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Vanadium bromoperoxidase and functional mimics

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Part of the book series: Structure and Bonding ((4143,volume 89))

Abstract

Haloperoxidases are enzymes which catalyze the oxidation of halides (iodide, bromide and chloride) by hydrogen peroxide, resulting in the halogenation of appropriate organic substrates or the halide-assisted disproportionation of hydrogen peroxide forming dioxygen. Two classes of vanadium haloperoxidases are known: vanadium bromoperoxidase, isolated mainly from marine algae, and vanadium chloroperoxidase from terrestrial fungi. A review of the structure, reactivity and enzyme kinetics of these enzymes is presented. Kinetic and mechanistic studies of several functional mimics of the vanadium haloperoxidases are also presented, including peroxo-complexes of vanadium(V) and other transition metal ions. These catalysts have proved useful in testing hypotheses concerning the role of vanadium in the haloperoxidase enzymes.

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Abbreviations

MCD:

monochlorodimedone

V-BrPO:

vanadium bromoperoxidase

V-HPO:

vanadium haloperoxidase

V-CIPO:

vanadium chloroperoxidase

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Correspondence to Alison Butler .

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H. A. O. Hill P. J. Sadler A. J. Thomson

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© 1997 Springer Verlag Berlin Heidelberg

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Butler, A., Baldwin, A.H. (1997). Vanadium bromoperoxidase and functional mimics. In: Hill, H.A.O., Sadler, P.J., Thomson, A.J. (eds) Metal Sites in Proteins and Models. Structure and Bonding, vol 89. Springer, Berlin, Heidelberg. https://doi.org/10.1007/3-540-62874-6_10

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  • DOI: https://doi.org/10.1007/3-540-62874-6_10

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