Calculate and compare the AG values for the oxidation of succinate by NAD+ and FAD. Use the data given in the table to findthe E of the NAD+: NADH and fumarate:succinate couples, and assume that E for the enzyme-bound FAD: FADH2 redoxcouple is nearly +0.05 V.OxidantReductant"E' (V)NAD+NADH + H+2-0.32FumarateSuccinateAG°' for the oxidation of succinate by NAD+:AG°' for the oxidation of succinate by FAD:2-0.03Why is FAD rather than NAD+ the electron acceptor in the reaction catalyzed by succinate dehydrogenase?The electron-transport chain can regenerate FAD, but not NAD+.FAD is an oxidant, whereas NAD+ is a reductant.The oxidation of succinate requires two NAD+ molecules but only one FAD molecule.The oxidation of succinate by NAD+ is not thermodynamically feasible.kJ mol-1kJ mol-1

Solution: The correct answer is: The oxidation of succinate by NAD* is not thermodynamically…

Answered: Calculate and compare the AG values for…

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter27: Metabolic Integration And Organ Specialization

Section: Chapter Questions

Problem 4P

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Similar questions

Energetics of the Hexokinase Reaction The standard-state free energy change. Gfor the hexokinase reaction, is â€” 1 6.7 kJ/mol. Use the values in Table I to calculate the value of Gfor this reaction in the erythrocyte at 37Â°C.
Distinguishing the Mechanisms of Class I and Class I Aldolases Fructose bisphosphate aldolase in animal muscle is a class 1 aldolase, which forms a Schiff base intermediate between substrate (for example. fructose-1, 6-bisphosphate or dihydroxyacetone phosphate) and a lysine at the active site (see Figure I8.12). The chemical evidence for this intermediate conies from studies with aldolase and the reducing agent sodium borohydride, NaBH4. Incubation of the enzyme with dihydroxyacetone phosphate and NaBH4 inactivates the enzyme. Interestingly, no inactivation is observed if NabH4 is added to the enzyme in the absence of substrate. Write a mechanism that explains these observations and provides evidence for the formation of a Schiff base intermediate in the aldolase reaction.
Using the ActiveModel for enoyl-CoA dehydratase, give an example of a case in which conserved residues in slightly different positions can change the catalytic rate of reaction.
The Catabolism of Uric Acid Write a balanced equation for the oxidation of uric acid to glyoxylic acid, CO2, and NH3, showing each step in the process and naming all of the enzymes involved.
Figure 27.3 illustrates the response of R (ATP-regenerating) and U (ATP-utilizing) enzymes to energy charge. a. Would hexokinase be an R enzyme or a U enzyme? Would glutamine: PRPP amidotransferase, the second enzyme in purine biosynthesis, be an R enzyme or a U enzyme? b. If energy charge = 0.5: Is the activity of hexokinase high or low? Is ribose-5-P pyrophosphokinase activity high or low? c. If energy charge = 0.95: Is the activity of hexokinase high or low? Is ribose-5-P pyrophosphokinase activity high or low?
Based on your knowledge of the structure of NAD+ and an assumption that coenzyme dissociation is the rate limiting step of the alcohol dehydrogenase mechanism, hypothesize why a N249W mutation at the coenzyme binding site would increase the rate of catalysis.
Extending the Mechanism of Methylmalonyl-CoA Mutase to Similar Reactions Based on the mechanism for the methylmalonyl-CoA mutase (see problem 14), write reasonable mechanisms for the following reactions shown.
Radiolabeling with 14C-Glutamate Describe the labeling pattern that would result from the introduction into the TCA cycle of glutamate labeled at Cy with 14C.
Characterizing Glycolysis List the reactions of glycolysis that a. are energy consuming (under standard-stale conditions), b. are energy yielding (under standard-state conditions), c. consume ATP. d. yield ATP e. are strongly influenced by changes in concentration of substrate and product because of their molecularity. f. are at or near equilibrium in the erythrocyte (see Table 18.2).
Based on your residing of this chapter, what would you expect to be the most immediate effect oil glycolysis, if the steady-state concentration of gJucose-6-P were 8.3 mM instead of 0.083 mM?
Using the ActiveModel for aldose reductase, describe the structure of the TIM barrel motif and the structure and location of the active site.
The Effect of lodoacetic Acid on the Glyceraldehyde-3-P Dehydrogenase Reaction (Integrates with Chapters 4 and 14.) How might iodoacetic acid affect the glyceraldehydes-3-phosphate dehydrogenase reaction in glycolysis? Justify your answer.

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