Begining with 1 M concentrations of each reactant and product at pH=7 and 25.0 degrees C, calculate the K'eq of the reaction Pyruvate + NADH Lactate + NADH+H+. Note the temperature of this reaction will not affect the standard reducton potential
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- Energetics of the Hexokinase Reaction The standard-state free energy change. Gfor the hexokinase reaction, is — 1 6.7 kJ/mol. Use the values in Table I to calculate the value of Gfor this reaction in the erythrocyte at 37°C.Begining with 1 M concentrations of each reactant and product at pH=7 and 25.0 degrees C, calculate the K'eq (to one decimal point) of the reaction Pyruvate + NADH+H+ <=> Lactate + NAD+.Note the temperature of this reaction will not affect the standard reducton potential delta E'o in the table 13-7b. please provide a comprehensive explanation with each step taken.Begining with 1 M concentrations of each reactant and product at pH=7 and 25.0 degrees C, calculate the K'eq of the reaction Pyruvate + NADH <=> Lactate + NADH+H+.Note the temperature of this reaction will not affect the standard reducton potential delta E'o in the table 13-7b.
- Calculate the standard free-energy change of the reaction catalyzed by theenzyme phosphoglucomutase, given that, starting with 20 mM glucose 1-phosphate and no glucose 6- phosphate, the final equilibrium mixture at 25 °C and pH 7.0 contains 1.0 mM glucose 1-phosphate and 19 mM glucose 6-phosphate. Does the reaction in the direction of glucose 6-phosphate formation proceed with a loss or a gain of free energy?If a reaction has a ΔG°′ value of at least −30.5 kJ · mol−1, suffi -cient to drive the synthesis of ATP (ΔG°′ = 30.5 kJ · mol−1), can it still drive the synthesis of ATP in vivo when its ΔG is only −10 kJ · mol−1? Explain.If a 0.1 M solution of glucose 1- phosphate at 25 °C is incubated with a catalytic amount of phosphoglucomutase, the glucose 1-phosphate is transformed to glucose 6-phosphate. At equilibrium, the concentrations of the reaction components are Calculate Keq and ΔG′° for this reaction.
- 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 KFor lactate dehydrogenase reaction if km for NADH is 2×10^-4 M . What concentration of it would be appropriate for determining Km for pyruvate?Calculate the biochemical standard cell potential for the oxidation of NADH by molecular oxygen O2 + 2NADH + 2 H+ → 2H2O + 2NAD+
- 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.For part (b) of this problem, use the following standard reduction potentials, free energies, and nonequilibrium concentrations of reactants and products: Consider the last two steps in the alcoholic fermentation of glucose by brewer’s yeast: pyruvate + NADH + 2H+ → ethanol + NAD+ + CO2 (a) Do you predict that ∆S° for this reaction is > 0 or < 0? (b) Calculate the nonequilibrium concentration of ethanol in yeast cells, if ∆G = -38.3 kJ/mol for this reaction at pH = 7.4 and 37 °C when the reactants and products are at the concentrations given above. (c) How would a drop in pH affect ∆G for the reaction described in part (b)? (d) How would an increase in intracellular CO2 levels affect ∆G for the reaction in part (b)? (e) How would an increase in intracellular CO2 levels affect ∆G°′ for the reaction in part (b)?Recall that beta-hydroxybutyrate is oxidized by the enzyme beta-hydroxybutyrate dehydrogenase withsimultaneous reduction of NAD+ to NADH. How might this affect the reduction potential at Complex I in theelectron transport chain? (Note: you will need to use the form of the Nernst equation that uses non-standardconditions.)