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Bromoperoxidases

A novel class of haloperoxidases, in which a heme prosthetic group was absent, was detected in brown algae (Phaeophyceae) by Vilter and coworkers (13-15). These publications escaped the attention of most biochemists involved in peroxidase research. Only when some of this work was published in the journal Phytochemistry (16) was there as increasing awareness of these findings. A clue for the involvement of vanadium was also published (16). It was shown that the bromoperoxidase could be inactivated at low pH and reactivated by vanadate. These results were subsequently confirmed (17, 18) when it was shown that vanadium was present in a number of bromoperoxidases from different sources and was essential for enzymatic activity. To date, these sources include the enzymes from the brown seaweed Ascophyllum nodosum [Pg.82]

Vanadium is also an essential element for some marine macro-algae, such as the brown seaweed F. spiralus and the green seaweed Entero-morpha compressa. The growth yield of these marine algae is enhanced considerably (26) when vanadate is added to the culture medium, which consists of artificial seawater. Some seaweeds contain vanadium. A study of 70 seaweeds from Japanese coastal waters yielded vanadium contents ranging from 0.3 to 10.6 ppm on the basis of dry weight (27). [Pg.83]

Most assay methods to detect bromoperoxidase activity are based on the bromination of monochlorodimedone, a cyclic diketone that has a high affinity for HOBr and that on bromination loses it absorbance at 290 nm (e = 20.2 mM cm ). This assay method was originally developed for measurements of chloroperoxidase activity by Hager et al. (28). [Pg.83]

Alternatively, bromination of phenol red to bromophenol blue may be used (29). [Pg.83]

A further reaction involves the bromination of fluoresceine to the tetrabrominated compound eosine (30). These are convenient assays, since marked color changes take place. [Pg.84]


Asymmetric sulfoxidation catalyzed by a Vanadium-dependent bromoperoxidase... [Pg.100]

Scheme 9.37 Vanadium-dependent bromoperoxidase (VBPO)-mediated conversion of nerolidol to a-, fl-, and y-snyderols. Scheme 9.37 Vanadium-dependent bromoperoxidase (VBPO)-mediated conversion of nerolidol to a-, fl-, and y-snyderols.
The gene encoding the esterase from Pseudomonas fluorescens was expressed in Escherichia coli, and the enzyme displayed both hydrolytic and bromoperoxidase activity (Pelletier and Altenbnchner 1995). [Pg.135]

Baden DG, MD Corbett (1980) Bromoperoxidases from Penicillus capitatus, Penicillus lamourouxii and Rhipocephalus phoenix. Biochem J 187 205-211. [Pg.136]

Hara 1, T Sakurai (1998) Isolation and characterization of vanadium bromoperoxidase from a marine macroalga iicHowia stolonifera. J Inorg Chem 72 23-28. [Pg.139]

Itoh N, AKM Quamrul Hasan, Y Izumi, H Yamada (1988) Substrate specificity, regiospecificity and stereospecificity of halogenation reactions catalyzed by non-heme-type bromoperoxidase of Corallina pilulifera. Eur J Biochem 172 477-484. [Pg.139]

Itoh N, N Morinaga, T Kouzai (1994) Purification and characterization of a novel metal-containing nonheme bromoperoxidase from Pseudomonas putida. Biochim Biophys Acta 1207 208-216. [Pg.139]

Jordan P, H Vilter (1991) Extraction of proteins from material rich in anionic mucilages partition and fractionation of vanadate-dependent bromoperoxidases from the brown algae Laminaria digitata and L. saccharina in aqueous polymer two-phase systems. Biochim Biophys Acta 1073 98-106. [Pg.140]

Manthey JA, LP Hager (1981) Purification and properties of bromoperoxidase from Penicillus capitatus. J Biol Chem 256 11232-11238. [Pg.142]

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. [Pg.145]

Weng M, O Pfeifer, S Kraus, F Lingens, K-H van Pee (1991) Purification, characterization and comparison of two non-heme bromoperoxidases from Streptomyces aureofaciens. J Gen Microbiol 137 2539-2546. [Pg.147]

ZeinerR, K-H van Pee, F Lingens (1988) Purification and partial characterization of multiple bromoperoxidases from Streptomyces griseus. J Gen Microbiol 134 3141-3149. [Pg.147]

