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Role of water activity on the rates of acetyl phosphate and ATP hydrolysis

1988; Wiley; Volume: 232; Issue: 1 Linguagem: Inglês

10.1016/0014-5793(88)80389-2

1873-3468

Leopoldo de Meis, V.A. Suzano,

Mitochondrial Function and Pathology

The rates of hydrolysis of acetyl phosphate in the presence of 0.1 M NaOH and of ATP in the presence of either 1 M HCl or 1 M NaOH were measured at different temperatures and in the presence of different concentrations of the organic solvents dimethyl sulfoxide or ethylene glycol. Under all conditions tested, there was a progressive increase in the rate constant of hydrolysis of both phosphate compounds as the water activity of the medium was decreased by the addition of organic solvents. At 25°C, substitution of 70% of the water of the medium by dimethyl sulfoxide promoted an increase of two orders of magnitude in the rate constant of acetyl phosphate hydrolysis. In the presence of 80% and 90% dimethyl sulfoxide the rate of acetyl phosphate hydrolysis increased by more than two orders of magnitude and was so fast that it could not be measured with the method used. The effect of organic solvents on the rate of ATP hydrolysis was less pronounced than that observed for acetyl phosphate hydrolysis. At 30°C, substitution of 90% of water by an organic solvent promoted a 4–6‐fold increase of the rate of ATP hydrolysis. Acceleration of either acetyl phosphate or ATP hydrolysis rates was promoted by a decrease in both activation energies ( E a ) and in entropies of activation Δ S ‡. The data obtained are discussed with reference to the mechanism of catalysis of enzymes involved in energy transduction such as the Ca 2+ ‐ATPase of sarcoplasmic reticulum and the F 1 ‐ATPase of mitochondria.