Journal
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
Volume 58, Issue 26, Pages 8714-8718Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201902005
Keywords
enzymes; biocatalysis; hydrogen atom transfer; photochemistry; reduction
Categories
Funding
- NIH-NIGMS [R01 GM127703]
- Searle Scholars Award [SSP-2017-1741]
- Sloan Research Fellowship
- Princeton Catalysis Initiative
- Princeton University
- EdwardC. Taylor Fellowship
Ask authors/readers for more resources
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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available