Crystal structure of dodecameric vanadium-dependent bromoperoxidase from the red algae Corallina officinalis 1 1Edited by R. Huber

Isupov, Michail N.; Dalby, Andrew R.; Brindley, Amanda A.; Izumi, Yoshikazu; Tanabe, Tadashi; Murshudov, Garib N.; Littlechild, Jennifer A.

doi:10.1006/jmbi.2000.3806

Cited by 178 publications

(157 citation statements)

References 48 publications

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“…These dimers are able to self-arrange in more complex structures, such as hexameric proteins, as shown by gel filtration chromatography results obtained for VBPO from L. digitata [53] and for the second VBPO from A. nodosum [60]. In contrast, the red algal VHPO dimers are not stabilized by covalent bonds but organized in a hexamer of dimers ( Figure 2D) [93,94]. This dodecamer is about 150 Å in diameter and forms a cavity in its center.…”

Section: Phylogenetic Relationships Of Vanadium Haloperoxidasesmentioning

confidence: 90%

“…Multimerization is a biological strategy to stabilize proteins [95]; consequently, in the case of red algal VHPOs, the high stability to organic solvent and high temperature might be a result of the strong interactions present in these highly symmetric multimers. In VBPO dimers, the surface of interaction represents 20 and 46% of the total exposed surface of a monomer for C. officinalis [93] and A. nodosum [39], respectively. In contrast, in the red algal VBPO dodecamer, only 12% of a monomer surface is exposed to the solvent [93,96,97].…”

Section: Phylogenetic Relationships Of 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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Section: Phylogenetic Relationships Of Vanadium Haloperoxidasesmentioning

confidence: 90%

Section: Phylogenetic Relationships Of Vanadium Haloperoxidasesmentioning

confidence: 99%

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

View full text Add to dashboard Cite

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“…The vanadium bromoperoxidase enzymes from two members of the red algal species, Corallina, have been previously studied in detail at a structural level [1,2]. These enzymes form a large dodecameric structure with 12 protein subunits each containing vanadium V which is essential for activity.…”

Section: Introductionmentioning

confidence: 99%

“…These enzymes form a large dodecameric structure with 12 protein subunits each containing vanadium V which is essential for activity. The structure of C. officinalis vanadium haloperoxidase was solved to 2.3Å in 2000 by Isupov et al, [1] and showed a 595 amino acid chain folded into a single α + β type domain. The structure does not contain any disulfide bridges as found in the related Ascophyllum bromoperoxidase [3].…”

Section: Introductionmentioning

confidence: 99%

“…The dimers then interact to form the dodecamer with a 23 cubic point symmetry, which is approximately 150Å in diameter [1] (Figure 1). Two vanadate atoms are associated with each dimeric subunit and are co-ordinated in a trigonal bipyramidal geometry with hydroxide and His496 in axial positions and three non-protein (solvent) oxygen atoms in equatorial positions.…”

Section: Introductionmentioning

confidence: 99%

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Vanadium containing bromoperoxidase – Insights into the enzymatic mechanism using X-ray crystallography

Littlechild

Rodríguez

Isupov

2009

Journal of Inorganic Biochemistry

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The structure of the vanadium bromoperoxidase from the red algae Corallina pilulifera has been solved in the presence of the substrates, phenol red and phloroglucinol. The results obtained give a putative location close to the active site of the enzyme. In addition bromide has been soaked into the crystals and has been shown to bind unambiguously within the active site using single anomalous dispersion. A mutant of the enzyme where arginine 397 has been changed to tryptophan, shows a different behaviour on bromide binding regarding the displacement of a specific leucine amino acid which is seen to move towards the incoming ion in the wild-type protein to produce a hydrophobic environment within the active site.These results have increased our understanding of the mechanism of the vanadium bromoperoxidases and have demonstrated that the substrate and bromide are specifically bound to the enzyme active site.3

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Vanadium in Biology

Wever

Renirie

Hasan

2005

Encyclopedia of Inorganic Chemistry

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In this article, the role of vanadium in a number of biological systems will be discussed. The metal oxide (vanadate) is present as the prosthetic group in the haloperoxidases, enzymes that are able to oxidize halides in the presence of hydrogen peroxide to hypohalous acids. The bromoperoxidases seem to be involved in the production of the huge amounts of brominated compounds formed by several seaweeds. The enzymes have unusual properties in terms of stability and structural organization. X‐ray structures at high resolution are available now for four vanadium haloperoxidases and details of the events occurring at the active site during catalysis are known. The metal oxide binds peroxide in a side‐on fashion and seems to acts as a Lewis acid in polarizing the bound peroxide for further nucleophilic attack by an incoming halide. These enzymes are also able to mediate in the presence of hydrogen peroxide, the enantioselective sulfoxidation of organic sulfides yielding chiral sulfoxides with high enantiomeric excess. The active site of the haloperoxidases is very similar to that found in acid phosphatases that hydrolyze phosphate monoesters and there is some evidence that the haloperoxidases have evolved from the phosphatases. Vanadium is found in the vanadium III state in certain blood cells of tunicates (Ascidians) under very acidic conditions. Despite many studies, there is no clue as to the physiological role of the metal and there are many questions regarding the mechanism of accumulation and reduction of the metal in these organisms. The metal also seems to be used as an electron sink by certain bacteria under anaerobic conditions. Furthermore, vanadium is accumulated in Amanita species. These toadstools contain up to 10 mM of a vanadium IV compound with very special structure in which the vanadium IV is eightfold coordinated in an unusual geometry. Although the compound has been reported to carry out redox reactions, the physiological function is elusive.

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Crystal structure of dodecameric vanadium-dependent bromoperoxidase from the red algae Corallina officinalis 1 1Edited by R. Huber

Cited by 178 publications

References 48 publications

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

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

Vanadium containing bromoperoxidase – Insights into the enzymatic mechanism using X-ray crystallography

Vanadium in Biology

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