1999年4月
A novel versatility of catalase I as a dioxygenase for indole-ring-opening dioxygenation
CHEMISTRY LETTERS
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- 巻
- 号
- 4
- 開始ページ
- 339
- 終了ページ
- 340
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1246/cl.1999.339
- 出版者・発行元
- CHEMICAL SOC JAPAN
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).
- リンク情報
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- DOI
- https://doi.org/10.1246/cl.1999.339
- J-GLOBAL
- https://jglobal.jst.go.jp/detail?JGLOBAL_ID=200902188529166169
- CiNii Articles
- http://ci.nii.ac.jp/naid/10004340995
- Web of Science
- https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000080069200033&DestApp=WOS_CPL
- ID情報
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- DOI : 10.1246/cl.1999.339
- ISSN : 0366-7022
- eISSN : 1348-0715
- J-Global ID : 200902188529166169
- CiNii Articles ID : 10004340995
- Web of Science ID : WOS:000080069200033