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Exploring the chemistry and biology of vanadium-dependent haloperoxidases Winter JM; Moore BSJ Biol Chem 2009[Jul]; 284 (28): 18577-81Nature has developed an exquisite array of methods to introduce halogen atoms into organic compounds. Most of these enzymes are oxidative and require either hydrogen peroxide or molecular oxygen as a cosubstrate to generate a reactive halogen atom for catalysis. Vanadium-dependent haloperoxidases contain a vanadate prosthetic group and utilize hydrogen peroxide to oxidize a halide ion into a reactive electrophilic intermediate. These metalloenzymes have a large distribution in nature, where they are present in macroalgae, fungi, and bacteria, but have been exclusively characterized in eukaryotes. In this minireview, we highlight the chemistry and biology of vanadium-dependent haloperoxidases from fungi and marine algae and the emergence of new bacterial members that extend the biological function of these poorly understood halogenating enzymes.|Biotransformation[MESH]|Catalysis[MESH]|Catalytic Domain[MESH]|Crystallography, X-Ray/methods[MESH]|Enzymes/chemistry[MESH]|Eukaryota/metabolism[MESH]|Fungi/metabolism[MESH]|Halogens/chemistry[MESH]|Ions[MESH]|Metals/chemistry[MESH]|Mutagenesis[MESH]|Oxygen/chemistry[MESH]|Peroxidases/*chemistry[MESH]|Phosphoric Monoester Hydrolases/chemistry[MESH]|Vanadium/*chemistry[MESH] |