Some structural aspects of vanadium bromoperoxidase from Ascophyllum nodosum

Tromp, M. G. M.; 'olafsson, Gunnar; Krenn, Bea E.; Wever, Ron

doi:10.1016/0167-4838(90)90075-q

Cited by 59 publications

(40 citation statements)

References 38 publications

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“…Incubation with the chaotropic agent guanidine/ HCl reveals a GI,, of 3.7 M, somewhat lower than that of 4.7 M reported for the vanadium bromoperoxidase from A. nodosum [25]. The observation that incubation of the enzyme at 80°C causes an initial loss of activity of about 20%, but prolonged incubation does not decrease the activity further, was also found for the vanadium bromoperoxidase from the lichen X. parietina [ 5 ] .…”

Section: Discussionmentioning

confidence: 80%

“…Vanadium bromoperoxidases have been reported [25] to be stable enzymes and the chloroperoxidase shows similar stability features. When the chloroperoxidase was incubated in 40% methanol, ethanol or 2-propanol and aliquots of the incubation mixture were taken and tested for activity the chloroperoxidase activity was hardly affected by incubation even after three weeks of incubation (data not shown).…”

Section: Resultsmentioning

confidence: 99%

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The Stability and Steady‐State Kinetics of Vanadium Chloroperoxidase from the Fungus Curvularia Inaequalis

Schijndel¹,

Barnett²,

Roelse³

et al. 1994

European Journal of Biochemistry

128

132

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Section: Discussionmentioning

confidence: 80%

Section: Resultsmentioning

confidence: 99%

The Stability and Steady‐State Kinetics of Vanadium Chloroperoxidase from the Fungus Curvularia Inaequalis

Schijndel¹,

Barnett²,

Roelse³

et al. 1994

European Journal of Biochemistry

128

132

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“…VHPO enzymes are also extremely thermostable, resistant to high concentration of organic solvents such as methanol, ethanol, 1-propanol, acetone [45] and dioxane and still active in concentrated solutions of guanidine hydrochloride or SDS [61,63].…”

Section: Biochemical Coordination Of V In Vanadium Haloperoxidasesmentioning

confidence: 99%

“…Up to now, a number of VHPOs have been characterized at the biochemical and molecular levels from red and brown macroalgae, terrestrial fungi and marine bacteria (see Table 1 for complete references). In the brown alga A. nodosum, the two VBPO isoenzymes present at different locations in the alga [61,71] feature distinct biochemical and structural properties [60], suggesting distinct biological roles in the algal physiology. In vitro halogenation experiments have shown that purified native VBPOI from A. nodosum catalyzes the bromination of pyrroles [72] or phenols [73], whereas the second VBPO is involved in the biosynthesis of methyl 4-bromopyrrole-2-carboxylate, a natural product isolated from the marine sponge [60].…”

Section: Vanadium Haloperoxidase -Catalyzed Halogenationmentioning

confidence: 99%

“…The ratio of vanadate per protein subunit was estimated around one VO 4 per subunit, but was lower in VBPOII from A. nodosum [60]. The affinity of VHPO for vanadate depends on pH [15,61,62], and is much stronger than for oxyanions, such as phosphate or molybdate (HVO 4 2->> HPO 4 2-> AsO 4 3− > MoO 4 2-) [34,61]. However, the peroxidase activity decreases in phosphate-containing buffers [21].…”

Section: Biochemical Coordination Of V In Vanadium Haloperoxidasesmentioning

confidence: 99%

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Vanadium haloperoxidases: From the discovery 30 years ago to X-ray crystallographic and V K-edge absorption spectroscopic studies

Leblanc

Vilter

Fournier

et al. 2015

Coordination Chemistry Reviews

128

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In the environment, vanadium-dependent haloperoxidases (VHPO) are likely to play a key role in the production of biogenic organo-halogens. These enzymes contain vanadate as a prosthetic group, and catalyze, in the presence of hydrogen peroxide, the oxidation of halide ions (Cl -, Br -or I -). They are classified according to the most electronegative halide that they can oxidize. Since the first discovery of a vanadium bromoperoxidase in the brown alga Ascophyllum nodosum thirty years ago, structural and mechanistic studies have been mainly conducted on two types of VHPO, chloro-and bromoperoxidases, and more recently on a vanadium-dependent iodoperoxidase. In this review, we highlight the main progress obtained on the structure-function relation of these proteins, based on biochemistry, crystallography and X-ray absorption spectroscopy (XAS). The comparison of 3D protein structures of the different VHPO helped identify the residues that govern the molecular mechanisms of catalysis and specificity of VHPO. Vanadium K-edge XAS gave further important insight to understand the fine changes around the vanadium cofactor during the catalytic cycle. The combination of different structural approaches, at different scales of resolution, shed new light on biological vanadium coordination in the active site, and its importance for the catalytic cycle and halide specificity of vanadium haloperoxidases. Keywords (max 6)Vanadium-dependent haloperoxidase, vanadium coordination, crystallographic structure, structural evolution, oligomeric state, X-ray absorption spectroscopy on biological vanadium

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Vanadium Haloperoxidases

Wever¹,

Hemrika²

2004

Handbook of Metalloproteins

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This chapter describes the occurrence and the biological function of the vanadium bromoperoxidases and chloroperoxidases. These enzymes that contain vanadate as the prosthetic group catalyze the oxidation of halides to the corresponding hypohalous acids. Purification and molecular characterization of these enzymes is reported and a detailed comparison is made between a bromoperoxidase and a chloroperoxidase, both kinetically as well as structurally. The vanadate‐binding site in haloperoxidases shows an interesting homology with the binding site of phosphate in a large group of phosphatases. Finally, on the basis of mutagenesis studies, a catalytic mechanism is presented for the vanadium chloroperoxidase activity that details the role in catalysis of the amino acid residues in the first coordination sphere of the metal oxide.

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Some structural aspects of vanadium bromoperoxidase from Ascophyllum nodosum

Cited by 59 publications

References 38 publications

The Stability and Steady‐State Kinetics of Vanadium Chloroperoxidase from the Fungus Curvularia Inaequalis

The Stability and Steady‐State Kinetics of Vanadium Chloroperoxidase from the Fungus Curvularia Inaequalis

Vanadium haloperoxidases: From the discovery 30 years ago to X-ray crystallographic and V K-edge absorption spectroscopic studies

Vanadium Haloperoxidases

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