期刊
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
卷 58, 期 26, 页码 8714-8718出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201902005
关键词
enzymes; biocatalysis; hydrogen atom transfer; photochemistry; reduction
资金
- NIH-NIGMS [R01 GM127703]
- Searle Scholars Award [SSP-2017-1741]
- Sloan Research Fellowship
- Princeton Catalysis Initiative
- Princeton University
- EdwardC. Taylor Fellowship
Flavin-dependent ene-reductases (EREDs) are known to stereoselectively reduce activated alkenes, but are inactive toward carbonyls. Demonstrated here is that in the presence of photoredox catalysts, these enzymes will reduce aromatic ketones. Mechanistic experiments suggest this reaction proceeds through ketyl radical formation, a reaction pathway that is distinct from the native hydride-transfer mechanism. Furthermore, this reactivity is accessible without modification of either the enzyme or cofactors, allowing both native and non-natural mechanisms to occur simultaneously. Based on control experiments, we hypothesize that binding to the enzyme active site attenuates the reduction potential of the substrate, enabling single-electron reduction. This reactivity highlights opportunities to access new catalytic manifolds by merging photoredox catalysis with biocatalysis.
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