ou 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 mM

ou 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 mM

Human Physiology: From Cells to Systems (MindTap Course List)

9th Edition

ISBN:9781285866932

Author:Lauralee Sherwood

Publisher:Lauralee Sherwood

Chapter2: Cell Physiology

Section: Chapter Questions

Problem 2SQE

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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?
How many ATP molecules could maximally be generated from one molecule of glucose, if the complete oxidation of 1 mole of glucose to CO2 and H2O yields 686 kcal of free energy and the useful chemical energy available in the high- energy phosphate bond of 1 mole of ATP is 12 kcal?
Given 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?
The 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 please
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?
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?
What is the free energy change for generating the electrical imbalance of protons in respiring mitochondria in culture, where Δψ is 150 mV? (Express your answer in kJ/mol using 3 significant figures.)
Consider the following chemical reaction: Glucose + ATP → Glucose-6-Phosphate + ADP + Pi Given the following information, calculate the actual free energy change (G’) of this reaction. G’ of Glucose + ATP → Glucose-6-Phosphate + ADP + Pi = -16.7 kJ/mol [Glucose] = 5.0 mM [ATP] = 1.85 mM [Glucose-6-Phosphate] = 0.083 mM [ADP] = 0.14 mM [Pi] = 1.0 mM Temperature = 37 C R (Gas Constant) = 8.314 J/mol•K
If the DGo for ATP hydrolysis into ADP + inorganic phosphate is -7.3 kcal/mole, and the DGo for sucrose synthesis from glucose + fructose is +5.5 kcal/mole, calculate standard free energy change for the combined reaction of ATP + glucose + fructose g ADP + sucrose + inorganic phosphate. DGo = -12.8 kcal/mole DGo = -1.8 kcal/mole DGo = 0 kcal/mole DGo = +1.8 kcal/mole DGo = +12.8 kcal/mole
A camel hump contains 12 kg of triacylgylcerols. (a) Given that there are 0.491 moles of ATP per gram of fat, how many moles of ATP could be produced by the fat in the camel hump?(b) If the hydrolysis of ATP releases 7.3 kcal/mole, how many kilocalories are produced by the utilization of the fat?
Suppose you're given the following information: ATP + H2O → ADP + Pi ΔG'° = -30.5 kJ/mol Phosphoenolpyruvate + H2O → Pyruvate + Pi ΔG'° = -61.9 kJ/mol What would the ΔG'° be for the reaction phosphoenolpyruvate + ADP → pyruvate + ATP? Please answer in units of kJ/mol, but do not include the units in your answer.
Calculate the actual, physiological ΔG for the reaction at 37 °C, as it occurs in the cytosol of neurons, with phosphocreatine at 4.7 mM, creatine at 1.0 mM, ADP at 0.73 mM, and ATP at 2.6 mM.