.Wheeler and Mathews (J. Biol. Chem. 286:16992–16996, 2011) reportedthe concentrations of adenine nucleotides in rat liver mitochondria as fol-lows: ATP, 5.5 mM; ADP, 5.1 mM; AMP, 1.8 mM.(a) Calculate the adenylate energy charge within the mitochondrion[ATP] + 0.5[ADP](adenylate energy charge[ATP] + [ADP] + [AMPJ'(b) Most measurements of adenylate energy charge in whole cells orcytosol give values close to 0.9. Speculate on reasons why it might beadvantageous for mitochondria to have an ADP concentration almost ashigh as that of ATP.(c) succinyl-CoA + ADP + P¡= -2.9 kJ/molIf [P;] within the mitochondrion is 0.05 M and succinate and succinyl-CoA are present at equimolar concentrations, what is the maximumsuccinate + ATP + CoA-SH AG°'mitochondrial concentration of CoA-SH at which the reaction can beexergonic?

ATP is the energy currency of a cell. Hydrolysis of ATP is exergonic in nature and liberates a huge…

Answered: .Wheeler and Mathews (J. Biol. Chem.…

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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11. Chambers and coworkers have reported [NAD*] and [NADH] concentrations in yeast mitochondria as 20 mM and 0.3 mM, respectively. Consider the Malate Dehydrogenase reaction below: Malate + NAD* → Oxaloacetate + NADH + H* AG° = +29.7 kJ/mol If Malate concentration in yeast mitochondria is 0.4 mM what is the maximum concentration of oxaloacetate needed to make the reaction exergonic at pH 7.0 and 37°C? А. 7.14 х 105 В. 2.04 х 104 С. 8.17 х 106 D. 5.45 x 108 Е. 2.63 х 107 F. 4.69 x 108 G. 4.90 X107 Н. 3.13 х 106 I. 5.05 х 106
answer ii only
answer only question g
14) Calculate K’eq and ΔG’0 for the following: A 0.1 M solution of glucose 1-phosphate at 25oC is incubated with a catalytic amount of phosphoglucomutase, the glucose 1-phosphate is transformed to glucose 6-phosphate. At equilibrium, the concentrations of the reaction components are Glucose 1-phosphate (4.5 X 10-3 M) and Glucose 6-phosphate (9.6 X 10-2 M).
The Nutrition Facts label on most food products shows % daily values based on a food energy requirement of 8,360 kJ (2,000 kcal) at normal resting state. a) Assuming that the efficiency of converting food energy to ATP is 50%, calculate the mass of ATP (in kg) that is harvested daily by the human body from 8,360 kJ of food energy. A total of 30.5 kJ of energy is needed to synthesize one mole of ATP under standard conditions. The molar mass of ATP is 505 g/mol. b) For an average 68-kg (150 lbs.) human adult, calculate the % mass of extracted ATP (from your answer in 2a) relative to body weight.
5. Given the following information tables, determine in which cell type cleavage of the terminal phosphate from ADP yields the greatest actual change in free energy. (Please work in kJ/mol.) TABLE 13-6 Standard Free Energies of Hydrolysis of Some Phosphorylated Compounds and Acetyl-CoA (a Thioester) TABLE 13-5 Total Concentrations of Adenine Nucleotides, Inorganic Phosphate, and Phosphocreatine in Some Cells AG (kJimol) (kcalimol) Concentration (MM) Phosphoenolpyruvate 1,3-Bisphosphoglycerate (+3-phosphoglycerate + P) Phosphocreatine -61.9 -14.8 ATP ADP AMP P, PCr Rat hepatocyte Rat myocyte 49.3 -11.8 3.38 1.32 0.29 4.8 -43.0 -103 8.05 0.93 0.04 8.05 28 ADP (+ AMP + P) -32.8 -7.8 -7.3 Rat neuron 2.59 0.73 0.06 2.72 4.7 ATP (+ ADP + P) Location of -30.5 Human erythrocyte 225 0.25 0.02 1.65 ATP (+ AMP • PP) AMP (+ adenosine P) cleavage is important! 45.6 -10.9 E. coli cell 7.90 1.04 0.82 7.9 -14.2 -34 For erythrocytes the concentrations are those of the cytosol (human erythrocytes lack a…
. In another key reaction in glycolysis, dihydroxyacetone phosphate (DHAP) is isomerized into glyceraldehyde-3-phosphate (GAP) Because ∆G°′ is positive, the equilibrium lies to the left. (a) Calculate the equilibrium constant and the equilibrium fraction of GAP from the above, at 37 °C. (b) In the cell, depletion of GAP makes the reaction proceed. What will ∆G be if the concentration of GAP is always kept at 1/100 of the concentration of DHAP?
Many years later, in 1989, Wild, et al. revisited the idea of allosteric control of ATCase by CTP. They noted that CTP did indeed inhibit ATCase, but that the inhibition was always incomplete, even at high concentrations of CTP. They hypothesized that perhaps CTP did not act alone, but in combination with some other nucleotide. They tested the activity of ATCase in the presence of several nucleotide combinations. The results are shown in Table 3. a. What combination gives the most effective inhibition? b. What is the physiological significance of this combination? c. Revise Figure 1 to include this new information. d. Redraw Figure 2 to include this new information. How does the combination compare with the values for the nucleotides alone? Table 3: Relative specific activities for combinations of nucleotide effectors. A value greater than one indicates stimulation, a value less than one indicates inhibition. Nucleotide Effector ATP CTP GTP UTP ATP/CTP ATP/GTP ATP/UTP CTP/GTP CTP/UTP…

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