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1. ChemInform Abstract: A Novel Versatility of Catalase I as a Dioxygenase for Indole-Ring-Opening Dioxygenation

Author

Yuka Takeda, Shin Ichi Tsugawa, Hirotaka Ihara, Takashi Sagawa, Tetsuya Yomo, Katsutoshi Ohkubo, Itaru Urabe, and Elizabeth Ko Mitamura

Subjects
Indole test, biology, Protoporphyrin IX, Chemistry, Stereochemistry, Tryptophan, Wild type, Bacillus, General Medicine, biology.organism_classification, chemistry.chemical_compound, Catalase, Dioxygenase, biology.protein, Selectivity
Abstract

Catalase I (wild type) from Bacillus stearothermophilus, which was found to have catalase activity, catalyzed dioxygen-inserted indole-ring opening reaction of methyl N-acetyl L-tryptophanate as tryptophan 2,3-dioxygenase (TDO) model in the presence of Na2S2O4. Heme-reconstruction with protoporphyrin IX manganese(III) chloride (MnClPP) via 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).

Published
2010
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