Vanadate-stimulated NADH oxidation by xanthine oxidase: An intrinsic property

Khandke, Lakshmi; Gullapalli, Sharada; Patole, Milind S.; Ramasarma, T.

doi:10.1016/0003-9861(86)90643-0

Cited by 27 publications

(8 citation statements)

References 20 publications

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“…The dehydrogenases of alcohol, aldehyde and glucose-6-phosphate also showed small and heat-stable rates (data not shown). Addition of polyvanadate instead of xanthine oxidase gave a good stimulation and this did not require the presence of xanthine (line PV, panel A) in agreement with our previous report [13].…”

Section: Effect Of Some Dehydrogenases On Nadh Oxidation By Xanthine supporting

confidence: 90%

“…Indeed xanthine oxidase being a flavoprotein may be showing this activity as an intrinsic property [13]. On the other hand the discovery of NADPHspecific isocitrate dehydrogenase possessing the additional property of catalyzing the polyvanadatestimulated oxidation of NADH, and not NADPH, is significant both for understanding the mechanism of this reaction and cellular function of this protein.…”

Section: Discussionmentioning

confidence: 99%

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Stimulation of NADH oxidation by xanthine oxidase and polyvanadate in presence of some dehydrogenases and flavin compounds

et al. 1991

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The rates of NADH oxidation in presence of xanthine oxidase increase to a small and variable extent on addition of high concentrations of lactate dehydrogenase and other dehydrogenases. This heat stable activity is similar to polyvanadate-stimulation with respect to pH profile and SOD sensitivity. Isocitric dehydrogenase (NADP-specific) showed heat labile, SOD-sensitive polyvanadate-stimulated NADH oxidation activity. Polyvanadate-stimulated SOD-sensitive NADH oxidation was also found to occur with riboflavin, FMN and FAD in presence of a non-specific protein, BSA, suggesting that some flavoproteins may possess this activity.

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Section: Effect Of Some Dehydrogenases On Nadh Oxidation By Xanthine supporting

confidence: 90%

Section: Discussionmentioning

confidence: 99%

Stimulation of NADH oxidation by xanthine oxidase and polyvanadate in presence of some dehydrogenases and flavin compounds

et al. 1991

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“…cat ventricles, human heart erythrocytes, mouse liver plasma membranes and rat liver microsomes was stimulated by vanadates, [6][7][8] Vanadates are capable of oxidizing NADH under non-enzymic conditions. Isopolydecavanadate in presence of phosphate buffer was found to be an effective oxidant of NADH compared to other forms of vanadates viz.…”

Section: Mechanismmentioning

confidence: 99%

“…1-3 Studies on the electron transfer reaction of NADH and its synthetic analogue were reported by several workers. [4][5][6][7][8][9][10] The mechanism of reaction of NADH largely depends on the nature of oxidants. When the oxidants are iminium ions of activated carbonyl compounds 11 and quinone, 12 there is a transfer of hydride ion from the 4th position of the dihydropyridine ring to the oxidizing agent in the rate limiting step (scheme 1).…”

Section: Nadhmentioning

confidence: 99%

Studies on electron transfer reactions of Keggin-type mixed addenda heteropolytungstovanadophosphates with NADH

Sami

Rajasekaran

2009

J Chem Sci

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The coenzyme nicotinamide adenine dinucleotide (NADH) undergoes facile electron transfer reaction with vanadium (V) substituted Keggin-type heteropolyanions (HPA) [PV V W 11 O 40 ] 4-(PV 1 ) and [PV V 2 W 10 O 40 ] 5-(PV 2 ) in aqueous phosphate buffer of pH 6 at ambient temperature. Electrochemical and optical studies show that the stoichiometry of the reaction is 1 : 2 (NADH : HPA). EPR and optical studies show that HPA act as one electron acceptor and the products of electron transfer reactions are one electron reduced heteropoly blues (HPB), viz. [PV IV W 11 O 40 ] 5-and [PV IV V V W 10 O 40 ] 6-.Oxygraph measurements show that there is no uptake of molecular oxygen during the course of reaction. The reaction proceeds through multi-step electron-proton-electron transfer mechanism, with rate limiting initial one electron transfer from NADH to HPA by outer sphere electron transfer process. Bimolecular rate constant for electron transfer reaction between NADH and PV 2 in phosphate buffer of pH = 6 has been determined spectrophotometrically.

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“…In addition, vanadate may also stimulate nonenzymatic vanadate-dependent oxidation of NAD(P)H by using xanthine-oxidase reaction as a source of superoxide Khandke et al 1986;Liochev and Fridovich 1986), which will possibly lead to the formation of ROS or RONS. But it is still uncertain whether nonenzymatic vanadate-dependent NADH oxidation is actually coupled with NADPH oxidase-mediated superoxide production.…”

Section: Electron Transfer Reactions Of Vanadatementioning

confidence: 98%

Chemical, Biochemical, and Biological Behaviors of Vanadate and Its Oligomers

Wang

2013

Biomedical Inorganic Polymers

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Vanadate is widely used as an inhibitor of protein tyrosine phosphatases (PTPase) and is routinely applied in cell lysis buffers or immunoprecipitations of phosphotyrosyl proteins. Additionally, vanadate has been extensively studied for its antidiabetic and anticancer effects. In most studies, orthovanadate or metavanadate was used as the starting compound, whereas these "vanadate" solutions may contain more or less oligomerized species. Whether and how different species of vanadium compounds formed in the biological media exert specific biological effect is still a mystery. In the present commentary, we focus on the chemical, biochemical, and biological behaviors of vanadate. On the basis of species formation of vanadate in chemical and biological systems, we compared the biological effects and working mechanism of monovanadate with that of its oligomers, especially the decamer. We propose that different oligomers may exert a specific biological effect, which depends on their structures and the context of the cell types, by different modes of action.

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Vanadate-stimulated NADH oxidation by xanthine oxidase: An intrinsic property

Cited by 27 publications

References 20 publications

Stimulation of NADH oxidation by xanthine oxidase and polyvanadate in presence of some dehydrogenases and flavin compounds

Stimulation of NADH oxidation by xanthine oxidase and polyvanadate in presence of some dehydrogenases and flavin compounds

Studies on electron transfer reactions of Keggin-type mixed addenda heteropolytungstovanadophosphates with NADH

Chemical, Biochemical, and Biological Behaviors of Vanadate and Its Oligomers

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