9kuh
From Proteopedia
Co-crystal structure of wild-type OYE2 with 2-(prop-1-en-2-yl)pyridine
Structural highlights
FunctionOYE2_YEAST Flavin-dependent enoate reductase that catalyzes the chemo- and stereoslective hydrogenation of electron-poor alkenes. The enzyme is reduced by NADPH, and oxygen, quinones, and alpha,beta-unsaturated aldehydes and ketones can act as electron acceptors to complete catalytic turnover. The physiological oxidant remains elusive (By similarity). Has an antioxidant activity, reducing reactive oxygen species (ROS) levels when overexpressed. Formation of OYE2-OYE3 heterodimers contribute to the induction of programmed cell death upon oxidative stress (PubMed:17897954).[UniProtKB:Q02899][1] Publication Abstract from PubMedOrganic nitriles are significant in pharmaceuticals, agrochemicals, cosmetics, and materials. Although numerous cyanidation methods have been developed, more eco-friendly and green protocols for manufacturing alkyl nitriles are in high demand. Here, we report a photoenzymatic enantioselective intermolecular hydrocyanoalkylation of alkenes catalyzed by flavin-dependent "ene"-reductases. The discovery of stereocomplementary enzymes that provide access to both enantiomers of the high-value nitriles further showcases the synthetic applications of this method. Radical trapping, isotopic labeling, and spectroscopic experiments have elucidated the formation of a charge transfer complex at the protein active site. The single-electron reduction of the cyanoalkyl radical precursor by flavin hydroquinone yields a cyanoalkyl radical, which then undergoes intermolecular radical addition. This active site can stereoselectively control the radical-terminating hydrogen atom transfer, enabling the synthesis of enantioenriched gamma-stereogenic nitriles. This work further expands the reactivity repertoire of biocatalytic transformations via non-natural radical mechanisms. Enantioselective Radical Hydrocyanoalkylation of Alkenes via Photoenzymatic Catalysis.,Wu D, Sun Z, Wang S, Yang J, He J, Lei X JACS Au. 2025 Jul 11;5(7):3625-3631. doi: 10.1021/jacsau.5c00633. eCollection , 2025 Jul 28. PMID:40747066[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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