 is a heme-containing oligopeptide obtained by enzymatic hydrolysis of horse heart cytochrome c. Among the catalysts examined, only MP-11 effectively oxidizes DBT to its oxide with an expense of hydrogen peroxide. The maximal oxidation rate was obtained in the aqueous media containing 30% methanol. During MP-11 catalyzed oxidation of DBT to DBT-5-oxide by phenylperacetic acid, phenylacetic acid was formed but not benzyl alcohol. This observation strongly suggested that MP-11 first reacts with peroxide to form compound I species. DBT oxidation by the MP-11/H2O2 system was then carried out either with H218O2 or under 18O2 atmosphere, indicating that the oxygen atom of DBT-5-oxide was derived from hydrogen peroxide but not from molecular oxygen or water. These results indicated that MP-11 oxidized DBT via the peroxygenation reaction, where the oxygen was transferred from the ferryl-oxy complex of the heme to DBT forming DBT-5-oxide.
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U2 - 10.1016/S0141-0229(01)00514-2
DO - 10.1016/S0141-0229(01)00514-2
M3 - Article
AN - SCOPUS:0037070477
SN - 0141-0229
VL - 30
SP - 334
EP - 339
JO - Enzyme and Microbial Technology
JF - Enzyme and Microbial Technology
IS - 3
ER -