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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.

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.

Biochemistry
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
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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.

TABLE 13-7b Standard Reduction Potentials of Some Biologically Important Half- Reactions Half-reaction E" (V) Pyruvate- + 2H + 2e- → lactate- -0.185 Acetaldehyde + 2H* + 2e- → ethanol -0.197 FAD + 2H+ + 2e- → FADH2 -0.219a Glutathione + 2H* + 2e- → 2 reduced glutathione -0.23 S+ 2H* + 2e¯ → H,S -0.243 Lipoic acid + 2H* + 2e- → dihydrolipoic acid -0.29 NAD+ + H+ + 2e- → NADH -0.320 NADP+ + H*+ + 2e- → NADPH -0.324 Acetoacetate + 2H* + 2e- → B-hydroxybutyrate -0.346 a-Ketoglutarate + CO2 + 2H* + 2e- → isocitrate 2H* + 2e → H2 (at pH 7) -0.38 -0.414 Ferredoxin (Fe3+) + e¯ → ferredoxin (Fe2*) -0.432 Source: Data mostly from R. A. Loach, in Handbook of Biochemistry and Molecular Biology, 3rd edn (G. D. Fasman, ed.), Physical and 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 depends on its protein environment.
Transcribed Image Text:TABLE 13-7b Standard Reduction Potentials of Some Biologically Important Half- Reactions Half-reaction E" (V) Pyruvate- + 2H + 2e- → lactate- -0.185 Acetaldehyde + 2H* + 2e- → ethanol -0.197 FAD + 2H+ + 2e- → FADH2 -0.219a Glutathione + 2H* + 2e- → 2 reduced glutathione -0.23 S+ 2H* + 2e¯ → H,S -0.243 Lipoic acid + 2H* + 2e- → dihydrolipoic acid -0.29 NAD+ + H+ + 2e- → NADH -0.320 NADP+ + H*+ + 2e- → NADPH -0.324 Acetoacetate + 2H* + 2e- → B-hydroxybutyrate -0.346 a-Ketoglutarate + CO2 + 2H* + 2e- → isocitrate 2H* + 2e → H2 (at pH 7) -0.38 -0.414 Ferredoxin (Fe3+) + e¯ → ferredoxin (Fe2*) -0.432 Source: Data mostly from R. A. Loach, in Handbook of Biochemistry and Molecular Biology, 3rd edn (G. D. Fasman, ed.), Physical and 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 depends on its protein environment.
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