Oxidation reactions catalyzed by vanadium chloroperoxidase from Curvularia inaequalis

Brink, Hilda B. ten; Dekker, Henk; Wever, Ron

doi:10.1016/s0162-0134(00)00044-1

Cited by 49 publications

(28 citation statements)

References 46 publications

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“…Among the fungal enzymes, two types, vanadium and heme-thiol peroxidases, are distinguished (5,43). Both types are capable of chlorinating and brominating organic substrates, but they also catalyze various other oxidation reactions (7,8,38). So far, both fungal vanadium and heme-thiol CPOs have been found only in ascomycetes and related deuteromycetes (2,12,24), although their presence in basidiomycetes was proposed some years ago (6) and very recently there have been indications that there is a putative CPO gene in Agaricus bisporus (white button mushroom) (41).…”

Section: Discussionmentioning

confidence: 99%

Novel Haloperoxidase from the Agaric Basidiomycete Agrocybe aegerita Oxidizes Aryl Alcohols and Aldehydes

Ullrich

Nüske

Scheibner

et al. 2004

Appl Environ Microbiol

321

347

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Agrocybe aegerita, a bark mulch-and wood-colonizing basidiomycete, was found to produce a peroxidase (AaP) that oxidizes aryl alcohols, such as veratryl and benzyl alcohols, into the corresponding aldehydes and then into benzoic acids. The enzyme also catalyzed the oxidation of typical peroxidase substrates, such as 2,6-dimethoxyphenol (DMP) or 2,2-azinobis-(3-ethylbenzothiazoline-6-sulfonate) (ABTS). A. aegerita peroxidase production depended on the concentration of organic nitrogen in the medium, and highest enzyme levels were detected in the presence of soybean meal. Two fractions of the enzyme, AaP I and AaP II, which had identical molecular masses (46 kDa) and isoelectric points of 4.6 to 5.4 and 4.9 to 5.6, respectively (corresponding to six different isoforms), were identified after several steps of purification, including anion-and cation-exchange chromatography. The optimum pH for the oxidation of aryl alcohols was found to be around 7, and the enzyme required relatively high concentrations of H 2 O 2 (2 mM) for optimum activity. The apparent K m values for ABTS, DMP, benzyl alcohol, veratryl alcohol, and H 2 O 2 were 37, 298, 1,001, 2,367 and 1,313 M, respectively. The N-terminal amino acid sequences of the main AaP II spots blotted after two-dimensional gel electrophoresis were almost identical and exhibited almost no homology to the sequences of other peroxidases from basidiomycetes, but they shared the first three amino acids, as well as two additional amino acids, with the heme chloroperoxidase (CPO) from the ascomycete Caldariomyces fumago. This finding is consistent with the fact that AaP halogenates monochlorodimedone, the specific substrate of CPO. The existence of haloperoxidases in basidiomycetous fungi may be of general significance for the natural formation of chlorinated organic compounds in forest soils.Heme peroxidases are found in plants, fungi, bacteria, and animals and have been grouped on the basis of sequence similarity into two superfamilies; animal peroxidases form one superfamily (18), and plant, fungal, and bacterial peroxidases form another superfamily (45). Peroxidases belonging to the latter superfamily have been proposed to have various functions in the individual organisms, including roles in the polymerization and detoxification of phenolic compounds in secondary metabolism, as well as in the decomposition of wood and humus (7,32).Over the last two decades, particular attention has been paid to the peroxidases of white rot fungi, which are involved in the biodegradation of lignin, humic materials, and organopollutants (13,16,33). These enzymes are capable of oxidizing recalcitrant aromatic molecules by one-electron abstractions, resulting in the formation of unstable radicals, which tend to disintegrate spontaneously (19). Numerous isozymes of lignin peroxidase (LiP) and manganese peroxidase (MnP), as well hybrid forms of both enzymes (the so-called versatile peroxidases), have been purified and characterized from different basidiomycetes, including Phanerochaete chrysospo...

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Section: Discussionmentioning

confidence: 99%

Novel Haloperoxidase from the Agaric Basidiomycete Agrocybe aegerita Oxidizes Aryl Alcohols and Aldehydes

Ullrich

Nüske

Scheibner

et al. 2004

Appl Environ Microbiol

321

347

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Section: Vanadium Haloperoxidasesmentioning

confidence: 99%

“…However, unlike the heme enzyme, there is no change in the oxidation state of the V-HPO metal center during the synthesis of the halogenating agent. Hence, V-HPOs do not suffer from oxidative inactivation during turnover and have received increasing attention as biocatalysts for pharmaceutical applications given their tolerance for organic solvents and high temperatures (12, 13), their ability to halogenate a range of organic compounds in a regio-and stereospecific manner (9,14,15), and their ability to oxidize organic sulfides in the absence of halides (16,17).The majority of naturally occurring organohalogens are of marine origin, and nearly all brominated natural products are produced by marine organisms (10). Some of the most frequently reported halometabolites are produced by marine red algae (Rhodophyceae) and include halogenated indoles, terpenes, acetylenes, phenols, and volatile hydrocarbons (9,10,15,18,19).…”

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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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“…Therefore these enzymes were called as hybrid MnP-LiP peroxidases or VP. VPs from various sources Pleurotus pulmonarius Brink et al (2000) Rev Environ Sci Biotechnol (2010) 9:117-140 127 (Camarero et al 2005), Pleurotus ostreatus (Cohen et al 2002), Bjerkandera adusta (Heinfling et al 1997(Heinfling et al , 1998aKrcmar and Ulrich 1998) Pleurotus eryngii (Gomez-Toribio et al 2001) and Bjerkandera sp. (Mester and Field 1998;Moreira et al 2005) have proved their potential to degrade azo dyes.…”

Section: Versatile Peroxidasementioning

confidence: 99%

Peroxidase mediated decolorization and remediation of wastewater containing industrial dyes: a review

Husain

2009

Rev Environ Sci Biotechnol

210

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In this article an effort has been made to review literature based on the role of peroxidases in the treatment and decolorization of a wide spectrum aromatic dyes from polluted water. Peroxidases can catalyze degradation/transformation of aromatic dyes either by precipitation or by opening the aromatic ring structure. Peroxidases from plant sources; horseradish, turnip, tomato, soybean, bitter gourd, white radish and Saccharum uvarum and microbial sources; lignin peroxidases, manganese peroxidases, vanadium haloperoxidases, versatile peroxidases, dye decolorizing peroxidases have been employed for the remediation of commercial dyes. Soluble and immobilized peroxidases have been successfully exploited in batch as well as in continuous processes for the treatment of synthetic dyes with complex aromatic molecular structures present in industrial effluents at large scale. However, recalcitrant dyes were also decolorized by the action of peroxidases in the presence of redox mediators.

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Oxidation reactions catalyzed by vanadium chloroperoxidase from Curvularia inaequalis

Cited by 49 publications

References 46 publications

Novel Haloperoxidase from the Agaric Basidiomycete Agrocybe aegerita Oxidizes Aryl Alcohols and Aldehydes

Novel Haloperoxidase from the Agaric Basidiomycete Agrocybe aegerita Oxidizes Aryl Alcohols and Aldehydes

Exploring the Chemistry and Biology of Vanadium-dependent Haloperoxidases

Peroxidase mediated decolorization and remediation of wastewater containing industrial dyes: a review

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