3. Experimental Determination of AG for ATP Hydrolysis A direct measurement of the standard free- energy change associated with the hydrolysis of ATP is technically demanding because the minute amount of ATP remaining at equilibrium is difficult to measure accurately. The value of AGo can be calculated indirectly, however, from the equilibrium constants of two other enzymatic reactions having less favorable equilibrium constants: Glucose6-phosphate + HO - glucose + Pi Keg= 270 ATP + glucose > ADP + glucose6-phosphate Key 890 Using this information for equilibrium constants determined at 25 °C, calculate the standard free energy of hydrolysis of ATP.

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3. Experimental Determination of AG for ATP Hydrolysis A direct measurement of the standard free-
energy change associated with the hydrolysis of ATP is technically demanding because the minute amount
of ATP remaining at equilibrium is difficult to measure accurately. The value of AGo can be calculated
indirectly, however, from the equilibrium constants of two other enzymatic reactions having less favorable
equilibrium constants:
Glucose6-phosphate + H.O
- glucose + Pi
Keg 270
ATP+glueose
> ADP + glucosE6-phosphate K eg 890
Using this information for equilibrium constants determined at 25 °C, calculate the standard free energy of
hydrolysis of ATP.
Transcribed Image Text:3. Experimental Determination of AG for ATP Hydrolysis A direct measurement of the standard free- energy change associated with the hydrolysis of ATP is technically demanding because the minute amount of ATP remaining at equilibrium is difficult to measure accurately. The value of AGo can be calculated indirectly, however, from the equilibrium constants of two other enzymatic reactions having less favorable equilibrium constants: Glucose6-phosphate + H.O - glucose + Pi Keg 270 ATP+glueose > ADP + glucosE6-phosphate K eg 890 Using this information for equilibrium constants determined at 25 °C, calculate the standard free energy of hydrolysis of ATP.
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