title: What's new in enzymatic halogenations.
abstract: The halogenation of thousands of natural products occurs during biosynthesis and often confers important functional properties. While haloperoxidases had been the default paradigm for enzymatic incorporation of halogens, via X+ equivalents into organic scaffolds, a combination of microbial genome sequencing, enzymatic studies and structural biology have provided deep new insights into enzymatic transfer of halide equivalents in three oxidation states. These are (1) the halide ions (X-) abundant in nature, (2) halogen atoms (X*), and (3) the X+ equivalents. The mechanism of halogen incorporation is tailored to the electronic demands of specific substrates and involves enzymes with distinct redox coenzyme requirements.
authors: Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115, USA.
authors: Danica Galonić
authors: DG
authors: Fujimori
authors: Christopher T
authors: CT
authors: Walsh
mesh_terms: D001688:Biological Products / Q000378:metabolism; D054879:Halogenation; D010084:Oxidation-Reduction; D010544:Peroxidases / Q000378:metabolism*
chemical_list: D001688:Biological Products; D010544:Peroxidases