2. For an exergonic reaction, what is the value of AG?
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- Calculate the standard free energy change (ΔG°′) for the following reaction: ½ O2 + FADH2 → H2O + FADThe following questions are based on the reaction A+ B ↔ C+D shown in Figure 8.1. 1. Which of the following terms best describes the progress of the reaction with respect to free energy change? a) endergonic, ∆G> 0 b) exergonic, ∆G> 0 c) exergonic, ∆G< 0 d) endergonic, ∆G< 0 2. Which of the following in Figure 8.1 remains unchanged by having an enzyme included? a) b b) d c) a d) c 3. The part labeled “C” on the above graph represents a) Energy of activation without enzyme b) Energy of activation with enzyme c) Amount of free energy released d) amount of energy required for the reaction progressThe following data were collected in the study of a new enzyme and an inhibitor of the new enzyme: Vo (nmol/sec) [S] (uM) 1.3 - Inhibitor + Inhibitor 2.50 0.62 2.6 4.00 1.42 6.5 6.30 2.65 13.0 7.60 3.12 26.0 9.00 3.58 What is the Km of the inhibited enzyme reaction?
- For a particular reaction, AH° = −16.1 kJ/mol and AS° = −21.8 J/(mol·K). Assuming these values change very little with temperature, at what temperature does the reaction change from nonspontaneous to spontaneous in the forward direction? OT= Is the reaction in the forward direction spontaneous at temperatures greater than or less than the calculated temperature? less than greater than KThe following data were collected in the study of a new enzyme and an inhibitor of the new enzyme: Vo (nmol/sec) - Inhibitor + Inhibitor 0.62 [S](HM) 1.3 2.50 2.6 4.00 1.42 6.5 6.30 2.65 13.0 7.60 3.12 26.0 9.00 3.58 What is the Vmax of the uninhibited enzyme reaction?How many net molecules of nucleoside triphosphate (ATP and equivalent molecules) are produced by complete aerobic catabolism of a glucose going through glycolysis, the pyruvate dehydrogenase complex and the citric acid cycle (TCA cycle)? Do not count the ATP eventually generated by re-oxidation of reduced coenzymes, just the number of NTPs produced in reactions of these pathways. Choose the one best answer. 02 03 04 05 06 8
- The primary source of phosphate for chemical reactions in cells comes as ATP, ADP, or AMP. The ΔG˚’ for the hydrolysis of ATP into ADP and Pi is -30.5 kJ/mol. Calculate the equilibrium constant for the hydrolysis of ATP.The following data were collected in the study of a new enzyme and an inhibitor of the new enzyme: Vo (nmol/sec) [S] (uM) Inhibitor + Inhibitor 1.3 2.50 0.62 2.6 4.00 1.42 6.5 6.30 2.65 13.0 7.60 3.12 26.0 9.00 3.58 What class of reversible enzyme inhibitor is being employed in this enzyme reaction?Consider a general reaction enzyme A(aq) B(aq) The AGo of the reaction is -9.150 kJ mol-. Calculate the equilibrium constant for the reaction at 25 °C. Keg = What is AG for the reaction at body temperature (37.0 °C) if the concentration of A is 1.9 M and the concentration of B is 0.50 M? 9:26 PM 35% 77°F 6/14/2021
- The following were obtained in a study of an enzyme known to follow Michaelis-Menten kinetics: Reaction Velocity (mmol/min) Substrate added (mmol/L) 217 0.8 325 2 433 4 488 6 647 20 652 1000 The Km for this enzyme is approximately _____________. (Round to the nearest integer)From data in the table, calculate the AG'º value for the reactions. Reaction AG° (kJ/mol) Phosphocreatine + H,O → creatine + P; |-43.0 |ADP + P; → ATP + H,O |+30.5 Fructose + P; → fructose 6-phosphate + H,0 +15.9 Phosphocreatine + ADP → creatine + ATP AG'º = kJ/mol ATP + fructose → ADP + fructose 6-phosphate AG'º = kJ/molTable 2: Effect of pH on Enzyme Activity pH Absorbance 2 0.05 4 0.35 6 0.8 8 0.5 10 0.4 12 0.1 Use the above data table to complete the following questions: a) Plot the data “pH Vs Abs” using “connect the data point type of graph”. Label the graph with dependent and independent variables where they should be. Provide a title for the graph. b) Over what pH range does catechol oxidase catalyze catechol to benoquinone? c) Explain why the graph has a bell-shaped curve.