Figure 1 The microbial fouling process on surfaces of certain macroalgae in aquatic environments is controlled by the selective oxidation of bromide with hydrogen peroxide and bromoperoxidase. Although chloride is many orders of magnitude more abundant in the sea, bromide is oxidized to hypobromous acid in situ. Figure 1 The microbial fouling process on surfaces of certain macroalgae in aquatic environments is controlled by the selective oxidation of bromide with hydrogen peroxide and bromoperoxidase. Although chloride is many orders of magnitude more abundant in the sea, bromide is oxidized to hypobromous acid in situ.
Figure 4 Stabilized bromine antimicrobials are produced by eosinophils, a type of mammalian white blood cell. Bacteria are captured by phagocytosis and contained intracellularly within vesicles called phagosomes. Granules release cationic surfactants, lytic enzymes, and eosinophil peroxidase into the phagosome in a process known as degranulation. Eosinophil peroxidase, an enzyme that is structurally similar to the bromoperoxidases found in seaweed (Figure I), selectively catalyzes oxidation of bromide to hypobromite by reducing hydrogen peroxide to water. The hypobromite immediately reacts with nitrogenous stabilizers such as aminoethanesulfonic acid (taurine) to form more effective and less toxic antimicrobial agents. Figure 4 Stabilized bromine antimicrobials are produced by eosinophils, a type of mammalian white blood cell. Bacteria are captured by phagocytosis and contained intracellularly within vesicles called phagosomes. Granules release cationic surfactants, lytic enzymes, and eosinophil peroxidase into the phagosome in a process known as degranulation. Eosinophil peroxidase, an enzyme that is structurally similar to the bromoperoxidases found in seaweed (Figure I), selectively catalyzes oxidation of bromide to hypobromite by reducing hydrogen peroxide to water. The hypobromite immediately reacts with nitrogenous stabilizers such as aminoethanesulfonic acid (taurine) to form more effective and less toxic antimicrobial agents.
It has been suggested (Bozzi et ah, 1997 Grant et ah, 1998) that Dps and E. inocua ferritin represent examples of a family of ancestral dodecameric protein which had as function to trap, but not to mineralize, metal ions, and that the ability to oxidize and mineralize iron efficiently and to form fourfold interactions came later. The hollow-cored dodecameric motif exemplified by Dps and E. inocua ferritin has clearly been adapted to a number of functions, since in addition to DNA binding and iron storage, other family members include a novel pilin, a bromoperoxidase and several other proteins of unknown function (Grant et ah, 1998). [Pg.187]

Figure 17.13 The structure and active site of the bromoperoxidase subunit from C. pilulifera. Residues conserved in all vanadium bromo- and chloroperoxidases are in grey, those that vary in cyan. (From Ohshiro et al., 2004. Copyright 2004 The Protein Society.)... Figure 17.13 The structure and active site of the bromoperoxidase subunit from C. pilulifera. Residues conserved in all vanadium bromo- and chloroperoxidases are in grey, those that vary in cyan. (From Ohshiro et al., 2004. Copyright 2004 The Protein Society.)...
Modification of halogen specificity of a vanadium-dependent bromoperoxidase, Protein Sci., 13, 1566-1571. [Pg.295]

Mittler R (2002) Oxidative stress, antioxidants and stress tolerance. Trends Plant Sci 7 405 410 Moore RM, Webb M, Tokarczyk R, Wever R (1996) Bromoperoxidase and iodoperoxidase enzymes and production of halogenated methanes in marine diatom cultures. J Geophys Res 101 20899-20908... [Pg.268]

Ohsawa N, Ogata Y, Okada N, Itoh N (2001) Physiological function of bromoperoxidase in the red marine alga, Corallina pilulifera production of bromoform as an allelochemical and the simultaneous elimination of hydrogen peroxide. Phytochemistry 58 683-692... [Pg.268]

Redox catalysis Zn, Fe, Cu, Mn, Mo, Co, V Se, Cd, Nl Enzymes (see Table 11.4 for more Information) Reactions with oxygen (Fe, Cu) Oxygen evolution (Mn) Nitrogen fixation (Fe, Mo) Inhibition of llpid peroxidation (Se) Carbonic anhydrase (Cd) Reduction of nucleotides (Co) Reactions with H2 (Nl) Bromoperoxidase activity (V)... [Pg.235]

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)... [Pg.75]

DeBoer E, Plat H, Wever R (1987) Algal vanadium(V)-bromoperoxidase. A halogenating enzyme retaining full activity in apolar solvent systems. In Laane C, Tramper J, Lilly MD (eds) Biocatalysis in organic media. Elsevier, Amsterdam, p 317... [Pg.107]


See other pages where Bromoperoxidases is mentioned: [Pg.291]    [Pg.253]    [Pg.134]    [Pg.137]    [Pg.146]    [Pg.146]    [Pg.53]    [Pg.61]    [Pg.107]    [Pg.291]    [Pg.292]    [Pg.138]    [Pg.265]    [Pg.152]    [Pg.56]    [Pg.90]    [Pg.99]    [Pg.222]    [Pg.232]    [Pg.240]    [Pg.269]    [Pg.186]   
See also in sourсe #XX -- [ Pg.291 ]

See also in sourсe #XX -- [ Pg.109 , Pg.111 ]




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Bromoperoxidase

Bromoperoxidase

Bromoperoxidase biosynthesis

Bromoperoxidase isolation

Bromoperoxidase kinetics

Bromoperoxidase mechanism

Bromoperoxidase selectivity

Bromoperoxidase specific activity

Bromoperoxidase structure

EXAFS, vanadium bromoperoxidases

Electron vanadium bromoperoxidases

Oxidation state, vanadium bromoperoxidases

Peroxidases vanadium bromoperoxidases

Vanadium bromoperoxidase

Vanadium bromoperoxidase active site

Vanadium bromoperoxidase reactivity

Vanadium bromoperoxidase structure

Vanadium bromoperoxidases

Vanadium bromoperoxidases active site structure

Vanadium bromoperoxidases bromide

Vanadium bromoperoxidases mechanism

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