NADH-dependent decavanadate reductase, an alternative activity of NADP-specific isocitrate dehydrogenase protein

Rao, Aparna V. S.; Ramasarma, T.

doi:10.1016/s0304-4165(00)00026-x

Cited by 19 publications

(16 citation statements)

References 44 publications

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“…In fact, it is known that the mechanism of vanadate-promoted photocleavage reaction on myosin involves addition of molecular oxygen to a stabilized seryl radical generated by a light-catalyzed vanadate (V 5+ ) reduction to vanadyl (V 4+ ) [28]. It was also recently shown that V 5+ of V 10 is more easily reduced in comparison to V 1 , V 2 and V 4 present in metavanadate solutions [29]. These observations could account for the rapid decomposition of the decameric vanadate (V 10 ), upon protein addition, into vandyl species after a short irradiation time as described above (Fig.…”

Section: Resultsmentioning

confidence: 99%

Decavanadate as a biochemical tool in the elucidation of muscle contraction regulation

Tiago

Aureliano

Moura

2004

Journal of Inorganic Biochemistry

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Recently reported decameric vanadate (V 10 ) high affinity binding site in myosin S1, suggests that it can be used as a tool in the muscle contraction regulation. In the present article, it is shown that V 10 species induces myosin S1 cleavage, upon irradiation, at the 23 and 74 kDa sites, the latter being prevented by actin and the former blocked by the presence of ATP. Identical cleavage patterns were found for meta-and decavanadate solutions, indicating that V 10 and tetrameric vanadate (V 4 ) have the same binding sites in myosin S1. Concentrations as low as 50 lM decavanadate (5 lM V 10 species) induces 30% of protein cleavage, whereas 500 lM metavanadate is needed to attain the same extent of cleavage. After irradiation, V 10 species is rapidly decomposed, upon protein addition, forming vanadyl (V 4+ ) species during the process. It was also observed by NMR line broadening experiments that, V 10 competes with V 4 for the myosin S1 binding sites, having a higher affinity. In addition, V 4 interaction with myosin S1 is highly affected by the products release during ATP hydrolysis in the presence or absence of actin, whereas V 10 appears to be affected at a much lower extent. From these results it is proposed that the binding of vanadate oligomers to myosin S1 at the phosphate loop (23 kDa site) is probably the cause of the actin stimulated myosin ATPase inhibition by the prevention of ATP/ADP exchange, and that this interaction is favoured for higher vanadate anions, such as V 10 .

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Section: Resultsmentioning

confidence: 99%

Decavanadate as a biochemical tool in the elucidation of muscle contraction regulation

Tiago

Aureliano

Moura

2004

Journal of Inorganic Biochemistry

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“…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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“…V 10 appears not to be affected by the products release during ATP hydrolysis, as shown by the NMR experiments. In addition, V 10 has a greater affinity for myosin binding sites than V 4 in the same way that, V 4 has a greater affinity than the lower vanadate oligomers, which can be explained if electrostatic forces play an important role in vanadate interaction with proteins that binds V 10 such as myosin, sarcoplasmic reticulum calcium pump and other nucleotide binding enzymes [21,23,24,[26][27][28]. In that sense, V 10 may contribute to the inhibition of actin-stimulated myosin ATPase activity, through binding at the myosin phosphate loop.…”

Section: The Iceberg Phenomena: Interactions and Enzyme Effectsmentioning

confidence: 99%

“…In that sense, it is of particularly importance the study of the structure of decavanadate formation in the presence of organic compounds [25]. Moreover, decavanadate modulates voltage-dependent Ca 2+ -active cation channel [26], mimics noradrenaline action [27] and induces decavanadate reductase activity [28].…”

Section: Introductionmentioning

confidence: 99%

Decavanadate effects in biological systems

Aureliano

Gândara

2005

Journal of Inorganic Biochemistry

117

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Vanadium biological studies often disregarded the formation of decameric vanadate species known to interact, in vitro, with high-affinity with many proteins such as myosin and sarcoplasmic reticulum calcium pump and also to inhibit these biochemical systems involved in energy transduction. Moreover, very few in vivo animal studies involving vanadium consider the contribution of decavanadate to vanadium biological effects. Recently, it has been shown that an acute exposure to decavanadate but not to other vanadate oligomers induced oxidative stress and a different fate in vanadium intracellular accumulation. Several markers of oxidative stress analyzed on hepatic and cardiac tissue were monitored after in vivo effect of an acute exposure (12, 24 h and 7 days), to a sub-lethal concentration (5 mM; 1 mg/kg) of two vanadium solutions (''metavanadate'' and ''decavanadate''). It was observed that ''decavanadate'' promote different effects than other vanadate oligomers in catalase activity, glutathione content, lipid peroxidation, mitochondrial superoxide anion production and vanadium accumulation, whereas both solutions seem to equally depress reactive oxygen species (ROS) production as well as total intracellular reducing power. Vanadium is accumulated in mitochondria in particular when ''decavanadate'' is administered. These recent findings, that are now summarized, point out the decameric vanadate species contributions to in vivo and in vitro effects induced by vanadium in biological systems.

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NADH-dependent decavanadate reductase, an alternative activity of NADP-specific isocitrate dehydrogenase protein

Cited by 19 publications

References 44 publications

Decavanadate as a biochemical tool in the elucidation of muscle contraction regulation

Decavanadate as a biochemical tool in the elucidation of muscle contraction regulation

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

Decavanadate effects in biological systems

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