A Novel Versatility of Catalase I as a Dioxygenase for Indole - ring - opening Dioxygenation
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