A direct measurement of the standard free-energy change associated with the hydrolysis of ATP is technically very demanding because the minute amount of ATP remaining at equilibrium is difficult to measure accurately. However, the value of AG'o for ATP hydrolysis can be calculated indirectly, from the equilibrium constants of two other enzymatic reactions having less favourable equilibrium constants: Glucose-6-phosphate + H20 = glucose + Pi K'eq = 271 (1) %3D ATP + glucose = ADP + glucose-6-phosphate K'eg = 889 (2) %3D Use this information to determine the value for AG'o for the hydrolysis of ATP at 25°C. Justify the method used.

A direct measurement of the standard free-energy change associated with the hydrolysis of ATP is technically very demanding because the minute amount of ATP remaining at equilibrium is difficult to measure accurately. However, the value of AG'o for ATP hydrolysis can be calculated indirectly, from the equilibrium constants of two other enzymatic reactions having less favourable equilibrium constants: Glucose-6-phosphate + H20 = glucose + Pi K'eq = 271 (1) %3D ATP + glucose = ADP + glucose-6-phosphate K'eg = 889 (2) %3D Use this information to determine the value for AG'o for the hydrolysis of ATP at 25°C. Justify the method used.

Chemistry

10th Edition

ISBN:9781305957404

Author:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Publisher:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Chapter1: Chemical Foundations

Section: Chapter Questions

Problem 1RQ: Define and explain the differences between the following terms. a. law and theory b. theory and...

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