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- The inhibitor X prevents coenzyme Q (Q) from participating in electron transfer in the electrontransport chain.(a) Will the presence of X prevent electrons from N ADH from passing through the electron trans-port chain? Explain why or why not.(b) Compound Y is a non-physiological reducing agent capable of directly reducing cytochromec1 in Complex III. Would oxygen consumption resume upon the addition of compound Y tomitochondria inhibited by inhibitor X? Be sure to explain your answer.The values of the reduction potential (Eº') of the conjugated redox pairs NAD+/NADH and pyruvate / lactate are -0'32 V and -0'19 V respectively. a) Which of the two conjugated pairs has a greater tendency to lose electrons? Reason for it. b) What is the strongest oxidizing agent? Reason for it. c) If we start with 1M concentrations of each reagent and product at pH 7.0 in which sense the reaction will pass pyruvate + NADH + H+ ⇄ lactate + NAD+ d) What is the standard free energy variation (ΔGº’ at 25ºC) for the conversion of pyruvate to lactate? e) What is the equilibrium constant of this reaction?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?
- Write a balanced equation for each of the following reactions or reaction sequences. (a) The reaction catalyzed by PFK-2 (b) The conversion of 2 moles of oxaloacetate to glucose (c) The conversion of glucose to UDP-Glc (d) The conversion of 2 moles of glycerol toglucose (e) The conversion of 2 moles of malate to glucose-6-phosphateBelow are the reduction reactions for oxygen and FAD. ½202 + 2e + 2H+ → H20 E°' = 0.83 V FAD + 2e + 2H* → FADH2 E" = -0.22 V What is the potential (E") for the oxidation of FADH by oxygen? What is the AG®' for the oxidation of FADH, by oxygen? If we assume that the pumping of protons in conjunction with the oxidation of FADH, requires 120 kJ, what percentage of the energy from FADH oxidation is stored in the proton gradient (think about how many protons are pumped when FADH, transfers electrons to oxygen)?The 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.
- The standard free energy change for the reaction catalyzed by phosphoglucomutase is -7.1kJ/mol, (a) calculate ΔG at 37°C when the concentration of glucose-1-phosphate is 1-mM and the concentration of glucose-6-phosphate is 25-mM, (b) Is the reaction spontaneous under these conditions?what each term means and why it applies to either anabolism or catabolism. a) endergonic b) exergonic c) favorable (delta G<0) d) unfavorable (delta G>0) e) K>1 (relate this to the equation K=[B]/[A], generally discussing the concentrations of products and reactants. e.g. In this situation, which has a higher concentration?) f) K<1 (relate this to the equation K=[B]/[A], generally discussing the concentrations of products and reactants. e.g. In this situation, which has a higher concentration?) g) hydrolysis h) condensationConsidering that 22.4 kJ/mole is required to transport 1 H+ across the mitochondrial membrane,how much energy is available for proton translocation from the oxidation of FADH2 at Complex II? Answer: 134 kJ/mol Can you please explain why the answer would be 134 kJ/mol?
- Under standard conditions, is the oxidation of ubiquinol (Coenzyme Q) by O2 sufficiently exergonic to drive the synthesis of ATP? If yes, how many ATP can be synthesized assuming 100% efficiency?To carefully prepared mitochondria were added succinate, oxidizedcytochrome c, ADP, orthophosphate, and sodium cyanide. Referring toFigure 14.16, answer the following.(a) List the sequence of electron carriers in this system.(b) Write a balanced equation for the overall reaction occurring in thissystem, showing oxidation of the initial electron donor, reduction of thefinal acceptor, and synthesis of ATP.(c) Calculate ΔG°' for the overall reaction. ΔG°' for ATP hydrolysis is-32.2 kJ/mol.(d) Why was cyanide added in this experiment?(e) What would the P/O ratio be if the same experiment were run with addition to the mitochondria of 2,4-dinitrophenol?Calculate the ΔG for Malate dehydrogenase reaction of CAC if the concentration of oxaloacetate is 1x 10-8 M, malate is 0.2 mM, NAD+ is 10 mM and NADH is 0.1 mM in rat liver mitochondria. ΔGo’ for this reaction is 30 kJ/mole. Please write the units of the final answer and the formula you are using to solve. R = 0.008314kJ/K*mol, T = 298K