Consider the malate dehydrogenase reaction from the citric acid cycle. Given the listed concentrations, calculate the free energychange for this reaction at energy change for this reaction at 37.0 °C (310 K). AG' for the reaction is +29.7 kJ/mol. Assume thatthe reaction occurs at pH 7.[malate]1.25 mM[oxaloacetate] = 0.290 mM[NAD+] = 430 mM[NADH] := 170 mMAG :kJ-mol-1* TOOLSx10

Malate dehydrogenase is citric acid cycle enzyme (metabolism) catalyzes the oxidation of malate into…

Answered: Consider the malate dehydrogenase…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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Consider the malate dehydrogenase reaction from the citric acid cycle. Given the listed concentrations, calculate the free energy change for this reaction at energy change for this reaction at 37.0 °C (310 K). AG' for the reaction is +29.7 kJ/mol. Assume that the reaction occurs at pH 7. [malate] = 1.43 mM [oxaloacetate] = 0.220 mM [NAD*] = 460 mM [NADH] = 180 mM AG : kJ-mol-1
Consider the malate dehydrogenase reaction from the citric acid cycle. Given the listed concentrations, calculate the free energy change for this reaction at energy change for this reaction at 37.0 ˚C (310 K). AG' for the reaction is +29.7 kJ/mol. Assume that the reaction occurs at pH 7. [malate] = 1.45 mM AG: [oxaloacetate] = 0.130 mM [NAD+ ] = 110 mM [NADH] = 44 mM 47.06 Incorrect kJ.mol-1
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 redox half reaction Oxaloacetate + 2H+ + 2e− → Malate has a standard reduction potential value of 0.166 V. Calculate the free energy (ΔG°′) for the following reaction: Malate + NAD+ → Oxaloacetate + NADH + H+
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…
When grown anaerobically on glucose, yeast (S. cerevisiae) converts pyruvate to acetaldehyde, then reduces acetaldehyde to Pethanol using electrons from NADH. Write the chemical equation for the reaction that reduces acetaldehyde (CH3CHO) to ethanol (CH3CH2OH). The table provides the standard reduction potential, E', of the relevant half-reactions. Half-reaction Acetaldehyde + 2 H+ + 2e¯ → ethanol NAD+ + 2H+ + 2e¯ → NADH + H+ E'° (V) -.197 -.320 Calculate the equilibrium constant, K'eq, at 25.0 °C for the reaction that reduces acetaldehyde to ethanol. K'e ×10 = eq
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
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
[AktivGrid] Draw the product of the reaction of isocitrate catalyzed by isocitrate dehydrogenase in the TCA (citric acid) cycle. Provide the structure in the protonation state found in physiological conditions. 9 H-C-OH 800- -H CH₂ ° Coo of NAD+ dehydrogen isocitrate ase NADH, H*, Drawing CO2
The standard free energy change for the reaction catalyzed by phosphoglucomutase is -7.1 kJ/mol. Calculate the equilibrium constant for the reaction. Calculate AG at 37°C when the concentration of glucose-1-phosphate is 1-mM and the concentration of glucose-6-phosphate is 25-mM. Is the reaction spontaneous under these conditions? HOCH, -20;POCH, H H H H H H ОН Н НО ОН Н H НО ОН H ОН H. ОН Glucose-l-phosphate Glucose-6-phosphate
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%)
(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

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Consider the malate dehydrogenase reaction from the citric acid cycle. Given the listed concentrations, calculate the free energy change for this reaction at energy change for this reaction at 37.0 °C (310 K). AGº' for the reaction is +29.7 kJ/mol. Assume that the reaction occurs at pH 7.