What is the equation that relates Keq with AE'o? (Hint: Rearrange two different equations). O In (Keq) = (NFAE'0)/(RT) O In (Keq) = (RT)/(NFAE'o) O In (Keq) = (nF)/(AE'•RT) O In (Keq) = (n)/(FAE'•RT) %3D %3D %3D

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What is the equation that relates Keq with AE'o? (Hint: Rearrange two different equations).
O In (Keq) = (nFAE'•)/(RT)
O In (Keq) = (RT)/(NFAE'o)
O In (Keq) = (nF)/(AE'•RT)
O In (Keq) = (n)/(FAE'•RT)
Transcribed Image Text:What is the equation that relates Keq with AE'o? (Hint: Rearrange two different equations). O In (Keq) = (nFAE'•)/(RT) O In (Keq) = (RT)/(NFAE'o) O In (Keq) = (nF)/(AE'•RT) O In (Keq) = (n)/(FAE'•RT)
Use the table below and the following information to answer questions
Standard Reduction Potential of Some
Biologically Important Half-Reactions, at pH 7.0 and 25°C (298 K)
Half-reaction
E° (V)
2H* + 2e H, (at standard conditions, pH 0)
Crotonyl-CoA + 2H + 2e butyryl-CoA
Oxaloacetate?- + 2H* + 2e malate2-
Pyruvate + 2H+ + 2e
Acetaldehyde + 2H* + 2e-
FAD + 2H* + 2e .
Glutathione + 2H* + 2e 2 reduced glutathione
S + 2H+ + 2e
Lipoic acid + 2H+ + 2e
NAD* + H* + 2e
NADP+ + H* + 2e"
0.000
-0.015
-0.166
lactate
- ethanol
-0.185
-0.197
FADH,
-0.219*
>
-0.23
H,S
-0.243
→ dihydrolipoic acid
-0.29
-0.320
-0.324
-0.346
-0.38
-0.414
-0.432
NADH
- NADPH
Acetoacetate + 2H* + 2e B-hydroxybutyrate
a-Ketoglutarate + co, + 2H* + 2e → isocitrate
2H* + 2e H, (at pH 7)
Ferredoxin (Fe3+) + e ferredoxin (Fe2+)
Source: Data mostly from Loach, PA. (1976) In Handbook of Biochemistry and Molecular Biology, 3rd edn (Fasman,
G.D., ed.), Physical and Chemical Data, Vol. I, pp. 122-130, CRC Press, Boca Raton, FL.
* This is the value for free FAD; FAD bound to a specific flavoprotein (for example succinate dehydrogenase) has a dif-
ferent E" that depends on its protein environments.
Transcribed Image Text:Use the table below and the following information to answer questions Standard Reduction Potential of Some Biologically Important Half-Reactions, at pH 7.0 and 25°C (298 K) Half-reaction E° (V) 2H* + 2e H, (at standard conditions, pH 0) Crotonyl-CoA + 2H + 2e butyryl-CoA Oxaloacetate?- + 2H* + 2e malate2- Pyruvate + 2H+ + 2e Acetaldehyde + 2H* + 2e- FAD + 2H* + 2e . Glutathione + 2H* + 2e 2 reduced glutathione S + 2H+ + 2e Lipoic acid + 2H+ + 2e NAD* + H* + 2e NADP+ + H* + 2e" 0.000 -0.015 -0.166 lactate - ethanol -0.185 -0.197 FADH, -0.219* > -0.23 H,S -0.243 → dihydrolipoic acid -0.29 -0.320 -0.324 -0.346 -0.38 -0.414 -0.432 NADH - NADPH Acetoacetate + 2H* + 2e B-hydroxybutyrate a-Ketoglutarate + co, + 2H* + 2e → isocitrate 2H* + 2e H, (at pH 7) Ferredoxin (Fe3+) + e ferredoxin (Fe2+) Source: Data mostly from Loach, PA. (1976) In Handbook of Biochemistry and Molecular Biology, 3rd edn (Fasman, G.D., ed.), Physical and Chemical Data, Vol. I, pp. 122-130, CRC Press, Boca Raton, FL. * This is the value for free FAD; FAD bound to a specific flavoprotein (for example succinate dehydrogenase) has a dif- ferent E" that depends on its protein environments.
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