Binding of vanadate (V) to ribonuclease-T1 and inosine, investigated by 15V NMR spectroscopy

Rehder, Dieter; Holst, Hartmut; Quaas, Rainer; Hinrichs, W.; Hahn, Ulrich

doi:10.1016/0162-0134(89)80037-6

Cited by 37 publications

(30 citation statements)

References 17 publications

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“…51 V spectra of both the ␤-lactamase and ␣-chymotrypsin complexes contained a broad resonance with maximum intensity around Ϫ510 ppm (vs VOCl 3 ). This is consistent with, but does not unequivocally prove, the presence of a 5-coordinated dioxovanadium species (6,15); it is, however, similar to the 51 V NMR resonance of most likely pentacoordinate (16) vanadium in the inosine/ vanadate/ribonuclease T 1 complex (17). Tetrahedral vanadate at the active site is also possible.…”

Section: Shown Inmentioning

confidence: 67%

Inhibition of Serine Amidohydrolases by Complexes of Vanadate with Hydroxamic Acids

Bell

Curley

Pratt

2000

Biochemical and Biophysical Research Communications

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Section: Shown Inmentioning

confidence: 67%

Inhibition of Serine Amidohydrolases by Complexes of Vanadate with Hydroxamic Acids

Bell

Curley

Pratt

2000

Biochemical and Biophysical Research Communications

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“…This stoichiometry for a diol system has previously been reported by others, 14-19,24 although a 1:1 stoichiometry has also been proposed. 32,33 However, a -2 charged 2:2 species alone does not fit the data satisfactorily. Since deviations were prevalent for data acquired at neutral to alkaline pH, a deprotonated complex was added to the speciation scheme.…”

Section: Resultsmentioning

confidence: 99%

Speciation in Vanadium Bioinorganic Systems. 5. Interactions between Vanadate, Uridine, and ImidazoleAn Aqueous Potentiometric, ⁵¹V, ¹⁷O, and ¹³C NMR Study

et al. 1998

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The full speciation has been determined in the aqueous vanadate-uridine (UrH 2 ) and vanadate-uridine-imidazole (ImH) systems. The studies performed allow direct comparison with the corresponding adenosine systems, and the role of the pyrimidine and purine bases on various complex properties could be evaluated. The studies also provide insight into possible biological mechanism of action. Formation constants have been determined in 0.600 M Na(Cl) medium at 25°C in the pH range 2-11, using a combination of potentiometry and 51 V NMR spectroscopy. In the H + -H 2 VO 4 --UrH 2 system, two dimeric complexes form: V 2 Ur 2 2-with log ) 7.66 ( 0.02 and V 2 Ur 2 3-with log ) -1.09 ( 0.04. The errors given are 3σ. Both species give rise to NMR resonances at -523 ppm. A minor 51 V NMR resonance at -507 ppm is probably originating from a VUr 2-species. No evidence was found for a 1:1 species at -523 ppm or a 1:1 species with 51 V NMR shift superimposed on the vanadate monomer. In the H + -H 2 VO 4 --UrH 2 -ImH system, two monomeric, mixed ligand species are formed: VUrIm -with log ) 3.12 ( 0.04 and VUrIm 2-with log ) -6.26 ( 0.20. The pK a values for the V 2 Ur 2 2-and VUrIm -species, 8.75 and 9.38, are both close to that of uridine (9.02) and are consistent with the interpretation that the deprotonation site is located on the base part of the nucleoside. For both the V 2 Ur 2 n-and VUrIm n-species, isomers have been identified. Equilibrium conditions are illustrated in distribution diagrams. A quantitative comparison with the analogous vanadate-adenosine and vanadate-adenosine-imidazole systems is presented. Furthermore, the solution structure of V 2 Ur 2 2-was examined using 17 O NMR spectroscopy. The complex gives rise to a broad resonance at approximately -1010 ppm, which at higher temperature sharpened into two signals of equal intensities at -1007 and -1032 ppm. This spectrum is consistent only with a solution structure containing pentacoordinate vanadium in an arrangement in which one hydroxyl group of the uridine forms an ester with one vanadium atom, and the other hydroxyl group bridges the two vanadium atoms. In addition, 13 C NMR studies revealed that the dinuclear vanadate-uridine species exchange while no evidence for intermolecular exchange between the complexes and free uridine was observed. The similarity between the vanadate-uridine and vanadate-adenosine complexes suggests that the role of the base in these complexes is very limited with respect to structural features and thermodynamic and kinetic properties.

