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- The hydrolysis of ATP has an enthalpy and entropy of -24.3 kJ/mol and +21.6 J.K-1.mol-1, respectively, at 37 o C. What is the free energy change for the hydrolysis of 5 mols of ATP? Explain what contributes to the negative enthalpy change and positive entropy change in this reaction. What physical characteristics of the reaction would change if an ATP hydrolase enzyme is added to the solution?Given the following coupled reactions: phosphoenolpyruvate + H2O → pyruvate + Pi ΔG°'= -61.9 kJ/mol ATP + H2O → ADP + Pi ΔG°'= -30.5 kJ/mol write the overall reaction, calculate the ΔG°’, and determine if the reaction is exergonic or endergonic. The overall reaction is ______ + _______ → _______ + _________ The overall ΔG°’ is ________ kJ/mol. Therefore, the reaction is _______(exergonic/endergonic)For the series of reactions below, what is the overall reaction and the value of ∆Go’(kJ/mol) for this set of reactions? Is the reaction spontaneous? (1) 2 Pi+ H2O ➔Pyrophosphate+ H2O (with 5 mM Mg2+) (2) (Mg)Pyrophosphate + AMP ➔(Mg)ATP (3) (Mg)ATP + creatine ➔creatine-phosphate + (Mg)ADP
- The conversion of glucose-1-phosphate to glucose-6-phosphate by the enzyme phosphoglucomutase has a △G°' of -7.6 kJ/mol. Calculate the equilibrium constant for this reaction at 298 K and a pH of 7. (R = 8.315 J/K-mol) A. 0.003 B. 0.047 C. 1.00 D. 21Given that the standard free-energy change for the reaction glucose + Pi →glucose 6-phosphate is 13.8 kJ/mol, and the standard free-energy change forthe reaction ATP → ADP + Pi is −30.5 kJ/mol, what is the free-energychange for the reaction glucose + ATP → glucose 6-phosphate + ADP?If the hydrolysis of 1 M glucose 6-phosphate catalyzed by glucose 6-phosphatase has a ΔG′∘ of −11.386 kJ/mol at 25 °C, what percentage of substrate remains once the reaction reaches equilibrium assuming no product was initially present? (Round answer to the nearest whole number)
- The decomposition of crystalline N2O5 N2O5(s) → 2NO2(g) + 1/2O2(g) is an example of a reaction that is thermodynamically favored, even though it absorbs heat. At 25 °C we have the following values for the standard state enthalpy and free energy changes of the reaction: ∆H° = +109.6 kJ/mol ∆G° = -30.5 kJ/mol (a) Calculate ∆S ° at 25 °C. (b) Why is the entropy change so favorable for this reaction?If the Go for ATP hydrolysis into ADP + inorganic phosphate is 7.3 kcal/mole, and the Go for glutamine synthesis from glutamic acid and NH3 is +3.4 kcal/mole, calculate the average Go for coupling these two reactions (glutamic acid + NH3 + ATP glutamine + ADP + inorganic phosphateConsider the following reaction: Glucose-1-phosphate → Glucose-6-phosphate ΔG° = −7.1 kJ/mol What is the equilibrium constant for this reaction at 25oC?
- The free energy released by the hydrolysis of ATP under standard conditions is −30.5 kJ/mol. If ATP is hydrolyzed under standard conditions exceptat pH 5.0, is more or less free energy released? Explain.The phosphoryl group transfer potentials for glucose-1-phosphate and glucose-6-phosphate are 20.9 kJ/mol and 13.8 kJ/mol, respectively. (a) What is the equilibrium constant for the reaction shown below at 25 °C? (b) If a mixture was prepared containing 1 m glucose-6-phosphate and 1 x 10-3 M glucose-1-phosphate, what would be the thermodynamically favored direction for the reaction?Consider the coupled reactions: 1,3-BPG → 3-PG + Pi ΔG°'= -16.3 kcalmolkcalmol ATP → ADP + Pi ΔG°'= -7.3 kcalmolkcalmol Which of the following is TRUE about the total ΔG°’ for the coupled reactions? A. +23.6 kcal/mol; nonspontaneous B. -23.6 kcal/mol; spontaneous C. +9.0 kcal/mol; nonspontaneous D. -9.0 kcal/mol; spontaneous