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. TABLE 13-7bStandard Reduction Potentials of Some Biologically Important Half-ReactionsHalf-reactionE" (V)Pyruvate + 2H+ 2e → lactate--0.185Acetaldehyde + 2H+ + 2e → ethanol-0.197FAD + 2H+ + 2e- → FADH₂-0.219aGlutathione + 2H+ + 2e → 2 reduced glutathione-0.23S + 2H+ + 2e → H₂S-0.243Lipoic acid + 2H+ + 2e → dihydrolipoic acid-0.29NAD+ + H+ + 2e → NADH-0.320NADP+ + H+ + 2e- → NADPH-0.324-0.346Acetoacetate + 2H+ + 2e → B-hydroxybutyratea-Ke glutarate + CO₂ + 2H+ + 2e → isocitrate-0.382H+ + 2e → H₂ (at pH 7)-0.414Ferredoxin (Fe³+) + e- → ferredoxin (Fe²+)-0.432Source: Data mostly from R. A. Loach, in Handbook of Biochemistry and Molecular Biology, 3rd edn (G. D. Fasman, ed.), Physicaland Chemical Data, Vol. 1, p. 122, CRC Press, 1976.This is the value for free FAD; FAD bound to a specific flavoprotein (e.g., succinate dehydrogenase) has a different E" that dependson its protein environment. TABLE 13-7a Standard Reduction Potentials of Some Biologically Important Half-ReactionsHalf-reactionE° (V)¹/2 O₂ + 2H+ + 2e- → H₂O0.816Fe³+ + e Fe²+0.771NO3 + 2H+ + 2e → NO₂ + H₂O0.421Cytochrome f (Fe³+) + e- → cytochrome f (Fe²+)0.365Fe(CN)63- (ferricyanide) + e- → Fe(CN)64-0.360.35Cytochrome a3 (Fe³+) + ¯ → cytochrome a3 (Fe²+)O₂ + 2H+ + 2e → H₂O₂0.2950.290.254Cytochrome a (Fe³+) + e- → cytochrome a (Fe²+)Cytochrome c (Fe³+) + e- cytochrome c (Fe²+)Cytochrome (Fe³+) + e- → cytochrome c₁ (Fe²+)Cytochrome b (Fe³+) + e- → cytochrome b (Fe²+)Ubiquinone + 2H+ + 2e¯ → ubiquinol0.220.0770.045Fumarate² + 2H+ + 2e → succinate2-0.0310.0002H+ + 2e → H₂ (at standard conditions, pH 0)Crotonyl-CoA + 2H+ + 2e → butyryl-CoA-0.015Oxaloacetate²- + 2H+ + 2e → malate²--0.166Source: Data mostly from R. A. Loach, in Handbook of Biochemistry and Molecular Biology, 3rd edn (G. D. Fasman, ed.), Physicaland Chemical Data, Vol. 1, p. 122, CRC Press, 1976.This is the value for free FAD; FAD bound to a specific flavoprotein (e.g., succinate dehydrogenase) has a different Eº that dependson its protein environment.

Relevant reaction and their standard reduction potential: Acetaldehyde + 2H+ + 2e- →ethanol…

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.

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.

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter18: Glycolysis

Section: Chapter Questions

Problem 12P

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