ArticleJournal of the American Chemical Society2026
How Fe(II)/2-Oxoglutarate Oxygenase Chooses Chlorination over Hydroxylation: Electric Field-Driven Ligand Exchange Governs C-Cl Formation.
Article in Journal of the American Chemical Society, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Non-heme Fe(II)/2-oxoglutarate (2OG)-dependent halogenases catalyze highly selective C-H halogenation. BesD is a non-heme Fe(II)/2OG halogenase that performs regio- and stereoselective chlorination of the l-lysine (l-Lys) substrate. Understanding the mechanism by which halogenation is favored over canonical hydroxylation is essential for guiding enzyme engineering efforts aimed at converting hydroxylases into halogenases. Here, we combine molecular dynamics (MD) and hybrid quantum mechanics/molecular mechanics (QM/MM) calculations to elucidate the origin of chlorination selectivity in BesD and variants derived from a homologous hydroxylase. Our results indicate that, although the initial inline Cl-Fe(III)-OH intermediate is inherently predisposed toward hydroxylation, it undergoes a two-step isomerization in which the -Cl and -OH ligands exchange coordination positions. This rearrangement positions the chloride ligand
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