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• W2034353508 abstract "Temperature-jump experiments of the reaction of the thiocyanate ion with human aquomethaemoglobin have been performed in the presence of a 10-fold excess of inositol hexakisphosphate (inositol-P6). Two kinetic phases corresponding to the α and β subunits were observed. Kinetic parameters of the reaction were evaluated from the reciprocal relaxation times on the basis of a fast relaxation of the iron(iii) ion spin states equilibrium before binding of the ligand. The association, kiL, and dissociation, k–iL, rate constants determined were: kαL= 225 dm3 mol–1 s–1, k–αL= 1.52 s–1, kβL= 2430 dm3 mol–1 s–1, k–βL= 6.51 s–1 at 27 °C, pH 6.44. There was good agreement between the equilibrium constant of the ligand binding step determined by static methods (Kequ= 204 ± 11 dm3 mol–1) and that evaluated from kinetic data [(KαLKβL)1/2= 235 ± 12 dm3 mol–1]. The value kβL/kαL= 11 obtained ensured proper separation of the two kinetic phases. Analyses of the subunit relaxation amplitudes, δEiL, showed that inositol-P6 perturbed the absorption spectrum of the β subunits. This suggests that in the presence of the organic phosphate, methaemoglobin behaves as a protein with independent binding sites rather than as an allosteric molecule. The kinetic and relaxation amplitude spectral characteristics of the subunits, in the presence of inositol-P6 have demonstrated that the kinetic dynamics are effectively decoupled in a stable tetramer." @default.
• W2034353508 created "2016-06-24" @default.
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• W2034353508 date "1993-01-01" @default.
• W2034353508 modified "2023-09-26" @default.
• W2034353508 title "Role of the relaxation of the iron(III) ion spin states equilibrium in the kinetics of ligand binding to methaemoglobin" @default.
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• W2034353508 doi "https://doi.org/10.1039/ft9938903921" @default.
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