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Using the half reactions from the given table, what is the reaction of this reduction-oxidation?

Using the half reactions from the given table, what is the reaction of this reduction-oxidation?

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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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.
In the tricarboxylic acid cycle, L-malate is oxidized to oxaloacetate, using NAD+ as an oxidizing agent. Using the half reactions from the given table, what is the reaction of this reduction-oxidation? Oxaloacetate + NAD+ +→ L-Malate + NADH L-Malate + Oxaloacetate -→ NAD+ + NADH L-Malate + NAD+ +→ Oxaloacetate + NADH L-Malate -→ Oxaloacetate + NAD+ + NADH
Transcribed Image Text:In the tricarboxylic acid cycle, L-malate is oxidized to oxaloacetate, using NAD+ as an oxidizing agent. Using the half reactions from the given table, what is the reaction of this reduction-oxidation? Oxaloacetate + NAD+ +→ L-Malate + NADH L-Malate + Oxaloacetate -→ NAD+ + NADH L-Malate + NAD+ +→ Oxaloacetate + NADH L-Malate -→ Oxaloacetate + NAD+ + NADH
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