QUESTION 2ADPAG"=-18.9 kJ/mol1,3-Bisphosphoglycerate → 3-PhosphoglycerateNormal free energy of the shown step of glycolysis coupled with synthesis of one molecule of ATP is -18.9 kJ/mol. Calculate AG" (in kJ/mol) of dephosphorylation of1,3-Biphosphoglycerate if AG"¹ of synthesis of ATP from ADP is 1.75.ATP AG" = 1.75 kJ/mol

Free energy change for biochemical reaction is given by ΔG°' = -R T ln Keq , where Keq is the…

Answered: QUESTION 2 ADP ATP AG"= 1.75 kJ/mol…

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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Question 1: The standard reduction potential for the the cytochrome c Fe3+/Fe2+ redox couple and for the dioxygen/water redox couple. Part a: Use these values, and the relevant equation, to compute the standard free energy change for the transfer of 4 electrons from cytochrome c to dioxygen. Part b: Next, compute the free energy needed to pump four protons across the mitochondrial membrane, using the relevant equation and values of -.14V for Δψ and 1.4 for ΔpH. Part c: If energy conservation by cytochrome c oxidase involved only the four pumped protons (and standard conditions applied), what would be the efficiency of energy conservation at this step? (what is the ratio [energy conserved in the gradient] / [redox energy used] ?)
Question:- 33) Glucose-6-phosphate has different pathways that it can enter in the liver during the fed state. All of the following are possible except OA.) it is oxidized to acetyl CoA for fatty acid biosynthesis O B). it can enter the pathway for glycogen biosynthesis O c.) it is a substrate for glucose-6-phosphatase OD. )it is oxidized in glycolysis to provide energy for the body
Question 1: In some microorganisms, carbon fixation occurs by reversal of the citric acid cycle. This reversal is accomplished in part by the use of a strong reductant (ferredoxin) to drive the alpha-ketoglutarate dehydrogenase reaction in the reductive direction. Part a: ΔG°‘ for reaction as it occurs in the ‘normal’ (oxidative) citric acid cycle is -30.1 kJ/mol. The standard reduction potential for NADH is -0.32 V. In order to drive the reaction in the reverse direction, the reductant (a ferredoxin) must have a lower reduction potential than NADH/NAD+. Remembering that this is a two-electron reduction, and using the numbers given just above, compute the value of the ferredoxin reduction potential that would be needed to make the standard free energy zero (so that the reductive reaction is enegetically just as favorable as the oxidative reaction). Assume that all of the other reactants are the same in the reductive as in the oxidative reaction. Write out the steps in your calculation;…
Question 1: ATP synthases contains 3 copies of each of the large subunits (called α and β in the E. coli enzyme). The number of c subunits can vary among different ATP synthases, ranging from 8 to 17. Part a: Briefly explain how this variation in the number of c subunits would affect the energetics of ATP synthesis. For a fixed value of the protonmotive force, how much energy can the gradient provide to drive one revolution of the ATP synthase, in a synthase with 8 c- subunits versus a synthase with 17 c-subunits?
QUESTION 26 During gluconeogenesis, whereby liver cells convert pyruvate to glucose, Fructose-6-phosphate (F6P) is converted to Glucose-6-phosphate (G6P). If the standard equilibrium concentrations are: [F6P] = 0.52 M and [G6P] = 1.48 M, then Keq’ is ______ and the reaction is ________. Fructose-6-P ó Glucose-6-P > 1; exergonic > 1; endergonic < 1; exergonic < 1; endergonic
Question 1: The 4 kinase steps in glycolysis are catalyzed by hexokinase, phosphofructokinase, phosphoglycerate kinase, and pyruvate kinase. Write each of these four reactions, including all participants. i. ii. iii. iv.
Question 1: Part a: Assume that the standard free energy of ATP hydrolysis is -31 kJ/mol. Assume the following values for the standard free energy changes of the four reactions: HK -16.7 kJ/mol; PFK -14.2 kJ/mol; PGK -18.9 kJ/mol; PK -31.7 kJ/mol. (from bio.libretexts.org). Use these values to compute the standard free energy of hydrolysis (releasing Pi) of i. glucose 6-P ii. fructose 1,6-bis-P iii. 1,3-bisphosphoglycerate iv. phosphoenolpyruvate Part b: Which of these four compounds is the strongest phosphoryl donor?______________ Which is the weakest?__________________ Part c: The phosphoglycerate kinase reaction is favorable by -18.9 kJ/mol in the glycolytic direction, as stated above. In gluconeogenesis, this step is simply reversed; i.e. it is not one of the three steps in gluconeogenesis that is driven by using different chemistry than that of glycolysis. How can this be? (Be specific: what specific factors could enable reversal of this step?)
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QUESTION 22 When the final product of a series of enzymatically-catalyzed reactions binds to the first enzyme in the pathway to limit its production, it generally uses ___ because the structure of this final product is generally not similar to that of any of the enzyme's normal substrates. Allosteric activation Zymogen activation Covalent modification Competitive inhibition Allosteric inhibition
Question:- ATP is an important source of energy for muscle contraction. Pyruvate dehydrogenase phosphate phosphatase is activated by calcium, which increases greatly in concentration during exercise. Why is activation of the phosphatase consistent with the metabolic requirements of muscle during contraction?

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