Indole Hydroxylation by Bacterial Cytochrome P450 BM-3 and Modulation of Activity by Cumene Hydroperoxide
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概要
- 論文の詳細を見る
Cytochrome P450 BM-3 from Bacillus megaterium catalyzed NADPH-supported indole hydroxylation under alkaline conditions with homotropic cooperativity toward indole. The activity was also found with the support of H2O2, tert-butyl hydroperoxide (tBuOOH), or cumene hydroperoxide (CuOOH). Enhanced activity and heterotropic cooperativity were observed in CuOOH-supported hydroxylation, and both the Hill coefficient and substrate concentration required for half-maximal activity in the CuOOH-supported reaction were much lower than those in the H2O2-, tBuOOH-, or NADPH-supported reactions. CuOOH greatly enhanced NADPH consumption and indole hydroxylation in the NADPH-supported reaction. However, when CuOOH was replaced by tBuOOH or H2O2, heterotropic cooperativity was not observed. Spectral studies also confirmed that CuOOH stimulated indole binding to P450 BM-3. Interestingly, a mutant enzyme with enhanced indole-hydroxylation activity, F87V (Phe87 was replaced by Val), lost homotropic cooperativity towards indole and heterotropic cooperativity towards CuOOH, indicating that the active-site structure affects the cooperativities.
- 社団法人 日本農芸化学会の論文
- 2005-02-23
著者
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Shimizu Sakayu
Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University
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Ogawa Jun
Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University
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Shimizu S
Agricultural Sciences Kyoto University
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Shimizu Sakayu
Division Of Applied Life Science Graduate School Of Agriculture Kyoto University
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Ogawa Jun
Division Of Applied Life Sciences Graduate School Of Agriculture Kyoto University
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LI Qing-Shan
Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University
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SCHMID Rolf
Institut fur Technische Biochemie, Universitat Stuttgart
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Li Qing-shan
Division Of Applied Life Sciences Graduate School Of Agriculture Kyoto University
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Schmid Rolf
Institut Fur Technische Biochemie Universitat Stuttgart
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SCHMID Rolf
Institut für Technische Biochemie, Universität Stuttgart
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