Structure of Monovanadates in Aqueous Solution.

Harnung, Sven E.; Larsen, Edwin M.; Pedersen, Erik; Sletten, Einar; Roos, Björn O.; Pietikäinen, Pirjo; Setälä, Harri; Trætteberg, M.; Nasiri, Ahmad; Tsuda, Tadashi

doi:10.3891/acta.chem.scand.47-0674

Cited by 18 publications

(13 citation statements)

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“…The concomitant presence in the ESI droplets, where a precise definition of the pH value is not possible, of the alcoxy derivatives, however, suggests 1 as the most likely structure in place of solvated [VO 2 (H 2 O) n ] + species. From neutral to alkaline medium, V(V) exists primarily as monomeric oxyanion (VO 3À 4 , HVO 2À 4 , H 2 VO À 4 ) [16] in agreement with ESI-MS findings [12]. Vanadium ions have many structural roles in living organisms that reflect the analogy with phosphorous.…”

Section: Monoperoxo Compoundsmentioning

confidence: 64%

“…As pointed out in the first part of this section, in alkaline medium and in the absence of hydrogen peroxide, V(V) exists primarily as monomeric oxyanions (VO 3À 4 ; HVO 2À 4 ; H 2 VO À 4 ) [16,30] in agreement also with ESI-MS findings that are visualized in Scheme 2 [12]. The negative-ion mode mass spectrum, observed after the addition of H 2 O 2 (equimolar to V(V)) and obtained in H 2 O-Pr i OH as infusion solvent, consists essentially of two ionic species centered at m/z 201 and 217.…”

Section: V(v)/h 2 O 2 /H + /Br -mentioning

confidence: 99%

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Vanadium (V) peroxocomplexes: Structure, chemistry and biological implications

Bortolini

Conte

2005

Journal of Inorganic Biochemistry

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Section: Monoperoxo Compoundsmentioning

confidence: 64%

Section: V(v)/h 2 O 2 /H + /Br -mentioning

confidence: 99%

Vanadium (V) peroxocomplexes: Structure, chemistry and biological implications

Bortolini

Conte

2005

Journal of Inorganic Biochemistry

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“…preted in terms of a pentacoordinate hydrate 6a with one additional water molecule in the coordination sphere. 36 More recent thermodynamic data, on the other hand, argue against such an increase in coordination number at this stage. 37 All attempts to optimize a structure resembling 6a resulted in expulsion of the water from the coordination sphere, 38 Ž .…”

Section: Anionic Speciesmentioning

confidence: 99%

Theoretical study of a vanadate peptide complex

Bühl

1999

J. Comput. Chem.

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“…These studies have clearly shown that, under conditions of a few millimolar concentrations of vanadate with equivalent amounts of ligand at neutral pH, the major product of the reaction is a binuclear bisligand product. Early studies proposed that the coordination about the vanadium in this type of product was trigonal bipyramidal (21), although there has been some controversy over the details of the structure (5,16,18). A recent X-ray structure of an adenosine-vanadate dimer showed a slightly distorted square-pyramidal coordination about each of the vanadium nuclei of the dimer in the crystalline material (22).…”

Section: Uridine 56-dihydrouridine and Methyl P-dribofuranoside Plmentioning

confidence: 99%

“…The interactions of vanadate with nucleosides (4,(16)(17)(18)(19)(20) and P-methylriboside (5) have been studied by a number of workers. These studies have clearly shown that, under conditions of a few millimolar concentrations of vanadate with equivalent amounts of ligand at neutral pH, the major product of the reaction is a binuclear bisligand product.…”

Section: Uridine 56-dihydrouridine and Methyl P-dribofuranoside Plmentioning

confidence: 99%

Influence of vanadium(V) complexes on the catalytic activity of ribonuclease A. The role of vanadate complexes as transition state analogues to reactions at phosphate

Leon-Lai¹,

Gresser²,

Tracey³

1996

Can. J. Chem.

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Abstract:The interactions of vanadate and its complexes of uridine, 5,6-dihydrouridine, and methyl P-D-ribofuranoside with bovine pancreatic ribonuclease A (RNase A) (EC 3.1.27.5) were studied by 5 1~ NMR spectroscopy and enzyme kinetics. From kinetic studies, it was found that neither inorganic vanadate nor the methyl P-D-ribofuranoside-vanadate complex significantly inhibited the RNase A catalyzed hydrolysis of uridine 2',3'-cyclic monophosphate. The NMR binding studies were in full agreement with the kinetics studies and showed that neither inorganic vanadate nor the methyl P-D-ribofuranoside-vanadate complex was bound tightly by the enzyme. Approximate binding constants were (5.0 + 1.0) x M and (3.0 + 0.6) x M for the uridine-and 5.6-dihydrouridine-vanadate complexes, respectively. An induced-fit mechanism is suggested, in which the pyrimidine subsite of the active site of RNase A must be fully occupied for the enzyme to be able to tightly bind the transition state or transition state analog. Calculation of the binding energies of vanadate complexes in ribonuclease, phosphoglycerate mutase, and phosphoglucomutase revealed an excess of binding energy over the analogous phosphate derivative of about 25 kJ/mol for all enzymes, even though the binding constants themselves varied by about six orders of magnitude. This energy represents about 40% of that expected to be available for a trigonal-bipyramidal transition state and requires a reassessment of the role of vanadate as a transition state analogue for phosphate transfer.Key words: vanadate, ribonuclease, transition state, binding constants, phosphate analogues, kinetics.Resum6 : Faisant appel a la spectrscopie RMN du 5 1~ et de la cinCtique des enzymes, on a CtudiC les interactions entre le vanadate et ses complexes de I'uridine, de la 5,6-dihydrouridine et du P-D-ribofuranoside de mCthyle avec la ribunuclease A du pancrCas de boeuf (RNase A) (EC 3.1.27.5). Sur la base des Ctudes cinCtiques, on a trouvC que, vis-a-vis de I'hydrolyse du monophosphate 2',3'-cyclique de I'uridine de la RNase A, ni le vanadate inorganique ni le complexe du P-D-ribofuranoside de mCthyle-vanadate n'inhibent cette rCaction d'une f a~o n significative. Les Ctudes par RMN ont montrt qu'il ne se produit aucune fixation entre ces matCriaux et elles Ctaient en parfait accord avec les ttudes cinCtiques; elles montrent aussi que ni le vanadate inorganique ni le complexe du P-D-ribofuranoside de mCthyle-vanadate ne se complexent fortement avec I'enzyme. Les constantes apparentes de fixation ont respectivement de (5,O + 1.0) x M et (3,O + 0.6) x M pour les complexes de I'uridine et du 5,6-dihydrouridine avec le vanadate. On propose un mCcanisme induit d'ajustement dans lequel il est important que tout le sous site de la pyrimidine du site actif de la RNase A soit occupC pour que I'enzyme soit capable de bien fixer 1'Ctat de transition ou son analogue. Des calculs d'Cnergie de fixation des complexes du vanadate dans la ribonucltase, la phosphoglycCratemutase ou la phosphoglucomutase ont rCvC...

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Structure of Monovanadates in Aqueous Solution.

Cited by 18 publications

References 0 publications

Vanadium (V) peroxocomplexes: Structure, chemistry and biological implications

Vanadium (V) peroxocomplexes: Structure, chemistry and biological implications

Theoretical study of a vanadate peptide complex

Influence of vanadium(V) complexes on the catalytic activity of ribonuclease A. The role of vanadate complexes as transition state analogues to reactions at phosphate

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