4 Given that the reduction potential Eo'=-320, +10, +816, and +50mV for NAD+, fumarate, O, and acyl-CoA DH bound- FAD,respectively, calculate the free energy for a pair of electrons originating from the first reaction of b-oxidation of a fatty acylgroup, as it traverses the ETC.R= 8.315 x 10 J/mol K; Faraday constant, F= 96.48 KJ/V-mol, assume standard state T= 25°C and physiological conditionsare T= 37°C. Report a whole number.Remember a Reduction potential is DEFINED asX() +e- --> X(red)Be sure you have defined your oxidation and reduction species properly.kJ/mole

An oxidizing species is the substance that donates electrons, and a reducing species is the…

Answered: Given that the reduction potential Eo'=…

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter20: Electron Transport And Oxidative Phosphorylation

Section: Chapter Questions

Problem 10P

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Energetics of the Hexokinase Reaction The standard-state free energy change. Gfor the hexokinase reaction, is â€” 1 6.7 kJ/mol. Use the values in Table I to calculate the value of Gfor this reaction in the erythrocyte at 37Â°C.
Given that the reduction potential Eo'=-320, +10, +816, and +50mV for NAD+, fumarate, 02 and G3P DH bound FAD, respectively, calculate the free energy for a pair of electrons originating from the oxidation of glycerol-3-P to DHAP of, as it traverses the ETC. R = 8.315 x 10 J/mol K; Faraday constant, F= 96.48 KJ/V-mol, assume standard state T= 25°C and physiological conditions are T= 37°C. Report a whole number. Remember a Reduction potential is DEFINED as X(ax) +e- --> X(red) Be sure you have defined your oxidation and reduction species properly. kJ/mole
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
Acetyl CoA + 2H* + 2e = pyruvate + COASH E = -0.48 V Ubiquinone + 2H* + 2e = Ubiquinol E" = +0.04 V Consider the redox rxn wherein a pair of e passes from pyruvate to ubiquinone. Calculate the change in standard Gibbs free energy (kJ/mol). Report answer to two decimal places.
Acetyl-CoA is formed from acetate by coupling two reactions: ATP + H20 = ADP + P; AG" = -36.03 kJ/mol %3D acetate + CoA acetyl CoA + H20 AG" = +33.21 kJ/mol %3D 1. Calculate the overall AG' (reported up to two decimal places) for the net reaction. kJ/mol 2. Calculate the Keg (reported up to two decimal places and do not use scientific notation) for the net reaction at 298.15K. NOTE: R= 8.314 x 103 kJ/mol-K
Calculate AG for this reaction under the following conditions: 37°C, pH 7, [Pyruvate] = [CO₂] = 4.0 mM, [OAA] = 2.0 mM, [ATP] = 3.5 mM, [P;] = 5.0 mM, and [ADP] = 1.8 mM. Use 2 signficant figures. AG= i kJ.mol-1 Under these conditions, the reaction is (Tolerance is +/- 2%)
Consider the two half-reactions below and their standard reduction potentials. NAD+ + H+ + 2e → NADH Elo= -0.32 V a-Ketoglutarate + CO₂ + 2H+ + 2e → Isocitrate E' = -0.38 V (a) What is AE" for the spontaneous redox reaction that is, the reaction that actually occurs under standard biochemical conditions (pH 7)? (b) Which of the following statements are correct under standard biochemical conditions? i. The concentration of H+ is 1.0 M. ii. The reaction NAD+ + Isocitrate → NADH + H+ + a-Ketoglutarate + CO₂ is favor- able. iii. NAD+ accepts electrons from isocitrate. iv. The NAD → NADH reaction actually occurs in reverse. The a-ketoglutarate → isocitrate reaction occurs as written. (c) Calculate AG" for the reaction in (a). (pH 7, 25°C, pressure, 1 atm.) (d) Suppose that the actual conditions are T = 25°C, pH = 7, CO₂ = 1 atm, [a-Ketoglutarate] 10 mM, [NAD+] = 2.5 mM, and [NADH] = 0.5 mM. PAR = 2 mM, [Isocitrate] DE What is the value of AG under those conditions? (Hints: pH 7 is already…
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
For 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 standard free energy change (AG) for the transfer of electrons from succinate to ubiquinone: Succinate + ubiquinone O-2.7 kJ/mol O2.7 kJ/mol O-8.7 kJ/mol O 14.7 kJ/mol succinate dehydrogenase relevant half-reactions and standard reduction potentials: fumarate + 2 H* + 2 e succinate ubiquinone + 2H + 2 e -6.0 kJ/mol 11 Fumarate + ubiquinol ubiquinol E = 0.031 V E = 0.045 V
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.
explain in quantitative terms the circumstances under which the following reaction can porceed; L-malate + NAD+ (forward arrow) oxaloacetate + NADH + H+ delta G' standard = +29.7 KJ/mol

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