Vanadium bromoperoxidase

Hara 1, T Sakurai (1998) Isolation and characterization of vanadium bromoperoxidase from a marine macroalga iicHowia stolonifera. J Inorg Chem 72 23-28. 

Soedjak HS, A Butler (1990) Charactarization of vanadium bromoperoxidase from Macrocystis and Fucus reactivity of bromoperoxidase towards acyl and alkyl peroxides and bromination of amines. Biochemistry 29 7974-7981. 

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)... 

Butler, A. Baldwin, A.H. (1997)Vanadium Bromoperoxidase and Functional Mimics. In Structure and Bmiding Metal Sites in Proteins and Models, Lewis Acids, and Vanadium, Sadler, P., Hill, H.A.O., Thompson, A., eds. Springs-Vwlag, New York, Volume 89, pp. 109-131. 

Abbreviated proposed mechanism of vanadium bromoperoxidase-catalyzed bromination 2123, 2124, 2175, 2261, 2263, 2269, 2280, 2328). 

Butler A, Carter-Franklin JN (2004) The Role of Vanadium Bromoperoxidase in the Biosynthesis of Halogenated Marine Natural Products. Nat Prod Rep 21 180... 

Carter JN, Beatty KE, Simpson MT, Butler A (2002) Reactivity of Recombinant and Mutant Vanadium Bromoperoxidase from the Red Alga Corallina officinalis. J Inorg Biochem 91 59... 

Clague MJ, Keder NL, Butler A (1993) Biomimics of Vanadium Bromoperoxidase Vanadium(V)-Schiff Base Catalyzed Oxidation of Bromide by Hydrogen Peroxide. Inorg Chem 32 4754... 

Andersson M, Conte V, Di Furia F, Moro S (1995) Vanadium Bromoperoxidases Mimicking Systems Bromohydrins Formation as Evidence of the Occurrence of a Hypobromite-Like Vanadium Complex. Tetrahedron Lett 36 2675... 

Soedjak HS, Walker JV, Butler A (1995) Inhibition and Inactivation of Vanadium Bromoperoxidase by the Substrate Hydrogen Peroxide and Further Mechanistic Studies. Biochemistry 34 12689... 

Kimblin C, Bu X, Butler A (2002) Modeling the Catalytic Site of Vanadium Bromoperoxidase Synthesis and Structural Characterization of Intramolecularly H-bonded Vanadium (V) Oxoperoxo Complexes, [V0(02)(NH2pyg2)]K and [V0(02)(BrNH2pyg2)]K. Inorg Chem 41 161... 

Andersson MA, Allenmark SG (1998) Asymmetric Sulfoxidation Catalyzed by a Vanadium Bromoperoxidase Substrate Requirements of the Catalyst. Tetrahedron 54 15293... 

Andersson M, Allenmark S (2000) The Potential of Vanadium Bromoperoxidase as a Catalyst in Preparative Asymmetric Sulfoxidation. Biocatal Biotransform 18 79... 

Carter-Franklin JN, Butler A (2004) Vanadium Bromoperoxidase-Catalyzed Biosynthesis of Halogenated Marine Natural Products. J Am Chem Soc 126 15060... 

Feiters MC, Leblanc C, Kiipper FC, Meyer-Klaucke W, Michel G, Potin P (2005) Bromine is an Endogenous Component of a Vanadium Bromoperoxidase. J Am Chem Soc 127 ... 

Vanadium bromoperoxidase (V-BrPO) has been isolated from many species of marine brown algae, including A. nodosum [1,26,27], Laminaria saccharina [28], Fucus distichus [29], and Macrocystis pyrifera [29] the red algae Ceramium rubrum [30] and C. pilulifera [31] and a terrestrial lichen, Xanthoria parie-tina [32],... 

Two vanadium bromoperoxidases that differ in carbohydrate content [26,33] have been isolated from A. nodosum. The most abundant bromoperoxidase, V-BrPO-I, was found in the thallus, and the other bromoperoxidase, V-BrPO-II, was reported to be present on the thallus surface [26], A previous report also concluded that V-BrPO is present in two different locations of A. nodosum, one in the cell walls of the transitional region between the cortex and medulla of the thallus and the other in the cell wall of the thallus surface [34], More recent experiments demonstrate that vanadium-dependent bromoperoxidase activity is present in both the cortical and surface protoplasts of M. pyrifera [35], L. saccharina, and L. digitata [36], The biosynthesis of V-BrPO in the protoplasts of L. saccharina has been shown using [35S]-methionine [36], The vanadium bromoperoxidases are all acidic proteins [26] with very similar amino acid compositions [37], V-BrPO (A. nodosum) has been crystallized, although refined structural data have not been reported yet [38], A different isolation procedure, based primarily on a two-phase extraction system, has been described [39,40], This procedure works well for certain types of algae (e.g., Laminaria) but not for the isolation of V-BrPO from A. nodosum, the principal source of V-BrPO for the mechanistic studies. 

Tschirret-Guth, R.A. and A. Butler. 1994. Evidence for organic substrate binding to vanadium bromoperoxidase../. Am. Chem. Soc. 116 411-412. 

Kimblin, C., X. Bu, and A. Butler. 2002. Modeling the catalytic site of vanadium bromoperoxidase Synthesis and structural characterization of intramolecularly H-bonded vanadium(V) oxoperoxo complexes, [VO(()2)(NI I2pyg2) K and [VO(02) (BrNH2pyg2)]K. Inorg. Chem. 41 161-163. 

Ten Brink, H.B., Holland, H.L., Schoemaker, H.E., van Lingen, H. and Wever, R. (1999). Probing the scope of the sulfoxidation activity of vanadium bromoperoxidase from Ascophyllum nodosum. Tetrahedron Asymmetry, 10,4563-4572. 

The focus of this chapter will be on the mechanistic chemistry of vanadium compounds that catalyze the oxidation of bromide by hydrogen peroxide—that is, functional mimics of vanadium bromoperoxidase. The reader is referred to references 2-8 for more comprehensive reviews of the enzyme. 

Figure 1. Proposed structure of the active site of vanadium bromoperoxidase based on EXAFS data (17).

Scheme 1. Scheme for vanadium bromoperoxidase, showing the formation of an oxidized intermediate which can react by two pathways to give products. 

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