The free energy-requiring step in the synthesis of ATP is not the formation of ATP from ADP and Pi (ΔG ≈ 0), but the release of tightly bound ATP. Explain why this is not inconsistent with the +30.5 kJ⋅mol-1 free energy of formation of ATP in solution.
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- The energy released by the hydrolysis of ATP is primarily stored between the alpha and beta phosphates equal to -57 kcal/mol harnessed as heat energy by the cell to perform work providing energy to coupled reactionsMATHEMATICAL The free-energy change (G) for the oxidation of the cytochrome aa3 complex by molecular oxygen is 2102.3kJ=224.5kcal for each mole of electron pairs transferred. What is the maximum number of moles of ATP that could be produced in the process? How many moles of ATP are actually produced? What is the efficiency of the process, expressed as a percentage?10) The phosphorylation of glucose is an unfavorable reaction, with ΔG°’ = 13.8 kJ/mol. We can couple this to the favorable reaction of ATP hydrolysis to make the overall process favorable. a) Describe how this works. b) If ΔG°’ for ATP hydrolysis = -32.2 kJ/mol, what is the overall ΔG°’ of the reaction?
- 2c which is altered by a catalyst such as an enzyme, the net free energy change of the reaction or the activation energy of the reaction?12. Explain why those biological reactions that have their equilibria shifted towards theproducts have negative values for ΔGo of reactions. Explain how equilibria relates toGibbs free energy.A certain first order reaction has the rate law Rate = k[A] with k=0.0068 sec-1. If the initial concentration of A is 0.75 M, what will be the concentration of A after 1 minute? What is the half-life for this reaction? How much time will it take for 75% of A to react? How much A will be left after the passage of three half-lives? What is the initial rate of the reaction?
- Neutral sphingomyelinase 2 converts sphingomyelin into ceramide and phosphorcholine. What kind of enzyme is it? Assume Vmax is 35 µM min-1. When you provide 3.0 x 10-5 M of sphingomyelin, you observe an initial velocity of 6.0 µM min-1. Calculate the KM.Calculate theequilibrium constant and thefree energy of (Mg)ATP hydrolysis in a closed system in which concentrations of ATP, ADP and Piare, respectively, 3.5, 1.0, and 5 mMand 25 degrees Celsius. Is the reaction spontaneous?R = 8.314 J/(deg Kelvin-mol).The ΔG°′ for hydrolytically removing a phosphoryl group from ATP is about twice as large as the ΔG°′ for hydrolytically removing a phosphoryl group from AMP (−14 kJ · mol−1). Explain the discrepancy.
- 5. For a Michaelis-Menten enzyme, k1 = 5.2 ⅹ 108 M-1 s-1, k-1 = 3.1 ⅹ 104 s-1, and k2 = 3.4 ⅹ 105 s-1. a) Write out the reaction, showing k1, k-1, and k2. Calculate Ks and Km. Does substrate binding approach equilibrium or the steady state? Justify your answer. b) What is kcat for this reaction? Justify your answer. c) Calculate Vmax for the enzyme. The total enzyme concentration is 25 pmol L-1, and each enzyme has two active sites. d) What substrate concentration would be required for the reaction in (c) to reach half of Vmax. Justify your answer mathematically. e) A second Michaelis-Menten enzyme has k1 = 4.2 ⅹ 107 M-1 s-1, k-1 = 6.1 ⅹ 104 s-1, and k2 = 5.3 ⅹ 102 s-1. Which enzyme is most efficient? 6. A pharmaceutical company is trying to develop aInitial rate data for an enzyme that obeys Michaelis–Menten kinetics areshown in the following table. When the enzyme concentration is 3 nmolml-1, a Lineweaver–Burk plot of this data gives a line with a y-intercept of0.00426 (μmol-1 ml s). (a) Calculate kcat for the reaction.(b) Calculate KM for the enzyme.(c) When the reactions in part (b) are repeated in the presence of 12 μM ofan uncompetitive inhibitor, the y-intercept of the Lineweaver–Burk plotis 0.352 (μmol-1 ml s). Calculate K′I for this inhibitor.2.For question number 1 if a mixture was prepared containing 1 M Glucose 6-Phosphate and 0.001 M Glucose 1-Phosphate the ∆G for this reaction is: included question 1 however, need help with 2 and provided the option for the answer 1.What is the Keq for the conversion of Glucose 1-Phosphate to Glucose 6-Phosphate if the phosphate transfer potential for Glucose 1-Phosphate and Glucose 6-Phosphate are 20.9 kJ/mol and 13.8 kJ/mol respectively?
