Complexation of histidine and alanyl-histidine by vanadate in aqueous medium

Fritzsche, Martina; Vergopoulos, Vassilios; Rehder, Dieter

doi:10.1016/s0020-1693(00)82836-4

Cited by 28 publications

(22 citation statements)

References 32 publications

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“…Under these conditions a single product signal, at -51 1 ppm, was observed. This signal is close to that (-5 19 ppm) previously reported for the product of the condensation with alanylhistidine (13). To ascertain the stoichiometry of this product, it is first necessary to know whether additional products are formed.…”

Section: Glycylhistidinesupporting

confidence: 86%

“…The good linear relationship that was obtained yielded a formation constant of (1.01 + 0.06) x 10, M-I for Kl. The absence of upward curvature in the experimental data indicated that the -5 11 ppm NMR signal was not a composite signal deriving from products of VP and V,P stoichiometry in the fashion recently reported for the -5 19 ppm product formed from the reaction of alanylhistidine with vanadate (13). However, reanalysis of the alanylhistidine data given in Tables 2 and 3 of ref.…”

Section: Glycylhistidinementioning

confidence: 50%

“…However, reanalysis of the alanylhistidine data given in Tables 2 and 3 of ref. 13, according to eq. [4], gave two excellent linear relationships with no upward curvature, as shown in Figs.…”

Section: Glycylhistidinementioning

confidence: 99%

“…This work has been limited in scope, in part because of the complexity of the interactions involved, particularly when the peptides contain functionalized side chains. The involvement of histidine in complex formation with vanadate has been studied (13), as has that of asparagine ( l l ) , tyrosine (l4), aspartic acid (9,15), and serine ( I I).…”

Section: Introductionmentioning

confidence: 99%

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Condensation reactions between vanadate and small functionalized peptides in aqueous solution

Tracey¹,

Jaswal²,

Nxumalo³

et al. 1995

Can. J. Chem.

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Abstract:The role that histidyl, seryl, tyrosyl, and other side chains of small peptides play in the formation of vanadate complexes has been investigated using 'H, I3c, and "V nuclear magnetic resonance spectroscopy. Formation constants of product complexes in aqueous solution have been determined and the influence of pH on the equilibria established. The results revealed that, in histidine-containing compounds, the protonation state of the imidazole ring of the free ligand strongly influences product formation. The results unequivocally showed that no vanadium-to-imidazole bond was formed for any of the histidine-containing complexes studied. However, imidazole and other aromatic side-chain residues have an effect on product stability via their influence on the protonation state (pK,) of the products. Aliphatic side-chains, such as those in asparagine or glutamate, do not appear to play a significant role in the formation of products. This is not true, however, of serine or threonine where the side-chains readily generate vanadium-oxygen bonds.

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Section: Glycylhistidinesupporting

confidence: 86%

Section: Glycylhistidinementioning

confidence: 50%

Section: Glycylhistidinementioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Condensation reactions between vanadate and small functionalized peptides in aqueous solution

Tracey¹,

Jaswal²,

Nxumalo³

et al. 1995

Can. J. Chem.

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“…[7] The interaction with oligopeptides in the physiological pH range, through the coordination of a deprotonated peptide group, was first proved to involve vanadium (v). [8] The amide coordination of a few synthetic ligands to V IV O ion was observed in the solid state too. [9] Costa Pessoa and coworkers suggested the deprotonation and coordination of V IV O by glycine/alanine dipeptides in aqueous solution.…”

Section: Introductionmentioning

confidence: 99%

Binding of Oxovanadium(IV) to Dipeptides Containing Histidine and Cysteine Residues

et al. 2005

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The complexation of the oxovanadium(IV) ion with five dipeptides containing L-histidine or L-cysteine (GlyHis, HisHis, HisGly, CysGly, GlyCys) was studied. L-histidinamide (HisNH 2 ) was assumed as a model system for dipeptides with L-histidine in the N-terminal position. The study was performed in aqueous solution through the combined application of potentiometric and spectroscopic (electronic absorption and EPR) techniques. The results indicate that simple dipeptides lacking a strong anchoring group can form monoand bischelated complexes with the V IV O ion if a suitable "donor" is present in the chain. The ligands behave like amino acids in the acidic and neutral pH range, inhibit the precipitation of hydroxides and suppress the formation of hy-

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A Study of the Electrochemistry of Carnosine Based on the Coupling Reaction with Diazo-p-aminoacetophenone

Duan

Chen

et al. 1999

Electroanalysis

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Carnosine could be determined in the range between 1.0610 À7 and 5.5610 À6 M by differential pulse adsorptive stripping voltammetry (DPASV) on a static mercury electrode after derivatization with diazo-p-aminoacetophenone (DPAAP) at pH 9.6±9.7. The detection limit was 6.8610 À8 M, the relative standard deviation (n 10) for 5.0610 À6 M of carnosine was 1.8 %. The coupling reaction and electrochemical reaction mechanism of azo-carnosine were investigated by structure analysis, UV spectroscopic, cyclic voltammetry, DPASV and electrocapillary at mercury electrodes. A reversible two-electron via two-proton redox and adsorption-controlled process occurred in four consecutive steps with an intermediate at the mercury electrode.

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Complexation of histidine and alanyl-histidine by vanadate in aqueous medium

Cited by 28 publications

References 32 publications

Condensation reactions between vanadate and small functionalized peptides in aqueous solution

Condensation reactions between vanadate and small functionalized peptides in aqueous solution

Binding of Oxovanadium(IV) to Dipeptides Containing Histidine and Cysteine Residues

A Study of the Electrochemistry of Carnosine Based on the Coupling Reaction with Diazo-p-aminoacetophenone

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