All dehydrogenases of glycolysis and the TCA cycle use NAD* (E° for NAD*/NADHis -0.32V) as electron acceptor except succinate dehydrogenase (which uses FAD (E° forFAD/FADH2 is 0.05V).Based on AG° = -NFEº, show and state (1-2 sentences) why is FAD a more appropriateelectron acceptor than NAD* in the dehydrogenation of succinate (consider the E° values of%3DUptake in Na+VmaxUptake in absence of Na+VmaxsubstrateK: (mM)Kt (mM)L-leucine4200.24230.2D-Leucine3104.754.7L-valine2250.31190.31fumarate/succinate (E° = 0.031), NAD*/NADH, and the succinate dehydrogenaseFAD/FADH2).

The oxidation-reduction reaction is also called the Redox reaction. This reaction involves the…

Answered: All dehydrogenases of glycolysis and…

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter20: Electron Transport And Oxidative Phosphorylation

Section: Chapter Questions

Problem 7P

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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.
Compare the delta ΔG0' values for the oxidation of succinate by NAD+ and by FAD. Use the data given in Table 18.1 to find the E0' of the NAD+-NADH and fumarate-succinate couples, and assume that E0' for the FAD – FADH2 redox couple is nearly 0.05 V. Why is FAD rather than NAD+ the electron acceptor in the reaction catalyzed by succinate dehydrogenase?
The half-reactions involved in the lactate dehydrogenase (LDH) reaction and their standard reduction potentials are (see attached)). Calculate ΔG at pH 7.0 for the LDH-catalyzed reduction of pyruvate under the following conditions: (a) [lactate]/[pyruvate] = 1 and [NAD+]/[NADH] = 1. (b) [lactate]/[pyruvate] = 160 and [NAD+]/[NADH] = 160. (c) [lactate]/[pyruvate] = 1000 and [NAD+]/[NADH] = 1000. (d) Discuss the eff ect of the concentration ratios in Parts a–c on the direction of the reaction.
The standard reduction potential for ubiquione (A or coenzyme Q) is .045 V, and the standard reduciton potential (E) for FAD is -0.219 V. Using these values, show that the oxidation for FADH2 by ubiquinone theoretically liberates enough energy to drive the synthesis of ATP. Faraday constant =96.48KJ/Vol delta G' standard for ATP Synthesis is +30.5 KJ/mol R=8.314 J/mol K=1.987 cal/mol K
The Km and kcat for fumarase with fumarate as a substrate are 5 × 10−6 M and 8 × 102 s−1, respectively. When malate is the substrate, the Km and kcat are 2.5 × 10−5 M and 9 × 102 s−1, respectively. What do these data tell you about the operation of this enzyme in the citric acid cycle?
Given the following question, for each of the three reactions catalyzed by NADH dehydrogenase complex, identify the following1. electron donor2. electron acceptor3. the reducing agent4. the oxidizing agent
If α-ketoglutarate is removed from TCA cycle and used to make glutamate, how many of each of the cofactors (not intermediates) and high energy molecules in the TCA cycle are lost? How much ATP does this equate to (NADH = 2.5 ATP, FADH2 = 1.5 ATP)?
Under standard conditions, is the oxidation of ubiquinol (Coenzyme Q) by O2 sufficiently exergonic to drive the synthesis of ATP? If yes, how many ATP can be synthesized assuming 100% efficiency?
What is the overall net reaction for the Pyruvate Dehydrogenase Complex? What enzyme(s) in the Citric Acid Cyclecatalyze(s) substrate-level phosphorylation? What enzyme(s) in the Citric Acid Cyclecatalyze(s) decarboxylation reactions? What enzyme(s) of the Citric Acid Cyclecatalyze(s) reactions in which NAD+or FAD is reduced to NADH or FADH2, respectively?
From the complete oxidation of glucose (glucose → 6CO2), how many total NADH electron carriers are produced?
The standard free energy change for the reaction catalyzed by phosphoglucomutase is -7.1kJ/mol, (a) calculate ΔG at 37°C when the concentration of glucose-1-phosphate is 1-mM and the concentration of glucose-6-phosphate is 25-mM, (b) Is the reaction spontaneous under these conditions?
The objective of this problem is to calculate the number of moles of reduced NAD and FAD generated per one mole of glucose consumed by bacteria, growing under aerobic conditions. The consumption of glucose by the bacteria is characterized as follows: for every 1 mole of glucose consumed, 70% is completely oxidized to CO2 and H2O, while 30% of the glucose is diverted to anabolic reactions prior to pyruvate undergoing oxidative decarboxylation. For the purposes of this problem, you should assume that all pyruvate coming to the TCA cycle is completely oxidized and none is diverted to anabolic processes at the diversion points of oxaloacetate, alpha-ketoglutarate or succinyl-CoA. Calculate the NADH and FADH generated

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