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what is the overall free energy change under standard conditions for the passage of two electrons from β-hydroxybutyrate to oxygen through passage through the electron transfer chain?

what is the overall free energy change under standard conditions for the passage of two electrons from β-hydroxybutyrate to oxygen through passage through the electron transfer chain?

Chemistry
Chemistry
10th Edition
ISBN:9781305957404
Author:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste
Publisher:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste
Chapter1: Chemical Foundations
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Problem 1RQ: Define and explain the differences between the following terms. a. law and theory b. theory and...
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what is the overall free energy change under standard conditions for the passage of two electrons from β-hydroxybutyrate to oxygen through passage through the electron transfer chain?

Standard Reduction Potentials of Some Biologically Important Half-Reactions Half-reaction E° (V) ½ 02 + 2H* +2e → H20 0.816 Fe+ + e Fe2+ 0.771 NO, + 2H* + 2e NO, + H,0 0.421 Cytochrome f (Fe)+ e cytochrome f (Fe2+) 0.365 Fe(CN) (ferricyanide) + e Cytochrome a, (Fe*) + e cytochrome a, (Fe2*) 0, + 2H +2e H,02 Cytochrome a (Fe*) + e cytochrome a (Fe2+) Cytochrome c (Fe)+ e cytochrome c (Fe2+) Fe(CN)- 0.36 0.35 0.295 0.29 0.254 Cytochrome c, (Fe+) + e- cytochrome c, (Fe2+) Cytochrome b (Fet) + e cytochrome b (Fe2+) Ubiquinone + 2H* + 2e Fumarate?- + 2H* + 2e 2H* + 2e H2 (at standard conditions, pH 0) 0.22 0.077 ubiquinol 0.045 succinate?- 0.031 0.000 Crotonyl-CoA + 2H* + 2e. Oxaloacetate?-+ 2H +2e →butyryl-CoA malate?- -0.015 -0.166 Pyruvate + 2H* + 2e lactate -0.185 Acetaldehyde+ 2H* + 2e ethanol -0.197 FAD + 2H* + 2e FADH2 -0.219 Glutathione + 2H* + 2e 2 reduced glutathione S+ 2H* + 2e H,S -0.23 -0.243 Lipoic acid + 2H +2e dihydrolipoic acid NAD+ + Ht + 2e NADH -0.29 -0.320 NADP* + H* + 2e NADPH -0.324 Acetoacetate + 2H* + 2e- B-hydroxybutyrate -0.346 a-Ketoglutarate + CO, + 2H + 2e isocitrate -0.38 2H* + 2e-H2 (at pH 7) -0.414 Ferredoxin (Fe3+) + e ferredoxin (Fe?+) -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:Standard Reduction Potentials of Some Biologically Important Half-Reactions Half-reaction E° (V) ½ 02 + 2H* +2e → H20 0.816 Fe+ + e Fe2+ 0.771 NO, + 2H* + 2e NO, + H,0 0.421 Cytochrome f (Fe)+ e cytochrome f (Fe2+) 0.365 Fe(CN) (ferricyanide) + e Cytochrome a, (Fe*) + e cytochrome a, (Fe2*) 0, + 2H +2e H,02 Cytochrome a (Fe*) + e cytochrome a (Fe2+) Cytochrome c (Fe)+ e cytochrome c (Fe2+) Fe(CN)- 0.36 0.35 0.295 0.29 0.254 Cytochrome c, (Fe+) + e- cytochrome c, (Fe2+) Cytochrome b (Fet) + e cytochrome b (Fe2+) Ubiquinone + 2H* + 2e Fumarate?- + 2H* + 2e 2H* + 2e H2 (at standard conditions, pH 0) 0.22 0.077 ubiquinol 0.045 succinate?- 0.031 0.000 Crotonyl-CoA + 2H* + 2e. Oxaloacetate?-+ 2H +2e →butyryl-CoA malate?- -0.015 -0.166 Pyruvate + 2H* + 2e lactate -0.185 Acetaldehyde+ 2H* + 2e ethanol -0.197 FAD + 2H* + 2e FADH2 -0.219 Glutathione + 2H* + 2e 2 reduced glutathione S+ 2H* + 2e H,S -0.23 -0.243 Lipoic acid + 2H +2e dihydrolipoic acid NAD+ + Ht + 2e NADH -0.29 -0.320 NADP* + H* + 2e NADPH -0.324 Acetoacetate + 2H* + 2e- B-hydroxybutyrate -0.346 a-Ketoglutarate + CO, + 2H + 2e isocitrate -0.38 2H* + 2e-H2 (at pH 7) -0.414 Ferredoxin (Fe3+) + e ferredoxin (Fe?+) -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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