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

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

Problem 1P

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The diagram on the right compares the O2 uptake activity of mitochondria isolated from cultures of (wt) STHdhQ7/Q7 and mutant STHDHQ111/Q111 striatal neuronal progenitor cells, as introduced in Question 1. Panels A and B be- long to wt mitochondria and Panels C and D be- long to HD mitochondria. The isotonic medium was buffered to pH 7.4 with inorganic phosphate. Respiration is supported initially by addition of py- ruvate (+ malate) at t = 0, followed by additions of ADP (sufficient to consume all of the O2 in the incubation medium), R (rotenone), S (succinate), and O (oligomycin). For Panels A and C, Ca2+ had been added to a concentration of 0.9 µM, Ca2+ 2. B A WT 400 ADP ADP 450 300 - 300 200 Ca2 10 uM 150 100 - C HD 400 ADP R ADP R SO 450 300 - V s Ca2 10 uM 300 200 - 150 100 - while for mitochondria in Panels B and D, had been added to the medium to a final concen- Time 20 min tration of 10 µM, sufficient to require translocation into the mitochondrial matrix by the Ca2+…
How many ATP molecules can be generated from one mol of 14CH3-COOH? (The conversion of acetate to acetyl-CoA requires the consumption of 2 ATP.)
Why does FAHD2 oxidation give 1.5 ATP while NADH oxidation gives 2.5 ATP? Explain this in relation to ETC.
Which of the reactions are spontaneous (favorable)? C6H130,P + ATP → › C6H14º₁₂P2 + ADP AG = -14.2 kJ/mol L-malate + NAD+ → oxaloacetate + NADH + H+ AG = 29.7 kJ/mol glutamate + NAD+ + H₂O → NH‡ + α-ketoglutarate + NADH + H+ AG = 3.7 kcal/mol → CH2O4 + H2O AG = 3.1 kJ/mol * CąHẠO, — CH,O4 + H,O DHAP C₂H + H₂ glyceraldehyde-3-phosphate AG = 3.8 kJ/mol Rh(I) C2H6 AG-150.97 kJ/mol
For lactate dehydrogenase reaction if km for NADH is 2×10^-4 M . What concentration of it would be appropriate for determining Km for pyruvate?
The muscle isozyme of lactate dehydrogenase is inhibited by lactate. Steady-state kinetic analysis yielded the following data, with lactate either absent or present at a fixed concentration. (a) Pyruvate is the substrate whose concentration is varied in one plot,NADH in the other. Identify each. Use an arrow and the appropriate letter(b, c, d, or e) to identify each of the following.(b) Reciprocal of Vmax for the uninhibited enzyme.(c) The line representing data obtained in the presence of lactate acting as a competitive inhibitor with respect to the variable substrate.(d) The line representing data obtained in the presence of lactate acting as a noncompetitive inhibitor with respect to the variable substrate.(e) Reciprocal of KM in the presence of lactate acting as a competitiveinhibitor.(f) If KM for NADH is 2 x 10-5 M, then which of the following is the mostappropriate NADH concentration to use when determining KM for pyruvate: 10-7 M, 10-6 M, 10-5 M, 10-4 M, or 10-3 M?
Refer to Table to explain why FAD rather than NAD+ is used in the succinate dehydrogenase reaction.
Pyruvate carboxylase catalyzes the first step of gluconeogenesis. ATP + HCO3─ + pyruvate → oxaloacetate + ADP + Pi ∆G0’ = ─2.1 kJ mol-1 a) Calculate ΔG for this reaction under the following physiological conditions: 370C, pH 7 [pyruvate] = [HCO3─] = 4.0 mM [oxaloacetate]= 2.0 mM [ATP] = 3.5 mM [Pi] = 5.0 mM [ADP] = 1.8 mM
ATP, like ADP and AMP, is a competitive inhibitor of NADH binding to malate dehydrogenase. Provide a structural explanation for this inhibition.
A dialyzed pigeon liver extract will catalyze the conversion of acetyl-CoAto palmitate and CoASH if supplied with Mg2+, NADPH, ATP, HCO3-, andcitrate.(a) If H14CO3– is supplied, what compounds will become labeled (permanently or transiently) during the course of the reaction? In whatcompounds will 14C accumulate?(b) Explain the role of citrate in this reaction.
Lactate dehydrogenase is one of the many enzymes that require NADH as coenzyme. It catalyzes the conversion of pyruvate to lactate:Draw the mechanism of this reaction (show electron-pushing arrows). (Hint: This is a common reaction throughout metabolism; the mechanism is similar to that catalyzed by other dehydrogenases that use NADH, such as alcohol dehydrogenase.)
Consider 3 molecules of galactose: (write only the whole number; no decimal places) How many turns of Krebs Cycle will these molecules undergo for complete oxidation? b. How many moles of ATP are produced upon complete oxidation via malate-aspartate shuttle? c. If all the galactose molecules oxidize via pentose phosphate pathway (oxidative stage only), how many moles of NADPH will be produced?

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