The enzymatic generation of carbon–halogen bonds is a powerful strategy used by both
nature and synthetic chemists to tune the bioactivity, bioavailability and reactivity of …

The market sizes for halogenated compounds are huge; in contrast to synthetic chemical
alternatives, halogenating enzymes afford the highly regiospecific incorporation of a …

Nature has evolved halogenase enzymes to regioselectively halogenate a diverse range of
biosynthetic precursors, with the halogens introduced often having a profound effect on the …

Halogenating enzymes are increasingly attracting attention for biocatalytic C− H
functionalization. Despite its importance for synthetic chemistry, selective introduction of …

Naturally produced halogenated compounds are ubiquitous across all domains of life where
they perform a multitude of biological functions and adopt a diversity of chemical structures …

We previously reported that the halogenase RebH catalyzes selective halogenation of
several heterocycles and carbocycles, but product yields were limited by enzyme instability …

Enzymes are powerful catalysts for site-selective C–H bond functionalization. Identifying
suitable enzymes for this task and for biocatalysis in general remains challenging, however …

Non‐heme iron halogenases are synthetically valuable biocatalysts that are capable of
halogenating unactivated sp3‐hybridized carbon centers with high stereo‐and …

Simple halogen substituents frequently afford key structural features that account for the
potency and selectivity of natural products, including antibiotics and hormones. For example …

During the last 20 years, focus has shifted from haloperoxidases to flavin‐dependent and
non‐heme‐iron halogenases because of their proven involvement in the biosynthesis of …