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For the reaction ATP(aq) + H200) <-> ADP(aq) + phosphate (aq), AG° = -30.5 kJ/mol. What...
2. For the following reaction: ATP+ creatine + H2O creatine phosphate + ADP + P, The relevant half reactions are: ATP → ADP + Pi Creatine phosphate + H2O-> creatine AG-30.5 kJ/mol ΔG°,--43.1 kJ/mol a. (2 pts.) Calculate the ΔG°, for the overall reaction. b. (2 pts.) Is the reaction spontaneous or non-spontaneous? Endergonic or exergonic?
er at initial change (AG The standard free energy change (AG) for ATP hydrolysis is -30.5 kJ/ mol ATP, ADP, and I are mixed together at initial concentrations of 1 M each then left alone until the reaction below has come to equilibrium. For each species (ie. ATP. ADP and P.) indicate whether the concentration will be equal to 1 M, less than 1 M, or greater than 1 M after the reaction had reached equilibrium. Explain why. ATP +...
ATP(aq) +H20(l) >>>ADP(aq) + HPO4^2- for which ΔG°rxn = –30.5 kJ/mol at 37.0 °C and pH 7.0. Calculate the value of ΔGrxn in a biological cell in which [ATP] = 5.0 mM, [ADP] = 0.60 mM, and [HPO42–] = 5.0 mM.
10) The AG for the hydrolysis of creatine phosphate is -43.1 k/mol, whereas the AG for ATP synthesis is+30.5 kj/mol, what is the overall ΔG., for the reaction shown below? creatine + ATP creatine phosphate+ADP O-73.6 kj/mol O12.6 k/mol -43.1 k/mol O73.6 k/mol -12.6 kj/mol 043.1 Wmol Answer not listed
Shown is acetyl phosphate. Say a new enzyme uses acetyl phosphate to phosphorylate ADP to make ATP (acetyl phosphate + ADP —> acetate + ATP). What is the standard free energy change of this reaction? CH3 Table 13-2 Standard Free Energies of Phosphate Hydrolysis of Some Compounds of Biological Interest AGo (kJ mol 1) 61.9 -49.4 45.6 43.1 -43.1 30.5 -20.9 19.2 13.8 13.8 -9.2 Compound Phosphoenolpyruvate 1,3-Bisphosphoglycerate ATP AMP + PP,) Acetyl phosphate Phosphocreatine ATP ㈠ ADP + Pi)...
Consider the following reaction: Glucose + ATP ↔Glucose -6-phosphate + ADP Using the information in the below determine Go for this reaction and comment on the spontaneity of this reaction. What the information does the Go parameters in the table below provides about the rate of the ATP hydrolysis. Below is the structure of glucose-6-phosphate. Identify which anomer does it represent? Standard free energies of hydrolysis of some phosphorylated compounds compound Go (kJ mol-1) ATP (to ADP) -30.5 pyrophosphate -19.3...
7.5 Hexokinase catalyzes the reaction: ATP + Glucose A glucose-6-phosphate + ADP AG - -4 562 cal / mol Keg = 2.21 x 103 Calculate the concentration of glucose-6-phosphate necessary to force the hexokinase reaction to go in the opposite direction (towards the synthesis of glucose and ATP) in the presence of 10-5 M glucose, 10-3 M ATP and 10-4 M ADP.
Given the following: phosphocreatine → creatine + Pi ΔG = −43.0 kJ/mol ATP → ADP + Pi ΔG = −30.5 kJ/mol What is the overall ΔG for the following Reaction? phosphocreatine + ADP → creatine + ATP A) -12.5 kJ/mol B) + 73.5 kJ/mol C) -73.5 kJ/mol D) + 12.5 kJ/mol
Consider the hydrolysis of ATP: ATP(aq) + H2O(l) → ADP(aq) + Pi(aq). This reaction has ΔH°= −24.3 kJ/mol and ΔS°= +21.6 J/mol-K. The actual concentrations of ATP, ADP, and Pi are not 1 M in a biological cell. How much energy can the conversion of ATP to ADP supply when it occurs at physiological conditions in E. coli where the temperature is 37°C and the approximate concentrations are ATP = 11.2 mM, ADP = 1.52 mM, Pi = 20.0 mM?...
The concentration of fructose 6-phosphate (F6P) and fructose 1, 6-biphosphate (F16BP), ATP, and ADP in muscle tissue were measured as 0.089, 0.012, 12.0, and 1.2 mM. For the reaction F6P(aq) + ATP(aq) rightarrow F16BP(aq) + ADP(aq) at 37 degree C, the standard Gibbs energy (at pFl=7) is -18.3 kJ/mol. Calculate the reaction Gibbs energy (kJ/mol) for the reaction in the muscle tissue environment. -71.2 -29.4 -7.3 +4.5 +11.2.