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Article
Simulation of the kinetics of adenosine 5′-triphosphate hydrolysis catalyzed by the Cu2+ ion: The role of conformation and the catalytic effect of the OH− ion
The hydrolysis kinetics of the dimeric complex (CuATP2− · OH2)2 {D} up to ≈40% ATP conversion at 25°C, pH 5.7–7.8, and [Cu · ATP]0 = (2.07 ± 0.03) × 10−3 mol/l is analyzed by numerical simulation. CuADP− + Pi (Pi
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Article
Kinetics and mechanism of adenosine 5′-triphosphate hydrolysis catalyzed by the Cu2+ ion: The role of conformation and the catalytic effect of the OH− ion
The kinetics of 5′-ATP hydrolysis catalyzed by the Cu2+ ion has been investigated by HPLC in the pH range 5.6–7.8 at 25°C. Two series of experiments differing in the initial [Cu · ATP]0 (1: 1) concentration have ...
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Article
Mathematical Modeling of Kinetics of Adenosine 5"-Triphosphate Hydrolysis Catalyzed by the Zn2+ Ion in the pH Range 7.4–8.3
Kinetic data on adenosine triphosphate (ATP) hydrolysis catalyzed by the Zn2+ ion in the pH range 7.4–8.3 are analyzed by the method of numerical simulation. The rates of forward and reverse reactions of isomeric...
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Article
Mathematical modeling of kinetics of adenosine-5’-triphosphate hydrolysis catalyzed by the Zn2+ ion in the pH range 8.5–9.0
The kinetics of adenosine-5’-triphosphate (ATP) hydrolysis catalyzed by Zn2+ at pH 8.5–9.0 is analyzed by numerical simulation. The rates of product formation (adenosine diphosphate (ADP) and adenosine monophosph...
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Article
Catalytic hydrolysis of ATP. pH-Dependence of the selectivity
Kinetic data on ATP4− hydrolysis in a complex with Zn2+ confirm the enzyme-like mechanism of the reaction. Dependence of the selectivity on pH is observed, which is explained by parallel reactions of cyclic and o...