The phosphorylation of a certain metabolite is coupled with ATP hydrolysis reaction to proceed: Reaction 1 M-OH + P₁ -> M-OP₁ + H₂O AG'₁= 22.7 kJ/mol Reaction 2 ATP + H₂O -> ADP + P₁ AG%2= -30.5 kJ/mol Net Reaction M-OH + ATP -> M-OP₁ + ADP AG°= ?
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Find the net ΔG° of the reaction.
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- 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)a newly identified bacterium called Nomore biochem is unable to synthesize ubiquinone. A mobile electron carrier called CXC3 is used as a substitute. From the information provided in the table, calculate delta G' and Keq value at 298K for the redox reaction that occurs in the Nomore Biochem electron transport chain. (constants: R=8.3 J/degree x mol, F= 96.1 kJ/v x mol Half Reactions E' (V) ubiquinone + 2e- + 2H+--> Ubiquinol + H2 0.045 NAD+ + 2e- + 2H+ --> NADH + H+ -0.320 CXC3 + 2e- + 2H+ --> CXC3H2 -0.450 explain the impact that using CXC3 instead of ubiquinone will have on ATP production in the cell. How might the cell adapt to this situation?Shown below are reduction potentials for four half-reactions. Which of the coupled reactions is favorable? (Note that for Cytochrome c you must multiply the reduction potential by 2 for each coupled reaction because only one electron is involved) a) 2 Cytochrome c (Fe3+) + H2O ó 2 Cytochrome c (Fe2+) + O2 b) NADH + Succinate- ó NAD+ + Fumarate- c) Fumarate- + H2O ó Succinate- + O2 d) All of the above
- A particular reaction has a ΔG‡ of 37.0 kJ mol-1. In the presence of an enzyme, the same reaction has a ΔG‡ of 5.70 kJ mol-1. Calculate the value of ΔΔG‡ in kJ mol-1.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. 21The turnover number of the enzyme fumarase that catalyzes the reaction, Fumarate + H20 ===→ L-malate, is 2.5 x 103 S - l and Km = 4.0 X 10- 6 mol/L. Calculate the rate of conversion of fumarate to L-malate if the fumarase concentration is 1.0 x 1 0 - 6 mol/L and the fumarate concentration is 2.04 x 10- 4 mol/L.
- 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?One of the examples that we have used to illustrate the concept of equilibrium is the isomerization of glucose-6-phosphate (G6P) to fructose-6-phosphate (F6P), which is the second step in g ycolysis. Draw a graph to show how the reaction Gibbs energy varies with the fraction fof F6P in solution.Label the regions of the graph that correspond to the formation of F6P and G6P being spontaneous, respectively.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
- What is the ∆G naught' for a phosphoryl transfer from ATP to glycerol? The hydrolysis of α-glycerophosphate to glycerol and inorganic phosphate has a ∆G naught' of -8.37 kj/mol. ATP + H2O <--> ADP + Pi ∆G naught' = -30.5 kj/mol What is the efficiency of this reaction (i.e. what % of the available energy remains in the system after the reaction)? Express your answer as a % of the total amount of energy available in the system. Where does the rest of the energy go?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 pleaseConsider 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 spontaneous
