Calculate and compare the AGº' values for the oxidation of succinate by NAD and FAD. Use the data given in the table to findthe E' of the NAD: NADH and fumarate:succinate couples, and assume that E' for the enzyme-bound FAD : FADH₂ redox+couple is nearly +0.05 V.OxidantNAD+FumarateReductantNADH + HSuccinate+AGO for the oxidation of succinate by NADAGO for the oxidation of succinate by FAD:n2E'o (V)-0.32T-0.03+FAD is an oxidant, whereas NAD is a reductant.+Why is FAD rather than NAD the electron acceptor in the reaction catalyzed by succinate dehydrogenase?+The oxidation of succinate by NAD is not thermodynamically feasible.+The oxidation of succinate requires two NAD molecules but only one FAD molecule.+The electron-transport chain can regenerate FAD, but not NAD˚.kJ mol-¹-1kJ mol-¹

Calculation for balance cell reaction using Nernst equationHalf reactions (Reduction) NAD + 2H+ +…

Answered: Calculate and compare the AG' values…

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter27: Metabolic Integration And Organ Specialization

Section: Chapter Questions

Problem 4P

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(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
A mutant version of DADH can use NADP+ as a cofactor for isopropanol oxidation. Velocity data was collected from reactions at a series of NADP+ concentrations. The following trendline was obtained for a Lineweaver-Burk plot of the data: y = 0.00007x + 0.0014 Note that the NADP+ substrate concentrations are in mM and the reaction velocity was measured in nmol/min. Calculate the Km and Vmax for DADH with this substrate. Show your work.
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?
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?
The enzyme lactate dehydrogenase catalyzes the reversible reaction lactate (CH3 CHOHCOO )+NAD* рyruvate (CH3 COCOO) + NADH + H+ Given the standard reduction potentials CH3 СОСОО + 2H+ + 2е CH3 CHОНСО" E°'= -0. 185 V NADŤ + H+ + 2e- → NADH = -0. 320 V E°' would you expect the reaction to be spontaneous in the forward or reverse direction under biochemical standard state conditions? How could you change the reaction conditions to force the reaction to be spontaneous in the opposite direction? Please explain your answer.
Given what you know about the involvement of nicotinamide nucleotides inoxidative and reductive metabolic reactions, predict whether the followingintracellular concentration ratios should be 1, > 1, or < 1. Explain youranswers.(a) [NAD+] >[NADH](b) [NADP+] >[NADPH](c) Since NAD+ and NADP+ are essentially equivalent in their tendency to attract electrons, discuss how the two concentration ratios might bemaintained inside cells at greatly differing values.
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
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
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.
Consider the typical beta oxidation of linoleic acid (C18:2 ^Δ9, 12): How many ATP are generated in complete oxidation of linoleic acid? How many NADH are generated in complete oxidation of linoleic acid? How many FADH2 are generated in complete oxidation of linoleic acid?
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+2⁢H++2⁢e^− ubiquinolubiquinol 0.045 NAD^++H^++2e−NAD^++H^++2⁢e^− NADHNADH –0.32 Calculate Δ?′0 for the reaction as shown. Δ?′0=____(V) Calculate Δ?′0 . Δ?′0=____(kJ/mol)
Calculate the slope on a Lineweaver-Burk plot (Km / Vmax) for the lactase reaction with inhibitor X. (inhibitor X changes lactase activity to a Vo of 0.10 mM per minute when [S] = 1.0 mM, and a Vo of 0.133333333333 mM per minute when [S] = 2.0 mM) 0.20 per minute 0.50 per minute 1.0 per minute 2.0 per minute 5.0 per minute

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