BesC Initiates C-C Cleavage through a Substrate-Triggered and Reactive Diferric-Peroxo Intermediate.

ABSTRACT: BesC catalyzes the iron- and O₂-dependent cleavage of 4-chloro-l-lysine to form 4-chloro-l-allylglycine, formaldehyde, and ammonia. This process is a critical step for a biosynthetic pathway that generates a terminal alkyne amino acid which can be leveraged as a useful bio-orthogonal handle for protein labeling. As a member of an emerging family of diiron enzymes that are typified by their heme oxygenase-like fold and a very similar set of coordinating ligands, recently termed HDOs, BesC performs an unusual type of carbon-carbon cleavage reaction that is a significant departure from reactions catalyzed by canonical dinuclear-iron enzymes. Here, we show that BesC activates O₂ in a substrate-gated manner to generate a diferric-peroxo intermediate. Examination of the rea

SUBMITTER: Manley OM 

PROVIDER: S-EPMC8876372 | biostudies-literature | 2021 Dec

REPOSITORIES: biostudies-literature