117. Thermodynamic effects involved in the metal-ion chelation of histidine, histidine methyl ester, and 4(or 5)-imidazolylacetic acid

Andrews, A. C.; Zebolsky, D. M.

doi:10.1039/jr9650000742

Cited by 16 publications

(9 citation statements)

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“…While the amine and imidazole groups demonstrate greater temperature dependent changes in protonation, these are not expected to influence uranyl coordination since they do not participate in inner-sphere interactions with uranyl under these conditions. The general trend of temperature dependent formation constants is consistent with other metal ion-histidine complexes, including those with Cu(II), Zn(II), and Ni(II) [31,32], however the formation of these complexes is expected to be more heavily influenced by the amino and imidazole protonation constants, as these groups directly coordinate these transition metal ions.…”

Section: Temperature Dependent Uranyl-histidine Formationsupporting

confidence: 65%

Solution interactions between the uranyl cation [UO22+] and histidine, N-acetyl-histidine, tyrosine, and N-acetyl-tyrosine

Xie

Badawi

Huang

et al. 2009

Journal of Inorganic Biochemistry

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Section: Temperature Dependent Uranyl-histidine Formationsupporting

confidence: 65%

Solution interactions between the uranyl cation [UO22+] and histidine, N-acetyl-histidine, tyrosine, and N-acetyl-tyrosine

Xie

Badawi

Huang

et al. 2009

Journal of Inorganic Biochemistry

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“…Because of the importance of L-histidine as the major low-molecular-weight Ni(II)-binding constituent in human serum, the complex equilibria between Ni(II) and the amino acid were examined for the purpose of investigating the ternary-complex equilibria. Although previously studied by other workers (Leberman & Rabin, 1959;Andrews & 1982Zebolsky, 1965Perrin & Sharma, 1967;Sovago et al, 1978), no clear mapping of the species as a function of pH at high ligand/metal ratios was available. Two major complexes, MB and MB2, dominate the distribution, with logf3101 and 1ogl102 equal to 8.57 and 15.57 respectively (Fig.…”

Section: Complex Species In Ni(ii)-l-his and Ni(ii)-asp-ala-his-nhme-mentioning

confidence: 98%

Nickel(II) transport in human blood serum. Studies of nickel(II) binding to human albumin and to native-sequence peptide, and ternary-complex formation with l-histidine

Glennon

Sarkar

1982

Biochemical Journal

116

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Detailed studies are reported on the Ni(II)-binding site of human serum albumin (HSA) and the results are compared with those obtained from the N-terminal native-sequence peptide, l-aspartyl-l-alanyl-l-histidine N-methylamide (Asp-Ala-His-NHMe). Equilibrium dialysis of HSA and Ni(II) in 0.1m-N-ethylmorpholine/HCl buffer, pH 7.53, demonstrates a specific Ni(II)-binding site on the protein. l-Histidine, the low-molecular-weight Ni(II)-binding constituent of human serum, is shown to have a greater affinity for Ni(II) than does HSA. A small but significant amount of ternary complex HSA-Ni(II)-l-histidine is also present in the equilibrium mixture containing the three components. The log (association constant) values for the binary and ternary Ni(II) complexes are 9.57 and 16.23 respectively. The complex equilibria between Asp-Ala-His-NHMe and Ni(II) have been investigated by analytical potentiometry in aqueous solution (0.15m-NaCl, 25 degrees C). Several species, including MA, MA(2), MH(-2)A, and MH(-1)A(2) [where M and A represent Ni(II) ion and anionic peptide respectively], were detected in the system, MH(-2)A being the major complex species. Equilibrium studies involving Asp-Ala-His-NHMe, Ni(II) and l-histidine reveal the presence of a ternary complex MH(-1)AB (where B represents anionic l-histidine) at physiological pH. Detailed studies of visible-absorption spectra of HSA in the presence of Cu(II) and Ni(II) reveal that the two metal ions bind HSA at the same site. The visible-absorption spectrum of Ni(II)-HSA complex shows a highly absorbing peak at 420nm (epsilon(max.) = 137; with shoulder at 450-480nm) characteristic of a square planar or square pyramidal co-ordination arrangement about the metal ion. Similar visible-absorption characteristics were observed for the major species MH(-2)A in the Asp-Ala-His-NHMe-Ni(II) system (lambda(max.) = 420nm; epsilon(max.) = 135; with shoulder at 450-480nm). The combination of experimental results from the protein studies and the peptide analyses provides strong evidence for the structure of the Ni(II)-binding site of HSA as one that involves the alpha-amino nitrogen atom, two deprotonated peptide nitrogen atoms, the imidazole nitrogen atom and the side-chain carboxy group of the aspartic acid residue. On the basis of the results obtained from the individual ternary systems involving protein and peptide, a mechanism for the transportation of Ni(II) in the serum is proposed.

