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- 小野田 晃
- 大阪大学大学院工学研究科
書誌事項
- タイトル別名
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- A New Reductase Containing Non-natural Metal Active Site
抄録
One useful synthetic reaction missing from nature's toolbox is the direct hydrogenation of substrates using hydrogen. To create an enzyme that can directly reduce organic substrates with hydrogen, researchers have combined metal hydrogenation catalysts with proteins. A direct hydrogenation of olefins catalyzed by rhodium(I) bound to carbonic anhydrase (CA) was reported by Kazlauskas and the colleagues recently. They minimized nonspecific binding of rhodium by replacing histidine residues on the protein surface using site-directed mutagenesis or by chemically modifying the histidine residues. Hydrogenation catalyzed by their Rh-bound CA is slightly slower than for uncomplexed rhodium(I), but the protein environment induces stereoselectivity favoring cis-over trans-stilbene by about 20:1. This enzyme is the first cofactor-independent reductase that reduces organic molecules using hydrogen.
収録刊行物
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- Bulletin of Japan Society of Coordination Chemistry
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Bulletin of Japan Society of Coordination Chemistry 56 41-42, 2010
錯体化学会
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詳細情報 詳細情報について
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- CRID
- 1390282680273729664
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- NII論文ID
- 130000402354
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- ISSN
- 18831737
- 18826954
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- 本文言語コード
- ja
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- データソース種別
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- JaLC
- Crossref
- CiNii Articles
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- 抄録ライセンスフラグ
- 使用不可