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
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
icon
Related questions
Question

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.
Expert Solution
steps

Step by step

Solved in 2 steps

Blurred answer
Similar questions
  • SEE MORE QUESTIONS
Recommended textbooks for you
Biochemistry
Biochemistry
Biochemistry
ISBN:
9781305577206
Author:
Reginald H. Garrett, Charles M. Grisham
Publisher:
Cengage Learning