A Well-Defined Osmium–Cupin Complex: Hyperstable Artificial Osmium Peroxygenase
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- Nobutaka Fujieda
- Department of Material and Life Science, Graduate School of Engineering, Osaka University, 2-1 Yamada-oka, Suita, Osaka 565-0871, Japan
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- Takumi Nakano
- Department of Material and Life Science, Graduate School of Engineering, Osaka University, 2-1 Yamada-oka, Suita, Osaka 565-0871, Japan
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- Yuki Taniguchi
- Department of Material and Life Science, Graduate School of Engineering, Osaka University, 2-1 Yamada-oka, Suita, Osaka 565-0871, Japan
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- Haruna Ichihashi
- Department of Material and Life Science, Graduate School of Engineering, Osaka University, 2-1 Yamada-oka, Suita, Osaka 565-0871, Japan
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- Hideki Sugimoto
- Department of Material and Life Science, Graduate School of Engineering, Osaka University, 2-1 Yamada-oka, Suita, Osaka 565-0871, Japan
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- Yuma Morimoto
- Department of Material and Life Science, Graduate School of Engineering, Osaka University, 2-1 Yamada-oka, Suita, Osaka 565-0871, Japan
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- Yosuke Nishikawa
- Institute for Protein Research, Osaka University, 3-2 Yamada-oka, Suita, Osaka 565-0871, Japan
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- Genji Kurisu
- Institute for Protein Research, Osaka University, 3-2 Yamada-oka, Suita, Osaka 565-0871, Japan
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- Shinobu Itoh
- Department of Material and Life Science, Graduate School of Engineering, Osaka University, 2-1 Yamada-oka, Suita, Osaka 565-0871, Japan
書誌事項
- 公開日
- 2017-04-03
- 資源種別
- journal article
- DOI
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- 10.1021/jacs.7b00675
- 公開者
- American Chemical Society (ACS)
この論文をさがす
説明
Thermally stable TM1459 cupin superfamily protein from Thermotoga maritima was repurposed as an osmium (Os) peroxygenase by metal-substitution strategy employing the metal-binding promiscuity. This novel artificial metalloenzyme bears a datively bound Os ion supported by the 4-histidine motif. The well-defined Os center is responsible for not only the catalytic activity but also the thermodynamic stability of the protein folding, leading to the robust biocatalyst (T
収録刊行物
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- Journal of the American Chemical Society
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Journal of the American Chemical Society 139 (14), 5149-5155, 2017-04-03
American Chemical Society (ACS)
