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Begining with 1 M concentrations of each reactant and product at pH=7 and 25.0 degrees C, calculate the K'eq (to one decimal point) of the reaction Pyruvate + NADH+H+ <=> Lactate + NAD+. Note the temperature of this reaction will not affect the standard reducton potential delta E'o in the table 13-7b. please provide a comprehensive explanation with each step taken

Begining with 1 M concentrations of each reactant and product at pH=7 and 25.0 degrees C, calculate the K'eq (to one decimal point) of the reaction Pyruvate + NADH+H+ <=> Lactate + NAD+. Note the temperature of this reaction will not affect the standard reducton potential delta E'o in the table 13-7b. please provide a comprehensive explanation with each step taken

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
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Begining with 1 M concentrations of each reactant and product at pH=7 and 25.0 degrees C, calculate the K'eq (to one decimal point) of the reaction Pyruvate + NADH+H+ <=> Lactate + NAD+.
Note the temperature of this reaction will not affect the standard reducton potential delta E'o in the table 13-7b.

please provide a comprehensive explanation with each step taken.
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 → H₂S -0.243 Lipoic acid + 2H+ + 2e → dihydrolipoic acid -0.29 NAD+ + H+ + 2e → NADH -0.320 NADP+ + H+ + 2e- → NADPH -0.324 -0.346 Acetoacetate + 2H+ + 2e → B-hydroxybutyrate a-Ke glutarate + CO₂ + 2H+ + 2e → isocitrate -0.38 2H+ + 2e → H₂ (at pH 7) -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 → H₂S -0.243 Lipoic acid + 2H+ + 2e → dihydrolipoic acid -0.29 NAD+ + H+ + 2e → NADH -0.320 NADP+ + H+ + 2e- → NADPH -0.324 -0.346 Acetoacetate + 2H+ + 2e → B-hydroxybutyrate a-Ke glutarate + CO₂ + 2H+ + 2e → isocitrate -0.38 2H+ + 2e → H₂ (at pH 7) -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.
TABLE 13-7a Standard Reduction Potentials of Some Biologically Important Half- Reactions Half-reaction E° (V) ¹/2 O₂ + 2H+ + 2e- → H₂O 0.816 Fe³+ + e Fe²+ 0.771 NO3 + 2H+ + 2e → NO₂ + H₂O 0.421 Cytochrome f (Fe³+) + e- → cytochrome f (Fe²+) 0.365 Fe(CN)63- (ferricyanide) + e- → Fe(CN)64- 0.36 0.35 Cytochrome a3 (Fe³+) + ¯ → cytochrome a3 (Fe²+) O₂ + 2H+ + 2e → H₂O₂ 0.295 0.29 0.254 Cytochrome 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¯ → ubiquinol 0.22 0.077 0.045 Fumarate² + 2H+ + 2e → succinate2- 0.031 0.000 2H+ + 2e → H₂ (at standard conditions, pH 0) Crotonyl-CoA + 2H+ + 2e → butyryl-CoA -0.015 Oxaloacetate²- + 2H+ + 2e → malate²- -0.166 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 Eº that depends on its protein environment.
Transcribed Image Text:TABLE 13-7a Standard Reduction Potentials of Some Biologically Important Half- Reactions Half-reaction E° (V) ¹/2 O₂ + 2H+ + 2e- → H₂O 0.816 Fe³+ + e Fe²+ 0.771 NO3 + 2H+ + 2e → NO₂ + H₂O 0.421 Cytochrome f (Fe³+) + e- → cytochrome f (Fe²+) 0.365 Fe(CN)63- (ferricyanide) + e- → Fe(CN)64- 0.36 0.35 Cytochrome a3 (Fe³+) + ¯ → cytochrome a3 (Fe²+) O₂ + 2H+ + 2e → H₂O₂ 0.295 0.29 0.254 Cytochrome 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¯ → ubiquinol 0.22 0.077 0.045 Fumarate² + 2H+ + 2e → succinate2- 0.031 0.000 2H+ + 2e → H₂ (at standard conditions, pH 0) Crotonyl-CoA + 2H+ + 2e → butyryl-CoA -0.015 Oxaloacetate²- + 2H+ + 2e → malate²- -0.166 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 Eº that depends on its protein environment.
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