(Model) investigations of the function of vanadium in biological systems

Rehder, Dieter; Priebsch, Wolfgang; Holst, Hartmut; Hillerns, Frank; Richter, J.

doi:10.1016/0162-0134(91)84392-m

Cited by 19 publications

(65 citation statements)

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“…5A). This result, therefore, is not consistent with the formation of a binuclear monoligand product, as previously reported from analysis of these data (18). The formation constant obtained from this analysis for VP (-515 ppm), obtained from the ligand concentration study, was (2.4 5 0.2) x 10' M-' (Fig.…”

Section: Plienylglutamatecontrasting

confidence: 58%

“…The spectra that were obtained gave a formation constant of about 70 M-' for the product at pH 7.0. A rather detailed study of this system, carried out at pH 7.2, has been reported (18). The reported data give a value of (1.1 + 0.1) x 1 o2 M-I for K, .…”

Section: Plienylglutamatementioning

confidence: 95%

“…In view or the co~nplications that can arise from competing interactions and the conclusions draw11 horn the original work, reevaluation of the published data might provide some useful insights. It has previously been shown that vanadate undergoes a condcnsaLion reaction with carboxylates to Torn1 a product that is in rapid equilibration with its precursors (18). It is then necessary to analyze the original data in accordance with eq.…”

Section: Plienylglutamatementioning

confidence: 99%

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Condensation reactions between vanadate and small functionalized peptides in aqueous solution

Tracey¹,

Jaswal²,

Nxumalo³

et al. 1995

Can. J. Chem.

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Abstract:The role that histidyl, seryl, tyrosyl, and other side chains of small peptides play in the formation of vanadate complexes has been investigated using 'H, I3c, and "V nuclear magnetic resonance spectroscopy. Formation constants of product complexes in aqueous solution have been determined and the influence of pH on the equilibria established. The results revealed that, in histidine-containing compounds, the protonation state of the imidazole ring of the free ligand strongly influences product formation. The results unequivocally showed that no vanadium-to-imidazole bond was formed for any of the histidine-containing complexes studied. However, imidazole and other aromatic side-chain residues have an effect on product stability via their influence on the protonation state (pK,) of the products. Aliphatic side-chains, such as those in asparagine or glutamate, do not appear to play a significant role in the formation of products. This is not true, however, of serine or threonine where the side-chains readily generate vanadium-oxygen bonds.

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Section: Plienylglutamatecontrasting

confidence: 58%

Section: Plienylglutamatementioning

confidence: 95%

Section: Plienylglutamatementioning

confidence: 99%

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Condensation reactions between vanadate and small functionalized peptides in aqueous solution

Tracey¹,

Jaswal²,

Nxumalo³

et al. 1995

Can. J. Chem.

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“…Since its discovery, AnI was used as a laboratory model enzyme for the understanding of VHPO properties. Numerous further studies were carried out to characterize the V coordination inside the active site of AnI (later called An-VBPOI in this review), based on electron paramagnetic resonance [26,34,35], on 51 V NMR [36][37][38], X-ray crystallography [39,40] and on XAS ( [41][42][43] see below).…”

Section: Ascophylum Nodosummentioning

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

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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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“…Vanadylkationen und Vanadataninonen werden unter physiologischen Bedingungen leicht durch Redoxreaktionen ineinander überführt (Rehder 1995 …”

Section: Metabolismusunclassified

Vanadium und seine anorganischen Verbindungen [MAK Value Documentation in German language, 2006]

2012

The MAK‐Collection for Occupational Health and Safety

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(Model) investigations of the function of vanadium in biological systems

Cited by 19 publications

References 0 publications

Condensation reactions between vanadate and small functionalized peptides in aqueous solution

Condensation reactions between vanadate and small functionalized peptides in aqueous solution

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

Vanadium und seine anorganischen Verbindungen [MAK Value Documentation in German language, 2006]

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