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“…These requirements are for the simple peptides and can be bypassed if an amino acid segment which is accessible to vanadate contains an appropriately functionalized sidechain as in glycylserine and other peptides (8,11,12). Clearly, different sidechain substituents will apply different constraints to complex formation and this is a topic of continuing interest.…”

Section: Discussionmentioning

confidence: 99%

“…Of particular interest in this regard is the interactions of vanadate with amino alcohols (6,7), amino acids (8-lo), and 'Author to whom correspondence should be addressed. small peptides (9)(10)(11)(12). A good understanding of the interactions of vanadate with such materials will provide a firm basis for extension into studies of more complex systems.…”

Section: Introductionmentioning

confidence: 99%

Stereochemical requirements for the formation of vanadate complexes with peptides

Jaswal¹,

Tracey²

1991

Can. J. Chem.

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The condensation reactions occurring between vanadate and a number of amino aiids and simple peptides have been studied by 51V nuclear magnetic resonance. Vanadate and ligand stoichiometry has been established for the complexes formed and their formation constants determined. The amino acids were all found to undergo rather weak interactions with vanadate and in general provided two products with 51V chemical shifts near -545 and -555 ppm. The peptides also gave minor products with NMR signals occurring with that of vanadate itself. However, in this case, the major products occur at approximately -510 ppm. These latter complexes are monovanadate, monoligand complexes which require the terminal amino, the carboxylate groups and an unsubstituted nitrogen in the peptide linkage in order for product formation to occur. Sidechains promote product formation, apparently by favouring a more readily complexed peptide conformation. Formation constants vary from about 20 to 50 M-' depending on the sidechain. The carboxylate group can be replaced by a hydroxymethyl. This, however, leads to a significant decrease in product formation at pH 7. Hydrogen ion concentration studies showed that the complexes, when considered to be formed from VO4H2-and neutral peptide, did not require or give off protons. However, when the carboxylate was replaced by the alcohol functionality a proton was released. On the basis of this study the coordination of the vanadatelpeptide complexes has been assigned.

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Binding of vanadate (V) to ribonuclease-T1 and inosine, investigated by 15V NMR spectroscopy

Cited by 37 publications

References 17 publications

Inhibition of Serine Amidohydrolases by Complexes of Vanadate with Hydroxamic Acids

Inhibition of Serine Amidohydrolases by Complexes of Vanadate with Hydroxamic Acids

Speciation in Vanadium Bioinorganic Systems. 5. Interactions between Vanadate, Uridine, and ImidazoleAn Aqueous Potentiometric, ⁵¹V, ¹⁷O, and ¹³C NMR Study

Stereochemical requirements for the formation of vanadate complexes with peptides

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Binding of vanadate (V) to ribonuclease-T1 and inosine, investigated by 15V NMR spectroscopy

Cited by 37 publications

References 17 publications

Inhibition of Serine Amidohydrolases by Complexes of Vanadate with Hydroxamic Acids

Inhibition of Serine Amidohydrolases by Complexes of Vanadate with Hydroxamic Acids

Speciation in Vanadium Bioinorganic Systems. 5. Interactions between Vanadate, Uridine, and ImidazoleAn Aqueous Potentiometric, 51V, 17O, and 13C NMR Study

Stereochemical requirements for the formation of vanadate complexes with peptides

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Speciation in Vanadium Bioinorganic Systems. 5. Interactions between Vanadate, Uridine, and ImidazoleAn Aqueous Potentiometric, ⁵¹V, ¹⁷O, and ¹³C NMR Study