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Vanadate

About: Vanadate is a research topic. Over the lifetime, 4497 publications have been published within this topic receiving 120109 citations. The topic is also known as: vanadate.


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Journal ArticleDOI
TL;DR: When Trypanosoma brucei procyclic trypomastigotes were permeabilized with digitonin in a reaction medium containing MgATP, succinate, and 3.5 microM free Ca2+, they lowered the medium Ca2+ concentration to the submicromolar level, a range that correlates favorably with that detected in the intact cells with fura-2.

61 citations

Journal ArticleDOI
TL;DR: It is proposed that the orthovanadate inhibition of MutS ATPase can take place by a similar mechanism to that described for other ATPases, and considering that vanadate is an intracellular trace component, this compound could be considered as a new modulator of the MMRS.
Abstract: MutS, a member of the ABC ATPases superfamily, is a mismatch DNA-binding protein constituent of the DNA post-replicative mismatch repair system (MMRS). In this work, it is shown that the ATPase activity of Pseudomonas aeruginosa and Escherichia coli MutS is inhibited by ortho- and decavanadate. Structural comparison of the region involved in the ATP binding of E.coli MutS with the corresponding region of other ABC ATPases inhibited by vanadate, including the myosin‐ orthovanadate‐Mg complex, showed that they are highly similar. From these results it is proposed that the orthovanadate inhibition of MutS ATPase can take place by a similar mechanism to that described for other ATPases. Docking of decavanadate on the ATP-binding region of MutS showed that the energetically more favorable interaction of this compound would take place with the complex MutS‐ ADP‐Mg, suggesting that the inhibitory effect could be produced by a steric impediment of the protein ATP/ADP exchange. Besides the effect observed on the ATPase activity, vanadate also affects the DNAbinding capability of the protein, and partially inhibits the oligomerization of MutS and the temperature-induced inactivation of the protein. From the results obtained, and considering that vanadate is an intracellular trace component, this compound could be considered as a new modulator of the MMRS.

60 citations

Journal ArticleDOI
TL;DR: In this paper, vanadate-substituted hydroxyapatite was used as a catalysts for the de-hydrogenation of propane in the presence of gaseous oxygen in the feedstream.
Abstract: Calcium hydroxyapatites substituted with vanadate were prepared for use as catalysts in the oxidative dehydrogenation of propane. Phosphate in the hydroxyapatite could not be fully substituted by vanadate, but partial substitution achieved an atomic ratio of V/P = 0.15. The conversion for propane and the selectivity for propylene increased from 5.9 and 1.4% on calcium hydroxyapatite to 16.5 and 54.2%, respectively, for vanadate incorporation in hydroxyapatite at V/P = 0.10 (atomic ratio). The latter correspond to results for Mg2V2O7 under the same reaction conditions (14.0 and 50.9%, respectively), which is generally accepted as an active catalyst for oxidative dehydrogenation. Dehydrogenation in the absence of gaseous oxygen in the feedstream on vanadate-substituted hydroxyapatite and 51V MAS NMR analyses of the catalysts used suggest that the abstraction and incorporation of lattice oxygen from and in vanadate, followed by redox between V4+ and V5+, directly contribute to the activation of propane. The effects of P(C3H8)/P(O2) in the feedstream and the catalyst weight on the oxidative dehydrogenation of propane over hydroxyapatite substituted with vanadate at V/P = 0.10 are also described.

60 citations

Journal ArticleDOI
TL;DR: In this article, the equilibrium concentrations of Na3VO4, NaVO3, and V2O5 in a mixed sodium sulfate-vanadate solution containing 30 mol% vanadate as a function of melt basic were derived.
Abstract: Thermodynamic calculations for the equilibrium concentrations of Na3VO4, NaVO3, and V2O5 in a mixed sodium sulfate-vanadate solution containing 30 mol% vanadate as a function of melt basic...

60 citations

Journal ArticleDOI
TL;DR: The known binding competition between the two cations and their opposite effects on the phosphorylation reaction suggest that interdependence of phosphorylated site, H+ sites, and Ca2+ sites is a basic mechanistic feature of enzyme catalysis and cation transport.

60 citations


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Performance
Metrics
No. of papers in the topic in previous years
YearPapers
2023109
2022211
202178
202075
201996
201899