Occurrence of bromoperoxidase in the marine green macro-alga, ulvella lens, and emission of volatile brominated methane by the enzyme

Ohshiro, Takashi; Nakano, Satoru; Takahashi, Yūzō; Suzuki, Minoru; Izumi, Yoshikazu

doi:10.1016/s0031-9422(99)00404-5

Cited by 36 publications

(18 citation statements)

References 27 publications

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“…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). To date, 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.…”

Section: Vanadium Haloperoxidasesmentioning

confidence: 99%

Exploring the Chemistry and Biology of Vanadium-dependent Haloperoxidases

Winter

Moore

2009

Journal of Biological Chemistry

201

168

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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. VanadiumVanadium is a trace element that is widely distributed in nature. After molybdenum, vanadium is the second most abundant transition metal in the ocean, with a concentration of 35-50 nM (1) and up to 100 mg/kg in carbon-containing sediments of marine origin. In fresh water, the concentration is reported as 1.3 g/liter (50 nM), and in the Earth's crust, vanadium is present at 100 ppm (1, 2). Vanadium exists in many oxidation states, with V(V) being the most common in sea water (1-3). Only the V(III), V(IV), and V(V) oxidation states are involved, however, in biological systems, where vanadium has limited distribution as an essential mineral in organisms such as sea squirts and mushrooms and as a cofactor in metalloenzymes. The most prevalent form of vanadium at neutral pH is the oxyanion vanadate, which is an oxidizing agent that is structurally and electronically similar to phosphate (1-3). Hence, vanadate and vanadate derivatives have been employed to interrogate a range of enzymes that interact with phosphorylated substrates (3). Interestingly, acid phosphatase enzymes have evolved to accommodate vanadate as a redox cofactor (4, 5). Vanadium-containing EnzymesTo date, two classes of vanadium-containing enzymes have been identified: vanadium nitrogenases and vanadium-dependent haloperoxidases (V-HPOs).2 Nitrogenases are utilized by nitrogen-fixing bacteria to reduce dinitrogen to ammonia. Although this metalloenzyme system commonly contains a molybdenum-iron cofactor, some bacteria produce additional nitrogenases that are genetically distinct and instead contain V-Fe or Fe-Fe central metals (6 -8). Vanadium nitrogenases have been identified from a diverse group of diazotrophic microorganisms and are synthesized under molybdenum-limiting conditions. On the other hand, V-HPOs have a larger distribution in nature, where they are present in macroalgae, fungi, and bacteria (1, 4 -5, 9). These enzymes, which contain a ligated vanadate ion, oxidize halide ions to their corresponding hypohalous acids at the expense of hydrogen peroxide and are classified by the most electronegative halide they oxidize. Thus, vanadium chloroperoxidases (V-ClPOs) oxidize chloride, bromide, ...

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Section: Vanadium Haloperoxidasesmentioning

confidence: 99%

Exploring the Chemistry and Biology of Vanadium-dependent Haloperoxidases

Winter

Moore

2009

Journal of Biological Chemistry

201

168

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“…A variety of halogenated compounds are found in many marine macroalgae. Haloperoxidase enzymes have been characterized from Corallina species (Itoh et al 1986; Sheffield et al 1993), Ascophyllum nodosum (Wever et al 1985), and Ulvella lens (Ohshiro et al 1999). These enzymes are thought to function in the biosynthesis of halogenated natural products.…”

mentioning

confidence: 99%

Modification of halogen specificity of a vanadium‐dependent bromoperoxidase

et al. 2004

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The halide specificity of vanadium-dependent bromoperoxidase (BPO) from the marine algae, Corallina pilulifera, has been changed by a single amino acid substitution. The residue R397 has been substituted by the other 19 amino acids. The mutant enzymes R397W and R397F showed significant chloroperoxidase (CPO) activity as well as BPO activity. These mutant enzymes were purified and their properties were investigated. The maximal velocities of CPO activities of the R397W and R397F enzymes were 31.2 and 39.2 units/mg, and the K m values for Cl − were 780 mM and 670 mM, respectively. Unlike the native enzyme, both mutant enzymes were inhibited by NaN 3 . In the case of the R397W enzyme, the incorporation rate of vanadate into the active site was low, compared with the R397F and the wild-type enzyme. These results supported the existence of a specific halogen binding site within the catalytic cleft of vanadium haloperoxidases.

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“…Theseare plausibly biosynthesized by successive bromination of the enols of C-2 or C-3 units containing C=O groups followed by loss of Cl (CH 2 0 from CH 3 CHO and CH 3 CHO from CH 3 .CO.CH 3 ) with concomitant formation of CH 2 Hal 2 , and CHHal 3 • This mechanism is supported by the biosynthesis of CH 2 Br 2 and CHBr 3 when the bromoperoxidase from the green macro alga Ulvella Zens was incubated with oxalacetate, bromide and H 2 0 2 [155]: the eightfold stimulation in enzymatic activity by added Co 2 + is noteworthy. It has been suggested [ 186] that in California this alga is an epiphyte on Laurencia that is well established as a source of brominated metabolites.…”

Section: Polyhalogenated Methanesmentioning

confidence: 93%

Biological Effects and Biosynthesis of Brominated Metabolites

Neilson

2003

The Handbook of Environmental Chemistry

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Abstract. On the basis of halogenated metabolites assembled by Gribble, an attempt is made to provide a hypothesis for the biosynthesis of representative groups. Examples of brominated and iodinated metabolites are drawn from the major classes of terpenoids and acetogenins, and related to the biosynthesis of their putative precursors. Brominated and iodinated carbocyclic and heterocyclic aromatic compounds are discussed as weil as mechanisms for the oxidative coupling of phenolic substrates. A few chlorinated metabolites are introduced for additional illustration. Halogenation by cationoid (Hai+) reactions catalyzed by haloperoxidases is discussed, and attention drawn to the alternative role of anionoid (Hal-) halogenation. The presentation is extended to the biosynthesis of isonitriles and dichloroimines by anionoid reaction of precursors with cyanide. The range of biota that produce brominated substrates is briefly indicated, and comments made on the ecological significance of metabolites and associations among biota.

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Occurrence of bromoperoxidase in the marine green macro-alga, ulvella lens, and emission of volatile brominated methane by the enzyme

Cited by 36 publications

References 27 publications

Exploring the Chemistry and Biology of Vanadium-dependent Haloperoxidases

Exploring the Chemistry and Biology of Vanadium-dependent Haloperoxidases

Modification of halogen specificity of a vanadium‐dependent bromoperoxidase

Biological Effects and Biosynthesis of Brominated Metabolites

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