A Novel Versatility of Catalase I as a Dioxygenase for Indole - ring - opening Dioxygenation
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Catalase I (wild type) from <I>Bacillus stearothermophilus</I>, which was found to have catalase activity, catalyzed dioxygen-inserted indole-ring opening reaction of methyl <I>N</I>-acetyl L-tryptophanate as tryptophan 2,3-dioxygenase (TDO) model in the presence of Na<SUB>2</SUB>S<SUB>2</SUB>O<SUB>4</SUB>. Heme-reconstruction with protoporphyrin IX manganese(III) chloride (MnClPP) <I>via</I> annealing was examined and the reconstituted MnClPP-catalase I also revealed dioxygenolytic behaviour with higher TDO activity and higher selectivity than the catalase I (wild type).
- Chemistry Letters
Chemistry Letters 1999(4), 339-340, 1999-04-05
The Chemical Society of Japan