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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: In this paper, the first monoclinic copper vanadate (n-type Cu2V2O7) thin film photoanodes were prepared by spray pyrolysis and evaluated for photoelectrochemical (PEC) water oxidation.
Abstract: Monoclinic copper vanadate (n-type Cu2V2O7) thin film photoanodes were prepared for the first time by spray pyrolysis and evaluated for photoelectrochemical (PEC) water oxidation. The spray pyrolys...

44 citations

Journal ArticleDOI
TL;DR: In this paper, the authors investigated the effect of V2O5 on the coordination number of the vanadate and lead structural units in the presence of Li2O and found that the decrease in density is related to the replacement of high dense PbO with low dense one V 2O5, where the increase in the molar volume can be attributed to the larger packing factor of V 2 o5 than that of Pb o.

44 citations

Journal ArticleDOI
TL;DR: The competitive inhibition pattern with respect to NAD and NADP suggests the possibility that vanadate oligomers may also inhibit catalysis of other NAD- or NADP-requiring dehydrogenases.
Abstract: Vanadate dimer and tetramer inhibit glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides. The inhibition by a vanadate mixture containing vanadate monomer, dimer, tetramer, and pentamer was determined by measuring the rates of glucose 6-phosphate oxidation and reduction of NAD (or NADP) catalyzed by glucose-6-phosphate dehydrogenase. The inhibition by vanadate is competitive with respect to NAD or NADP and noncompetitive (a mixed type) with respect to glucose 6-phosphate (G6P) when NAD or NADP are cofactors. This inhibition pattern varies from that observed with phosphate and thus suggests vanadate interacts differently than a phosphate analogue with the enzyme. 51V NMR spectroscopy was used to directly correlate the inhibition of vanadate solutions to the vanadate dimer and/or tetramer, respectively. The activity of the vanadate oligomer varied depending on the cofactor and which substrate was being varied. The vanadate dimer was the major inhibiting species with respect to NADP. This is in contrast to the vanadate tetramer, which was the major inhibiting species with respect to G6P and with respect to NAD. The inhibition by vanadate when G6P was varied was weak. The competitive inhibition pattern with respect to NAD and NADP suggests the possibility that vanadate oligomers may also inhibit catalysis of other NAD- or NADP-requiring dehydrogenases. Significant concentrations of vanadate dimer and tetramer are only found at fairly high vanadate concentrations, so these species are not likely to represent vanadium species present under normal physiological conditions. It is however possible the vanadate dimer and/or tetramer represent toxic vanadate species.

44 citations

Journal ArticleDOI
TL;DR: Results are interpreted as evidence that a plasma membrane redox system in root cells is closely associated with the ATPase which can drive K+ transport, and membrane components common to theredox system and ATPase function in the transport of K+.
Abstract: Carrot (Daucus carota L.) cells grown in suspension culture oxidized exogeneous NADH. The NADH oxidation was able to stimulate K+ (86Rb+) transport into cells, but it did not affect sucrose transport.N,N'-Dicyclohexyl-carbodiimide, diethylstilbestrol, and oligomycin, which only partially inhibited NADH oxidation, almost completely collapsed the K+ (86Rb+) transport. Vanadate, which is less effective as an ion transport inhibitor, was less effective in inhibiting the NADH-driven transport of K+ (86Rb+).p-Fluormethoxycarbonylcyanide phenylhydrazone inhibits the K+ transport over 90% including that induced by NADH. The results are interpreted as evidence that a plasma membrane redox system in root cells is closely associated with the ATPase which can drive K+ transport. Because of the inhibitor effects, it appears that membrane components common to the redox system and ATPase function in the transport of K+.

44 citations

Journal ArticleDOI
TL;DR: These data provide the first experimental evidence for the view that functional coupling of the ATPase domain of an ABC transporter to the membrane-integral domains is crucial for conferring sensitivity to vanadate and bafilomycin A1.

44 citations


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