All dehydrogenases of glycolysis and the TCA cycle use NAD* (E° for NAD*/NADH is -0.32V) as electron acceptor except succinate dehydrogenase (which uses FAD (E° for FAD/FADH2 is 0.05V). Based on AG° = -NFEº, show and state (1-2 sentences) why is FAD a more appropriate electron acceptor than NAD* in the dehydrogenation of succinate (consider the E° values of
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- All the dehydrogenases of glycolysis and the citric acid cycle use NAD+ (E°' for NAD+/NADH is -0.32 V) as the electron acceptor, except succinate dehydrogenase, which uses covalently bound FAD (E°' for FAD/FADH2 is +0.050 V). Suggest why FAD is a more appropriate electron acceptor than NAD+ in the dehydrogenation of succinate, based on the E°' values of fumarate/succinate (E°' = +0.031 V)The standard reduction potential for ubiquione (A or coenzyme Q) is .045 V, and the standard reduciton potential (E) for FAD is -0.219 V. Using these values, show that the oxidation for FADH2 by ubiquinone theoretically liberates enough energy to drive the synthesis of ATP. Faraday constant =96.48KJ/Vol delta G' standard for ATP Synthesis is +30.5 KJ/mol R=8.314 J/mol K=1.987 cal/mol K(a) Consider the oxidation of malate to oxaloacetate by NAD*: malate + NAD+ → oxaloacetate + NADH + H+ In yeast mitochondria, where the pH = 8.1, this reaction is exergonic only at low oxaloacetate concentrations. Assuming a pH = 8.1, a temperature of 37 °C, and the steady-state concentrations given below, calculate the maximum concentration of oxaloacetate at which the reaction will still be exergonic. malate + NAD*→ oxaloacetate + NADH + H* lactate + NAD →→ pyruvate + NADH + H+ half reaction Pyruvate + 2H+ + 2e → lactate Pyruvate + CO₂ + H + 2e → malate Intracellular steady state concentrations: malate = 410 μM; NAD = 20.0 mM; pyruvate = 3.22 mM; NADH = 290 μM; AG=+29.7 kJ/mol AG¹ = +25.1 kJ/mol E° (V) - 0.190 - 0.330 lactate 1.1 mM CO₂ = 15.5 torr
- All the dehydrogenases of glycolysis and the citric acid cycle use NAD+ (?′°E′° for NAD+/NADH is −0.32 V−0.32 V) as electron acceptor except succinate dehydrogenase, which uses covalently‑bound FAD (?′°E′° for FAD/FADH2 in this enzyme is 0.050 V).0.050 V). The ?′°E′° value for fumarate/succinate is 0.031 V.0.031 V. a)Calculate the Δ?′°ΔG′° value for the oxidation of succinate using NAD+. b)Calculate the Δ?′°ΔG′° value for the oxidation of succinate using covalently‑bound FAD.Consider one of the reactions of the citric acid cycle shown below Malate + NAD+ ⇆ Oxaloacetate + NADH + H+ (malate dehydrogenase) ΔG˚′ = +29.7 kJ/mol. Describe two factors that allow this thermodynamically unfavorable reaction to occur in the direction of malate to oxaloacetate.In the citric acid cycle, malate dehydrogenase catalyzes the following reaction: Malate + NAD+ à oxaloacetate + NADH Calculate the standard free energy change for this reaction (∆Go’). Will it proceed as written under standard conditions? What do you think affects the actual free energy change (∆G) allowing for formation of oxaloacetate from malate?
- The reaction catalyzed by malate dehydrogenase has a ΔG°′ value of +29.7 kJ⋅mol−1. Given what this says about the occurrence of the reaction catalyzed by malate dehydrogenase in cells explain how the reaction catalyzed by citrate synthase (−31.5 kJ⋅mol−1) influences that activity of malate dehydrogenase. In addition, explain how the activity of citrate synthase functions as a regulatory point for the citric acid cycleThe half-reactions involved in the lactate dehydrogenase (LDH) reaction and their standard reduction potentials are (see attached)). Calculate ΔG at pH 7.0 for the LDH-catalyzed reduction of pyruvate under the following conditions: (a) [lactate]/[pyruvate] = 1 and [NAD+]/[NADH] = 1. (b) [lactate]/[pyruvate] = 160 and [NAD+]/[NADH] = 160. (c) [lactate]/[pyruvate] = 1000 and [NAD+]/[NADH] = 1000. (d) Discuss the eff ect of the concentration ratios in Parts a–c on the direction of the reaction.Given the following information, calculate the physiological ΔG of the isocitrate dehydrogenase reaction at 25°C and pH 7.0: [NAD+]/[NADH] = 8, [α-ketoglutarate] = 0.1 mM, and [isocitrate] = 0.02 mM. Assume standard conditions for CO2 (ΔG°′ is given in Table). Is this reaction a likely site for metabolic control?
- Compare the delta ΔG0' values for the oxidation of succinate by NAD+ and by FAD. Use the data given in Table 18.1 to find the E0' of the NAD+-NADH and fumarate-succinate couples, and assume that E0' for the FAD – FADH2 redox couple is nearly 0.05 V. Why is FAD rather than NAD+ the electron acceptor in the reaction catalyzed by succinate dehydrogenase?One process catalyzed by NADHNADH dehydrogenase is NADH+H^++ubiquinone ↽−−⇀ NAD+ubiquinolNADH+H^++ubiquinone ↽−−⇀ NAD^++ubiquinol The standard reduction potentials for the half‑reactions are given in the table. Oxidant Reductant ?′0 ubiquinone+2H++2e−ubiquinone+2H++2e^− ubiquinolubiquinol 0.045 NAD^++H^++2e−NAD^++H^++2e^− NADHNADH –0.32 Calculate Δ?′0 for the reaction as shown. Δ?′0=____(V) Calculate Δ?′0 . Δ?′0=____(kJ/mol)In the hydrolysis of ATP to ADP and Pi, the equilibrium concentration of ATP is too small to be measured accurately. A better way of determining K’eq, and hence ΔG◦’ of this reaction, is to break it up into two steps whose values of ΔG◦’ can be accurately determined. This has been done using the following pair of reactions (the first being catalyzed by glutamine synthetase): (1) ATP + glutamate + NH3 ⇌ ADP + Pi + glutamine + H+ ΔG1◦’= -16.3 kJ/mol (2) glutamate + NH3 ⇌ glutamine + H2O + H+ ΔG2◦’= 14.2 kJ/mol What is the ΔG◦’ of ATP hydrolysis according to these data and is the overall reaction spontaneous? What is the value of the equilibrium constant for the overall reaction at 25.0 °C. If the concentration of ATP at equilibrium is 20.0 mM and the concentration of ADP at equilibrium is 50 nM. What is the concentration the phosphate group (in mM) at equilibrium?