Calculate AG for ATP hydrolysis in muscle at 16 °C. Use the muscle concentrations from the first question. AG= kJ/mol
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- ATP Synthase is known to catalyze the synthesis of ATP with a ΔG°’ close to zero, and a Keq' close to 1. Why is the value of ΔG°’ different from the known value which is 30.5 kJ/mol (the energy for the reverse of ATP hydrolysis)? If the Keq' value is close to one, how is it ensured that the reaction is driven to the product side and more ATP is obtained?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)1. a. Calculate the physiological DG of the reaction shown below at 37°C, as it occurs in the cytosol ofneurons, with phosphocreatine at 4.7 mM, creatine at 1.0 mM, ADP at 0.73 mM, and ATP at 2.6mM. The standard free energy change for the overall reaction is –12.5 kJ/mol. Phosphocreatine + ADP ® creatine + ATP b. The enzyme phosphoglucomutase catalyzes the conversion of glucose 1-phosphate to glucose6-phosphate. Calculate the standard free energy change of this reaction if incubation of 20 mMglucose 1-phosphate (no glucose-6 phosphate initially present) yields a final equilibrium mixtureof 1.0 mM glucose 1-phosphate and 19 mM glucose 6-phosphate at 25°C and pH 7.0. c. If the rate of a nonenzymatic reaction is 1.2 x 10–2 μM s–1, what is the rate of the reaction at 37℃ inthe presence of an enzyme that reduces the activation energy by 30.5 kJ/mol?
- 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?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.Consider the following equilibrium at 25ºC :Glucose-1-Phosphate Glucose-6-PhophateUsing the equilibrium concentrations of [Glucose-1-Phosphate] = 0.35 M and [Glucose-6-Phosphate] = 1.65 M, calculate BOTH K′eqand Gº′ for this reaction. Is this reaction exergonicor endergonic? R = 8.314 J/K·mol
- Consider the following reaction:ATP → AMP + 2 PiCalculate the equilibrium constant (Keq) given the following ΔG°′ values:ATP → AMP + PPi (−32.2 kJ/mol)PPi → 2Pi (−33.5 kJ/mol)A total of 30.5 kJ mol-1 of free energy is needed to synthesise ATP from ADP and Pi when the reactants and products are at 1.0 M concentrations and the temperature is 25oC. Because the actual physiological concentrations of ATP, ADP, and Pi are not 1.0 M, and the temperature is 37oC, the free energy required to synthesise ATP under physiological conditions is actually ~ 46.2 kJ mol-1. A 68 kg adult requires an energy intake of 8,550 kJ of food per day (24 hours). Calculate the mass (in Kg) of ATP synthesised by a human adult in 24 hours, assuming that the percentage efficiency of converting inputted calories in ATP is 50%. What percentage of the body weight does this represent?Under standard conditions, NADH reoxidation by the electron-transport chain has a free-energy change equal to –220 kJ/mol. With 100% efficiency, how many ATP could be synthesized under standard conditions? What is the "actual" efficiency given these numbers?
- You know that the free energy of ATP hydrolysis depends on the ATP/ADP ratio. Given that under standard conditions DGo = -30.5 kJ/mol, what should be DG of ATP hydrolysis under normal intracellular concentrations? [ATP] = 2.3 mM, [ADP] = 0.25 mM, [Pi] = 1.65 mM What is the energy of ATP hydrolysis in a cell that is ATP-depleted? [ATP] = 0.1 mM, [ADP] = 2.8 mM, [Pi] = 1.65 mMThe hydrolysis of ATP to ADP has a △G°' of -30 kJ/mol. If in an E. coli cell the concentrations of ATP, ADP and inorganic phosphate are 7.90 mM, 1.04 mM and 7.9 mM, respectively, which statement is true about the hydrolysis of ATP in the cell? (Assume a temperature of 298 K. R = 8.315 J/K-mol) A. The formation of ATP from ADP is occurring more rapidly than the hydrolysis. B. The hydrolysis is being allosterically controlled. C. Hydrolysis can proceed spontaneously. D. The hydrolysis is at equilibrium. QUESTION 10 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. 21 help with these questions pleaseIf 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 phosphate