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. Assumethat the reaction occurs at pH 7.[malate] = 1.45 mMAG:[oxaloacetate] = 0.130 mM[NAD+ ] = 110 mM[NADH] = 44 mM47.06IncorrectkJ.mol-1

The free energy change for the malate dehydrogenase reaction of the TCA cycle is ≈21.122…

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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Calculate and compare the AGº' values for the oxidation of succinate by NAD and FAD. Use the data given in the table to find the 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. Oxidant NAD + Fumarate Reductant NADH + H Succinate + AGO for the oxidation of succinate by NAD AGO for the oxidation of succinate by FAD: n 2 E'o (V) -0.32 T -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 -1 kJ mol-¹
Refer to the figure shown here, and determine the value of E for the overall oxidation/reduction reaction (refer to the book/lecture slides if you need help with the overall reaction). 121/202 + 2H+ + 2e → H₂0 NAD + H* + 2e → NADH O-1.136 volts O 0.496 volts O+1.136 volts voltsm -0.496 volts EU (volts) +0.816 - 0.320
Which of the reactions are spontaneous (favorable)? C6H130,P + ATP → › C6H14º₁₂P2 + ADP AG = -14.2 kJ/mol L-malate + NAD+ → oxaloacetate + NADH + H+ AG = 29.7 kJ/mol glutamate + NAD+ + H₂O → NH‡ + α-ketoglutarate + NADH + H+ AG = 3.7 kcal/mol → CH2O4 + H2O AG = 3.1 kJ/mol * CąHẠO, — CH,O4 + H,O DHAP C₂H + H₂ glyceraldehyde-3-phosphate AG = 3.8 kJ/mol Rh(I) C2H6 AG-150.97 kJ/mol
Calculate the standard free-energy change, deltaG'o, for the reaction in which acetaldehyde is reduced by the biological electron carrier NADH in the reaction acetaldehyde + NADH + H+ → ethanol + NAD+. Then calculate the actual free-energy change, deltaG, when the acetaldehyde is 1.51 M, the NADH is 1.02 M, the ethanol is 0.13 M and the NAD+ is 0.19 M, at 33.35oC and pH = 7. Give the actual free-energy change in kJ/mol to one decimal place. See Table 13-7b for the E'o values. please provide comprehensive explaination with each step.
For the following enzymes (3-6) predict how the conditions will most likely affect the enzymes activity with one of the following and provide a 1 sentence explanation: a. increase activity b. decrease activity c. not likely to alter activity 3) alpha-ketoglutarate dehydrogenase complex binding to AMP when [AMP] is high. 4) phosphohexose isomerase binding NADH when [NADH] is high 5) phosphofructose-1 binding NAD+ when [NAD+] is high 6) pyruvate dehydrogenase complex binding to ATP when [ATP] is high
Draw the products of the reaction of xylulose-5-phosphate and erythrose-4-phosphate catalyzed by transketolase in the pentose phosphate pathway. Provide the structure in the protonation state found in physiological conditions. H H H OH FO HO-H H-OH H OPO3²- Q transketolase Draw glyceraldehyde-3- phosphate H H- H H H O OH OH OPO3²- Draw fructose-6- phosphate Q I I
Calculate the standard free-energy change, deltaG'o, for the reaction in which acetaldehyde is reduced by the biological electron carrier NADH in the reaction acetaldehyde + NADH + H+ → ethanol + NAD+. Then calculate the actual free-energy change, deltaG, when the acetaldehyde is 1.51 M, the NADH is 1.02 M, the ethanol is 0.13 M and the NAD+ is 0.19 M, at 33.35oC and pH = 7. Give the actual free-energy change in kJ/mol to one decimal place. See Table 13-7b for the E'o values.
Write out the full redox reaction that happens when both of these reactions are added to the same reaction where there is 1M concentrations of each reactant and products, pH7, and temeprature is 290K. Identify which compounds will be reduced and which compounds will be oxidized. redox reaction 1: Pyruvate¯ + 2H+ + 2e¯ → lactate¯ E'o(V) = -0.185 redox reaction 2: NAD+ + H+ + 2e¯ → NADH E'o(V) = -0.320
Given the following information on reduction potentials, calculate the standard free energy in kJ/mol based on your understanding of electron transfer through the pyruvate dehydrogenase complex. Round to nearest whole number. Lipoamide + 2H+ + 2e- → dihydrolipoamide ∆εο = -0.29 FAD + 2H+ + 2e- → FADH2 ∆εο = −0.01
Under standard conditions, will the following reactions proceed spontaneously as written? (1) Fumarate + NADH + H+ (2) succinate + NAD+ Cyto a (Fe²+) + cyto b (Fe³+) = cyto a (Fe³+) + cyto 6 (Fe²+) b
Malate dehydrogenase has a ΔGo′ΔGo′= 29.5 kJ/mol for the formation of oxaloacetate from malate yet plays a crucial role in the Citric Acid Cycle. Explain (briefly) how this enzyme with a very non-spontaneous ΔGo′ΔGo′can function well in a biochemical pathway.
All dehydrogenases of glycolysis and the TCA cycle use NAD* (E° for NAD*/NADH is -0.32V) as electron acceptor except succinate dehydrogenase (which uses FAD (E° for FAD/FADH2 is 0.05V). Based on AG° = -NFEº, show and state (1-2 sentences) why is FAD a more appropriate electron acceptor than NAD* in the dehydrogenation of succinate (consider the E° values of %3D Uptake in Na+ Vmax Uptake in absence of Na+ Vmax substrate K: (mM) Kt (mM) L-leucine 420 0.24 23 0.2 D-Leucine 310 4.7 5 4.7 L-valine 225 0.31 19 0.31 fumarate/succinate (E° = 0.031), NAD*/NADH, and the succinate dehydrogenase FAD/FADH2).

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