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“…There are several sources of the proton dissociation constants for aqueous L-histidine at p = 0.1 MPa in the literature. (17)(18)(19)(20)(21)(22) We use the values of the acid dissociation molality quotients Q a,1 for reaction (1) and Q a,2 for reaction (4) at T = 298.15 K, m = 0.1 mol · kg −1 and m = 0.5 mol · kg −1 , and p = 0.1 MPa from Martell and Smith (17) to obtain the thermodynamic equilibrium constants K a , as pK a,1 = (6.02±0.03) and pK a,2 = (9.06 ± 0.03). We also use pQ a,1 = pK a,1 at T = 298.15 K for m 0.5 mol · kg −1 since reaction (1) is isoelectric, and pQ a,2 = pK a,2 + (1.022 kg 1/2 · mol −1/2 ) · m 1/2 for reaction (4) based on Debye-Hückel behavior at T = 298.15 K, p = 0.1 MPa, and m 0.66 mol · kg −1 .…”

Section: Resultsmentioning

confidence: 98%

“…We use r H m,1 = r H • m,1 at T = 298.15 K for m 0.5 mol · kg −1 since reaction (1) is isoelectric. We have also used all the experimental results from the literature (17,18,20,21) at m 0.5 mol · kg −1 for pK a,2 (or pQ a,2 ) at 273. 15 T /K 313.15 to determine the standard enthalpy change for reaction (13) and (14) for the apparent molar heat capacities C p,φ of aqueous L-histidine {H · His(aq)}, L-histidine + HCl{H 2 · His + Cl − (aq)}, and L-histidine + NaOH {Na + His − (aq)}.…”

Section: Resultsmentioning

confidence: 99%

“…We have used experimental results from the literature (17)(18)(19)(20)(21)(22) at m 0.5 mol · kg −1 for pK a,1 (or pQ a,1 ) at 273. 15 T /K 313.15 to estimate the standard enthalpy change 0.34750 296.3 ± 1.9 296.7 ± 1.9 296.4 ± 1.8 295.9 ± 1.8 294.9 ± 1.8 293.8 ± 2.0 0.66092 317.3 ± 1.9 317.9 ± 1.9 317.9 ± 1.9 317.8 ± 2.0 317.3 ± 2.1 316.6 ± 2.3…”

Section: Resultsmentioning

confidence: 99%

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Thermodynamics for proton dissociations from aqueous l -histidine at temperatures from 278.15 K to 393.15 K and at the pressure 0.35 MPa: apparent molar volumes and apparent molar heat capacities of the protonated cationic, neutral zwitterionic, and deprotonated anionic forms

Jardine

Call

Patterson

et al. 2001

The Journal of Chemical Thermodynamics

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Apparent molar volumes V φ and apparent molar heat capacities C p,φ were determined for individual solutions of aqueous L-histidine, of aqueous L-histidine with equimolal HCl, and of aqueous L-histidine with equimolal NaOH at molalities m = (0.015 to 0.66) mol · kg −1 , at temperatures T = (278.15 to 393.15) K, and at the pressure p = 0.35 MPa. Apparent molar volumes were generated from density measurements obtained with a vibrating-tube densimeter. Apparent molar heat capacities were generated from heat capacity measurements with a twin fixed-cell, power-compensation, differential-output, temperature-scanning calorimeter. These results were then fitted by regression to empirical equations to describe the (V φ ,m,T ) and (C p,φ , m, T ) surfaces for each of the three systems. These regression equations were then used to calculate the changes in partial molar volume r V m and partial molar heat capacity r C p,m as functions of m and T for both the first and second proton dissociation reactions for protonated aqueous L-histidine. The changes in enthalpy r H m and entropy r S m and the acid dissociation molality quotient Q a were then obtained as functions of m and T for each proton dissociation reaction by integration, using our ( r C p,m , m, T ) results and literature values for r H m and Q a . Our results illustrate the unique thermodynamic properties of the cationic, neutral zwitterionic, and anionic forms of L-histidine in aqueous solution.

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117. Thermodynamic effects involved in the metal-ion chelation of histidine, histidine methyl ester, and 4(or 5)-imidazolylacetic acid

Cited by 16 publications

References 0 publications

Solution interactions between the uranyl cation [UO22+] and histidine, N-acetyl-histidine, tyrosine, and N-acetyl-tyrosine

Solution interactions between the uranyl cation [UO22+] and histidine, N-acetyl-histidine, tyrosine, and N-acetyl-tyrosine

Nickel(II) transport in human blood serum. Studies of nickel(II) binding to human albumin and to native-sequence peptide, and ternary-complex formation with l-histidine

Thermodynamics for proton dissociations from aqueous l -histidine at temperatures from 278.15 K to 393.15 K and at the pressure 0.35 MPa: apparent molar volumes and apparent molar heat capacities of the protonated cationic, neutral zwitterionic, and deprotonated anionic forms

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