Vanadium peroxidases

Krenn BE, Y Izumi, H Yamada, R Wever (1989) A comparison of different (vanadium) peroxidases the bro-moperoxidase of Corallina pilulifera is also a vanadium enzyme. Biochim Biophys Acta 998 63-68. 

Some haloperoxidases contain vanadium and a review of vanadium peroxidases has been given (Butler 1998). The structure of the vanadium enzyme in the terrestrial fungus Cur-vularia inaequalis has been determined by x-ray analysis (Messerschmidt et al. 1997), and the apochloroperoxidase possesses, in addition, phosphatase activity that can be rationalized on the basis of the isomorphism of phosphate and vanadate (Renirie et al. 2000). 

Butler A (1998) Vanadium peroxidases. Curr Opinion Chem Biol 2 279-285. 

Hemrika W, Renirie R, Dekker HL, Barnett P, Wever R (1997) From Phosphatases to Vanadium Peroxidases A Similar Architecture of the Active Site. Proc Natl Acad Sci U S A 94 2145... 

Butler, A. and J.N. Carter-Franklin. 2004. The role of vanadium peroxidase in the biosynthesis of halogenated marine natural products. Nat. Prod Rep. 21 180-188. 

Another class of peroxidases which can perform asymmetric sulfoxidations, and which have the advantage of inherently higher stabilities because of their non-heme nature, are the vanadium peroxidases. It was shown that vanadium bromoperoxidase from Ascophyllum nodosum mediates the production of (R)-methyl phenyl sulfoxide with a high 91% enantiomeric excess from the corresponding sulfide with H202 [38]. The turnover frequency of the reaction was found to be around 1 min-1. In addition this enzyme was found to catalyse the sulfoxidation of racemic, non-aromatic cyclic thioethers with high kinetic resolution [309]. 

Interestingly, a study of the bromide-dependent chloroperoxidase bromination of tyrosine reveals that the active brominating agent is free bromine and not a bromine-enzyme complex [122]. The situation is very different for bromoperoxidase- and vanadium peroxidase-catalyzed brominations [106-108]. 

Vanadium Peroxidase and nitrogenase activity in some algae and possibly fungi... 

Other vanadium-containing enzymes appear to be particularly important in the production of polybrominated compounds in the sea (8, 70). The vanadium peroxidases utilize hydrogen peroxide to oxidize bromide or iodide, probably to corresponding hypohalite ions, which then react with NOM to produce polyhalogenated compounds (eq 17) (8, 70). 

Since the discovery by Cantley et al. that vanadate is a powerful and allosteric inhibitor of Na ,K -ATPase, vanadium began to interest biochemists and Chasteen has reviewed work published up to 1983.Particularly interesting new studies involve vanadium peroxidases and nitrogenases. ... 

Vanadium. Vanadium is essential in rats and chicks (85,156). Estimated human intake is less than 4 mg/d. In animals, deficiency results in impaired growth, reproduction, and Hpid metaboHsm (157), and altered thyroid peroxidase activities (112). The levels of coen2yme A and coen2yme Q q in rats are reduced and monoamine oxidase activity is increased when rats are given excess vanadium (157). Vanadium may play a role in the regulation of (NaK)—ATPase, phosphoryl transferases, adenylate cyclase, and protein kinases (112). 

Vilter H (1984) Peroxidase from Phaeophyceae a vanadium (V)-dependent peroxidase from Ascophyllum nodosum. Phytochem 23 1387-1390. 

Renirie R, W Hemrika, R Wever (2000) Peroxidase and phosphatase activity of active-site mutants of vanadium chloroperoxidase from the fungus Curvularia inaequalis. J Biol Chem 275 11650-11657. 

Peroxidases (E.C. 1.11.1.7) are ubiquitously found in plants, microorganisms and animals. They are either named after their sources, for example, horseradish peroxidase and lacto- or myeloperoxidase, or akin to their substrates, such as cytochrome c, chloro- or lignin peroxidases. Most of the peroxidases studied so far are heme enzymes with ferric protoporphyrin IX (protoheme) as the prosthetic group (Fig. 1). However, the active centers of some peroxidases also contain selenium (glutathione peroxidase) [7], vanadium (bromoperoxidase)... 

Enzymes requiring vanadium for catalytic activity. Perhaps the best studied of these are the vanadium-dependent nitrogenases [EC 1.18.6.1]. Other vanadium-dependent enzymes include vanadium haloperoxidase, vanadium chloroperoxidase, and vanadium bromoper-oxidase. In the vanadium chloroperoxidase and bromo-peroxidase reactions, the vanadium(V) is coordinated in a trigonal bipyramidal site to a histidyl residue, three nonprotein oxygens, and, presumably, to a hydroxide. 

Haloperoxidases are peroxidases capable of halogenating substrates in the presence of halide and hydrogen peroxide [14] or other reactions such as sulfoxidation, epoxidation and aromatic hydroxylation. Here, the halide ion is initially bound to the active site which may incorporate heme or vanadium or be metal free. The halide ion is incorporated into the substrate after electron transfer... 

Vanadoproteins are found in most marine algae and seaweed and in some lichens.616 Among these are haloperoxidases,252 253 617 618b enzymes that are quite different from the corresponding heme peroxidases discussed in Section A,6. The vanadium is bound as... 

A. Messerschmidt, X. Prade, and R. Wever, Implications for the catalytic mechanism of the vanadium-containing enzyme chloro-peroxidase from the fungus Curvularia inaequalis by X-ray structures of the native and peroxide form, Biol. Chem. 1997, 378, 309-315. 

F. van Rantwijk, and R. A. Sheldon, Enantioselective sulfoxidation mediated by vanadium-incorporated phytase a hydrolase acting as a peroxidase,... 

Most other peroxidases are Fe-heme-containing systems, which function as two-electron redox catalysts (Scheme 8). Dihydrogen peroxide oxidizes the Fe-heme moiety by two electrons, forming Compound 1 (a heme + FeIV=0 species) [97], Compound 1 oxidizes the halide ion, forming the active halogenating species. This mechanism cannot be operative in V-BrPO because the vanadium is already in its highest accessible oxidation state. Moreover, native V-BrPO does not oxidize bromide without an acceptable peroxide source. However, it should... 

Many peroxovanadates have potent insulin-mimetic properties [1,2]. Apparently, this functionality derives from the ability of these compounds to rapidly oxidize the active site thiols found in the group of protein tyrosine phosphatases that are involved in regulating the insulin receptor function [3], The discovery of vanadium-dependent haloperoxidases in marine algae and terrestrial lichens provided an additional stimulus in research toward obtaining functional models of peroxidase activity, and there is great interest in duplicating the function of these enzymes (see Section 10.4.2). 

Vilter, H. 1984. Peroxidases from Phaeophyceae A vanadium(V)-dependent peroxidase from Ascophylum nodosum. Phytochem. 23 1387-1390. 

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