Abstract
Nature 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.
Highlights
Nature has developed an exquisite array of methods to introduce halogen atoms into organic compounds
vanadium-dependent haloperoxidases (V-HPOs) have a larger distribution in nature, where they are present in macroalgae, fungi, and bacteria (1, 4 –5, 9)
Crystal structures are available for three V-HPOs, namely vanadium chloroperoxidases (V-ClPOs) from the fungus C. inaequalis [37,38,39], V-BrPO from the brown alga A. nodosum [40], and V-BrPO from the red alga C. officinalis [41]
Summary
Halogens are an abundant component of the Earth’s biosphere, so it is of little surprise that nature produces a profuse number of organohalogens [10]. V-BrPOs are proposed to be responsible for the halogenation of natural products produced by marine algae [15, 18], and the first V-HPO to be isolated and characterized was the V-BrPO from the brown alga Ascophyllum nodosum in 1984 [22]. V-BrPOs have been characterized from all major classes of marine algae [23,24,25,26,27,28] as well as terrestrial lichen [29] Their proposed role in the biosynthesis of brominated cyclic sesquiterpenes from marine red algae was established through in vitro chemoenzymatic conversion of (E)-(ϩ)-nerolidol (Fig. 1, 1) to yield the marine natural products ␣-snyderol [2], -snyderol [3], and ␥-snyderol [4] [15]. CNQ-525 was shown to be wholly responsible for the synthesis of the chlorinated meroterpenoids, in which the putative V-ClPOs may be responsible for the chlorination and cyclization of SF2415B1 (Fig. 1, 5) to A80915C [6] in a manner reminiscent of that of snyderol biosynthesis in Corallina officinalis
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