Consider the two half-reactions below and their standard reduction potentials.NAD+ + H+ + 2e → NADHElo= -0.32 Va-Ketoglutarate + CO₂ + 2H+ + 2e → Isocitrate E' = -0.38 V(a) What is AE" for the spontaneous redox reaction that is, the reaction that actuallyoccurs 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]DEWhat is the value of AG under those conditions?(Hints: pH 7 is already included in AG". Similarly, 1 atm is the standard pressure ofCO2, which is also taken into account in AG.)

∆G'0 = -nF∆E'0 here; ∆G'0 is the change in standard Gibbs free energy. 'n' is the number of…

Answered: Consider the two half-reactions below…

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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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%)
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 K
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
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?
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.
The ΔG°′ for hydrolytically removing a phosphoryl group from ATP is about twice as large as the ΔG°′ for hydrolytically removing a phosphoryl group from AMP (−14 kJ · mol−1). Explain the discrepancy.
a) Calculate the enzyme and specific activity of a reaction with 3 μM Hsp90 using the following information: The rate is measured in a spectrophotometer as 0.028 OD units/min in a 1 ml reaction volume. The absorbance was detected at 340nm and the extinction coefficient for NADH at this wavelength is 6200 L M-1 min-1 and the molecular mass of Hsp90 is 82.7 kDa. The rate of NADH utilisation is equivalent to the rate of ATP utilised by Hsp90. Show all your calculations and the units for your answers. b) Calculate the turnover number for the reaction described in (a) above
Consider the following equilibrium at 25ºC :Glucose-1-Phosphate Glucose-6-PhophateUsing the equilibrium concentrations of [Glucose-1-Phosphate] = 0.35 M and [Glucose-6-Phosphate] = 1.65 M, calculate BOTH K′eqand Gº′ for this reaction. Is this reaction exergonicor endergonic? R = 8.314 J/K·mol
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
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 reactionPyruvate-(aq) + NADH(aq) + H+(aq) → lactate-(aq) + NAD+(aq)where NAD+ is the oxidized form of nicotinamide adenine dinucleotide, occurs in muscle cells deprived of oxygen during strenuous exercise and can lead to cramp. Calculate the biological standard Gibbs energy, ΔrG⊕, for the reaction at 310 K given that the thermodynamic standard reaction Gibbsenergy ΔrGΘ = -66.6 kJ mol-1.

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