name: 2. A direct measurement of the standard free-energy change associated with the hydrolysis of ArTo. technically demanding because the minute amount of ATP remaining at equilibrium is difficult to measure accurately. The value of AG°can be calculated indirectly, however, from the equilibrium constants of two other enzymatic reactions having less favorable equilibrium constants: Glucose 6-phosphate + H20 → glucose + Pi Keg = 270 %3D ATP + glucose ADP + glucose 6-phosphate Keg = 890 Using this information for equilibrium constants determined at 25 °C, calculate the standard free energy of hydrolysis of ATP. VDb (6) praby

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2. A direct measurement of the standard free-energy change associated with the hydrolysis of ArTo.
technically demanding because the minute amount of ATP remaining at equilibrium is difficult to
measure accurately. The value of AG°can be calculated indirectly, however, from the equilibrium
constants of two other enzymatic reactions having less favorable equilibrium constants:
Glucose 6-phosphate + H20
→ glucose + Pi
Keg = 270
%3D
ATP + glucose
ADP + glucose 6-phosphate
Keg = 890
Using this information for equilibrium constants determined at 25 °C, calculate the standard free
energy
of hydrolysis of ATP.
VDb
(6)
praby
Transcribed Image Text:name: 2. A direct measurement of the standard free-energy change associated with the hydrolysis of ArTo. technically demanding because the minute amount of ATP remaining at equilibrium is difficult to measure accurately. The value of AG°can be calculated indirectly, however, from the equilibrium constants of two other enzymatic reactions having less favorable equilibrium constants: Glucose 6-phosphate + H20 → glucose + Pi Keg = 270 %3D ATP + glucose ADP + glucose 6-phosphate Keg = 890 Using this information for equilibrium constants determined at 25 °C, calculate the standard free energy of hydrolysis of ATP. VDb (6) praby
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