Effect of Strontium Ion on the Hydrolysis of ATP
In cellular energy transformations, the ATP-ADP cycle plays a central role by coupling both with energy-yielding reactions, e.g., oxidative phosphorylation in mitochondria and photosynthetic phosphorylation in chloroplasts, as well as with energy-requiring reactions including active transport, muscular contraction, and biosynthesis.
KeywordsAdenosine Triphosphate Standard Free Energy Acid Dissociation Constant Alkali Earth Metal Standard Free Energy Change
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- 1.L. Levintow and A. Meister, Reversibility of the enzymatic synthesis of glutamine, J. Biol. Chem. 209, 265–280 (1954).Google Scholar
- 2.T. Benzinger, C. Kitzinger, R. Hems, and K. Burton, Free-energy changes of the glutaminase reaction and the hydrolysis of the terminal pyrophosphate bond of adenosine triphosphate, Biochem. J. 71, 400–407 (1959).Google Scholar
- 4.E. A. Robbins and P. D. Boyer, Determination of the equilibrium of the hexokinase reaction and the free energy of hydrolysis of adenosine triphosphate, J. Biol Chem. 224, 121–135 (1957).Google Scholar
- 6.R. A. Alberty, Effect of pH and metal ion concentration on the equilibrium hydrolysis of adenosine triphosphate to adenosine diphosphate, J. Biol. Chem. 243, 1337–1343 (1968).Google Scholar
- 7.R. A. Alberty, Standard Gibbs free energy, enthalpy, and entropy changes as a function of pH and pMg for several reactions involving adenosine phosphates, J. Biol. Chem. 244, 3290–3302 (1969).Google Scholar
- 8.R. C. Phillips, P. George, and R. J. Rutman, Thermodynamic data for the hydrolysis of adenosine triphosphate as a function of pH, Mg2+ion concentration, and ionic strength, J. Biol. Chem. 244, 3330–3342 (1969).Google Scholar
- 11.L. Pauling, The Nature of the Chemical Bond, 3rd ed., p. 518, Cornell University Press, Ithaca, N.Y., 1960. For the atomic weights, see The Merck Index (M. Windholz, ed.), 9th ed., Merck and Co., Rahway, N.J. (1976).Google Scholar