Dissociation constants of toluic acids in aqueous solution at different temperatures and study of related thermodynamic parameters

1978 ◽  
Vol 23 (2) ◽  
pp. 103-107 ◽  
Author(s):  
M. Sengupta ◽  
K. Pal ◽  
A. Chakravarti ◽  
P. Mahapatra
1999 ◽  
Vol 77 (7) ◽  
pp. 1305-1309 ◽  
Author(s):  
Ashraf A El-Bindary ◽  
Adel Z El-Sonbati ◽  
Hanan M Kera

Proton-ligand dissociation constants of 4-(4-acetophenyl)hydrazono-3-methyl-2-pyrazolin-5-one (AHMP) and metal-ligand stability constants of its complexes with some transition metal ions were calculated potentiometrically in 0.1 M KCl and 50% (v/v) ethanol-water mixture. The order of stability constants was found to be Th4+ > UO22+ > Ce3+ > La3+ > Mn2+ < Co2+ < Ni2+ < Cu2+ > Zn2+. The dissociation constant, pK1H, of AHMP and the stability constants, log K, of their complexes were determined at different temperatures (298, 308, and 318 K). The corresponding thermodynamic parameters (ΔG, ΔH, and ΔS) were derived and discussed. The dissociation process is nonspontaneous, endothermic, and entropically unfavourable. The formation of the metal complexes has been found to be spontaneous, exothermic, or endothermic (depending the metal), and entropically favourable. The stoichiometries of these complexes were determined conductometrically and indicated the formation of 1:1 and 1:2 (metal:ligand) complexes. Key words: 4-(4-acetophenyl)hydrazono-3-methyl-2-pyrazolin-5-one, dissociation and stability constants, thermodynamic parameters, stoichiometries.


2020 ◽  
Vol 11 (1) ◽  
Author(s):  
Khémesse Kital ◽  
Moumouny Traoré ◽  
Diégane Sarr ◽  
Moussa Mbaye ◽  
Mame Diabou Gaye Seye ◽  
...  

Abstract The aim of this work is to determine the thermodynamic parameters and the kinetics of complex formation between orthophthalaldehyde (OPA) and agmatine (AGM) in an alkaline medium (pH 13). Firstly, the association constant (Ka) between orthophthalaldehyde and agmatine was determined at different temperatures (between 298 K and 338 K) with a step size of 10 K. Secondly, the thermodynamic parameters such as standard enthalpy (ΔH°), standard entropy (ΔS°),and Gibbs energy (∆G) were calculated, where a positive value of ΔH° (+45.50 kJ/mol) was found, which shows that the reaction is endothermic. In addition, the low value of ΔS°(+0.24 kJ/mol) indicates a slight increase in the disorder in the reaction medium. Furthermore, the negative values of ΔG between −35.62 kJ/mol and −26.02 kJ/mol show that the complex formation process is spontaneous. Finally, the parameters of the kinetics of the reaction between OPA and AGM were determined as follows: when the initial concentration of AGM (5 × 10−6 M) is equal to that of the OPA, the results show that the reaction follows an overall 1.5 order kinetics with an initial rate of 5.1 × 10−7Mmin−1 and a half-life of 8.12 min. The partial order found in relation to the AGM is 0.8. This work shows that the excess of OPA accelerates the formation reaction of the complex.


2014 ◽  
Vol 12 (0) ◽  
pp. 404-409 ◽  
Author(s):  
Fumihiko Ogata ◽  
Daisuke Imai ◽  
Megumu Toda ◽  
Masashi Otani ◽  
Naohito Kawasaki

1996 ◽  
Vol 319 (3) ◽  
pp. 675-681 ◽  
Author(s):  
Jean-Paul RENAUD ◽  
Dmitri R. DAVYDOV ◽  
Karel P. M. HEIRWEGH ◽  
Daniel MANSUY ◽  
Gaston HUI BON HOA

An approach to the quantitative spectral analysis of substrate binding and inactivation of cytochrome P-450 in microsomes is described. The method is based on the application of the principal component analysis technique on the Soret-region spectra measured at different temperatures at various concentrations of substrate. This approach allowed us to study the thermodynamic parameters of substrate binding and spin transitions in human cytochrome P-450 3A4 expressed in yeast (Saccharomyces cerevisiae) microsomes. These parameters are discussed in comparison with the values reported earlier by Ristau et al. [(1979) Acta Biol. Med. Ger. 38, 177–185] for rabbit liver cytochrome P-450 2B4 in solution with benzphetamine as a substrate. Our analysis shows the substrate-free states of 2B4 and 3A4 to be very similar. However, substrate binding seems to perturb haem-protein interactions in 3A4 in contrast with 2B4, where the effect of substrate binding on the thermodynamic parameters of spin transitions was insignificant. The implication of the results for the mechanism of substrate-induced spin shift is discussed.


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