Deciphering the Unconventional Reduction of C=N Bonds by Old Yellow Enzymes Using QM/MM.

ABSTRACT: The reduction of C=X (X = N, O) bonds is a cornerstone in both synthetic organic chemistry and biocatalysis. Conventional reduction mechanisms usually involve a hydride ion targeting the less electronegative carbon atom. In a departure from this paradigm, our investigation into Old Yellow Enzymes (OYEs) reveals a mechanism involving transfer of hydride to the formally more electronegative nitrogen atom within a C=N bond. Beyond their known ability to reduce electronically activated C=C double bonds, e.g., in α, β-unsaturated ketones, these enzymes have recently been shown to reduce α-oximo-β-ketoesters to the corresponding amines. It has been proposed that this transformation involves two successive reduction steps and proceeds via imine intermediates formed by the reductive dehydration of

SUBMITTER: Sahrawat AS 

PROVIDER: S-EPMC10845114 | biostudies-literature | 2024 Feb

REPOSITORIES: biostudies-literature