Studies on transition metal peroxo complexes—X. The nature of peroxovanadates in aqueous solution

Campbell, N. J.; Dengel, Andrew C.; Griffith, William P.

doi:10.1016/s0277-5387(00)86249-x

Cited by 91 publications

(44 citation statements)

References 31 publications

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“…In a solution of vanadate and excess H 2 O 2 at a pH >5, formation of diperoxovanadate species is favored [36,37]. Tungsten also has strong affinity for peroxide and the composition of peroxotungsten species has been known to be sensitive to pH [38,39]. Thus, in the present study, the strategically maintained pH of approximately 5.5 was found to be conducive for the successful synthesis of the desired pV and pW compounds.…”

Section: Discussionmentioning

confidence: 55%

“…The importance of pH for the successful synthesis of peroxo metal compounds has been emphasized in the literature [36][37][38][39]. In a solution of vanadate and excess H 2 O 2 at a pH >5, formation of diperoxovanadate species is favored [36,37].…”

Section: Discussionmentioning

confidence: 99%

“…The main general features are presented in Table 1.The strong absorption at approximately 960 cm −1 has been assigned to the ν(M=O) mode of terminal M=O (M=V or W) group. The bands observed for peroxo group were in the range characteristic of side-on-bound peroxo ligand [36][37][38][39] The presence of coordinated peptide in the complexes pW1 and pV1 was evident from their IR spectra, which showed characteristic differences between the spectral pattern originating from triglycine in the complexes and that of free peptide. The IR spectra of triglycine and a limited number of metal complexes with coordinated triglycine were investigated previously [40][41][42].…”

Section: Synthesis and Characterizationmentioning

confidence: 95%

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Kinetics of Inhibition of Rabbit Intestine Alkaline Phosphatase by Heteroligand Peroxo Complexes of Vanadium(V) and Tungsten(VI)

Kalita

Das

Islam

2008

Biol Trace Elem Res

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The present work was undertaken to examine and compare some biologically important properties of peroxo compounds of V(V) and W(VI) containing biogenic species as ancillary ligand. New anionic peroxovanadate(V) complex of the type Na[VO(O(2))(2)(triglycine)].3H(2)O (pV1) and a molecular peroxotungstate(VI) [WO(O(2))(2)(triglycine)].3H(2)O (pW1) were synthesized and characterized for the purpose and their stability in solution was ascertained. Studies on kinetics of inhibition of alkaline phosphatase activity by the newly synthesized compounds and series of dipeptide and amino acid containing peroxo complexes of vanadium and tungsten synthesized previously by us viz., Na[VO(O(2))(2)(gly-gly)(H(2)O)].H(2)O (gly-gly = glycyl-glycine), Na[VO(O(2))(2)(asn)].H(2)O (asn = asparagine), Na[VO(O(2))(2)(gln)].H(2)O (gln = glutamine), and [WO(O(2))(2)(gly-gly)(H(2)O)].3H(2)O, revealed that each of these species is a potent mixed-type inhibitor of the enzyme. Significant difference was noted between the peroxovanadium (pV) and peroxotungsten (pW) compounds in terms of their oxidant activity with reduced glutathione.

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Section: Discussionmentioning

confidence: 55%

Section: Discussionmentioning

confidence: 99%

Section: Synthesis and Characterizationmentioning

confidence: 95%

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Kinetics of Inhibition of Rabbit Intestine Alkaline Phosphatase by Heteroligand Peroxo Complexes of Vanadium(V) and Tungsten(VI)

Kalita

Das

Islam

2008

Biol Trace Elem Res

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“…61,62 In a solution of vanadate or molybdate and excess H 2 O 2 at a pH ≥ 5, formation of diperoxo species of these metals is favoured. 16,87,88 We have observed that formation of the [MO(O 2 ) 2 ] (M = V or Mo) moieties and their coordination to the macroligands occurred optimally at near neutral pH.…”

Section: Synthesis and Characterizationmentioning

confidence: 99%

Macromolecular peroxo complexes of Vanadium(V) and Molybdenum(VI): Catalytic activities and biochemical relevance

Islam

Boruah

2015

J Chem Sci

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Our recent achievements concerning the synthesis and characterization of water soluble peroxo complexes of V(V) and Mo(VI) in macroligand environment, as well as some key features of biological relevance of these compounds, such as their hydrolytic stability, activity with phosphohydrolase enzyme vis-à-vis free peroxovanadium (pV) or peroxomolybdenum (pMo) complexes, and their activity in biomimetic oxidative bromination are presented here. Immobilization of pMo species on insoluble polymer matrices viz., amino acid functionalized Merrifield resins and poly(acrylonitrile) on the other hand, afforded a set of heterogeneous catalysts highly effective in facile organic transformations such as selective oxidation of organic sulfides and oxidative bromination of aromatic substrates by H 2 O 2 , at ambient temperature. The methodologies are straightforward, high-yielding, halogen-free and the catalysts afford easy regeneration. Our findings illustrate the various features which make the procedures sustainable and synthetically useful.

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“…Both diperoxovanadate and monoperoxovanadate are assumed to possess a seven-coordinated pentagonal bipyramidal geometry (25,38,39). Because of the reactivity of the peroxo group with thiols, we had expected the monoperoxovanadate to have a considerable biological activity.…”

Section: Thiol-induced Inactivation Of Pv and Pmo: Mathematical Modelmentioning

confidence: 99%

Properties of Pervanadate and Permolybdate

Mikalsen¹,

Kaalhus²

1998

Journal of Biological Chemistry

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Pervanadate and permolybdate are irreversible protein-tyrosine phosphatase inhibitors, with IC 50 values of 0.3 and 20 M, respectively, in intact cells. Maximal inhibition was obtained within 1 min at higher concentrations of the compounds. They induced prominent changes in the phosphorylation status of the gap junction protein, connexin43. These effects were utilized as model systems to assess the stability and inactivation of the compounds. Although the concentrated stock solutions were relatively stable, the diluted compounds were unstable. The biological activity had decreased to 20 -30% after 6 h of incubation in a phosphate buffer, 1 h in phosphate buffer with 10% fetal calf serum, and 1-3 minutes in culture medium. Thiols reacted rapidly with the compounds and inactivated them (initial reaction rates with cysteine: permolybdate > pervanadate > H 2 O 2 ). Catalase inactivated the compounds, and permolybdate was the more sensitive. The cells inactivated permolybdate faster than pervanadate. Cellular inactivation of permolybdate, and to a lesser degree pervanadate, appeared to be partly dependent on catalase and thiols. However, a general decrease in cellular thiols was not the mediator of the biological effects of pervanadate or permolybdate. Mathematical modeling of the thiol reactivity suggested that monoperoxovanadate at maximum could possess 20% of the biological activity of diperoxovanadate.

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Studies on transition metal peroxo complexes—X. The nature of peroxovanadates in aqueous solution

Cited by 91 publications

References 31 publications

Kinetics of Inhibition of Rabbit Intestine Alkaline Phosphatase by Heteroligand Peroxo Complexes of Vanadium(V) and Tungsten(VI)

Kinetics of Inhibition of Rabbit Intestine Alkaline Phosphatase by Heteroligand Peroxo Complexes of Vanadium(V) and Tungsten(VI)

Macromolecular peroxo complexes of Vanadium(V) and Molybdenum(VI): Catalytic activities and biochemical relevance

Properties of Pervanadate and Permolybdate

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