How much free energy will be released during ATP hydrolysis of ATP in this condition? Please write the formula you will be using to calculate.
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- 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 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 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 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 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•KIf palmitic acid is subjected to complete combustion in a bomb calorimeter, one can calculate a standard free energy of combustion of 9788 kJ/mol. From the ATP yield of palmitate oxidation, what is the metabolic efficiency of the biological oxidation, in terms of kilojoules saved as ATP per kilojoule released? (Ignore the cost of fatty acid activation.)
- Consider the following chemical equation whose delta(G) = 9kcal/mol: AC + BD ---> AB + CD what are the reactants and what are the products is this reaction spontaneous? How do you know? Is energy released or consumed by this reaction? If an enzyme, which catalyzes this reaction is added, what will happen to delta (G) If this reaction is coupled to another reaction, whose delta(G) is -12 kcal/mol, what will be the net delta(G) value? will the overall reaction be spontaneousA 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?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?
- Gastric juice (pH 1.5) is produced by pumping HCl from blood plasma (pH 7.4) into the stomach. Calculate the amount of free energy required to concentrate the H+ in 1 L of gastric juice at 37 °C. Under cellular conditions,how many moles of ATP must be hydrolyzed to provide this amount of free energy? The free-energy change for ATP hydrolysis under cellular conditions is about −58 kJ/mol . Ignore the effects of the transmembrane electrical potential.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?Use the Michaelis-Menten equation to complete the enzyme kinetic data set, when Km is known to have a value of 1 mmol L-1