Unlocking the catalytic precision of ligand-controlled enzymatic halogenation.

ABSTRACT: A single-component flavin-dependent halogenase, AetF, has emerged as an attractive biocatalyst for catalyzing halogenation. However, its flavin chemistry remains unexplored and cannot be predicted due to its uniqueness in sequence and structure compared to other flavin-dependent monooxygenases. Here, we investigated the flavin reactions of AetF using transient kinetics. Our data revealed that NADP⁺ binding is required for formation of C4a-hydroperoxy flavin adenine dinucleotide (FAD) (FAD_C4aOOH), a key flavin-oxygen adduct required for generating a halogenating species. In the presence of NaBr without L-tryptophan, the flavin oxygen adduct intermediates [possibly FAD_C4aOOH and C4a-hydroxy FAD (FAD_C4aOH)] are highly stabilized (>4,000 s) before re

SUBMITTER: Phintha A 

PROVIDER: S-EPMC11725856 | biostudies-literature | 2025 Jan

REPOSITORIES: biostudies-literature