5. Calculating the effect of pH on AG°ATP hydrolysis at pH 7.0 is accompanied by release of a hydrogen ion to the mediumATP4. + H20 ADP3- + HPO42- + H+If the AG" for this reaction is -30.5 kJ/mol, what is AG° (that is, the free energy change for the samereaction with all components, including H*, at a standard state of 1 M)?

ATP is commonly referred to as the "storage battery" of cells. To understand how energy is absorbed,…

Answered: 5. Calculating the effect of pH on AG°…

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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Calculate theequilibrium constant and thefree energy of (Mg)ATP hydrolysis in a closed system in which concentrations of ATP, ADP and Piare, respectively, 3.5, 1.0, and 5 mMand 25 degrees Celsius. Is the reaction spontaneous?R = 8.314 J/(deg Kelvin-mol).
Intramitochondrial ATP concentrations are about 5 mM, and phosphate concentration is about 10 mM. Consider that ADP is five times more abundant than AMP. a. Calculate the molar concentrations of ADP and AMP at an energy charge of 0.85. b. Calculate ∆G' for ATP hydrolysis under these conditions (∆G0' for ATP hydrolysis is -32.2 kJ/mol) The energy charge is defined as ( [ATP] + 1/2 [ADP] ) / ( [ATP] + [ADP] + [AMP] )
Calculate AG for the below balanced redox reaction as written. You may find a list of standard reduction potentials useful. 3 12 (s) + 2 Al (s) → 61 (aq) + 2 Al3+ (aq) O-4.24 x 102 kJ/mol O-6.48 x 102 kJ/mol O -2.12 x 102 kJ/mol O-1.27 x 103 kJ/mol O-6.37 x 102 kJ/mol
Please provide an explanation for how to work through this practice problem: Using table 12.1, calculate the free energy change for the synthesis of ATP from cAMP and inorganic phosphate. (Note: cAMP is hydolyzed to AMP, and the free engery of hydrolysis for ATP and ADP is approximately equal.) Table 12.1: (Compound: Change in Free Energy in kJ/mol) cAMP: -50.4 Creatine phosphate: -43.3 ATP: -30.5 Glucose 6-phosphate: -13.9 AMP: -9.2
24. Hexokinase catalyzes the phosphorylation of glucose from ATP, yielding glucose-6-P and ADP. The standard-state free energy change for hydrolysis of glucose-6-P is -13.9 kJ/mol. Calculate the standard-state free energy change and equilibrium constant for the hexokinase reaction. AG" for ATP hydrolysis -31.5 kJ/mol
1) Define metabolism and describe the importance of metabolism to life. 2) Calculate the change in free energy (∆G ) for the below reaction and answer the two follow up questions: Gfinal state = 3.4 kcal/ mol and Ginitial state = 10.7 kcal/ mol Recall: ∆G = Gfinal state – Ginitial state a. Is this a spontaneous or non-spontaneous reaction? Explain. b. Is there energy released from this reaction which can be used to do work? Explain. 2) List four conditions which impact an enzymes rate of activity. Explain.
Calculate ΔG° (answer in kJ/mol) for each of the following reactions from the equilibrium constant at the temperature given. (d)CoO(s)+CO(g)⇌Co(s)+CO2(g) T=550°C Kp=4.90×102 (e)CH3NH2(aq)+H2O(l)⟶CH3NH3+(aq)+OH−(aq) T=25°C Kp=4.4×10−4 (f)PbI2(s)⟶Pb2+(aq)+2I−(aq) T=25°C Kp=8.7×10
Consider a general reaction enzyme A(aq) B(aq) The AGo of the reaction is -9.150 kJ mol-. Calculate the equilibrium constant for the reaction at 25 °C. Keg = What is AG for the reaction at body temperature (37.0 °C) if the concentration of A is 1.9 M and the concentration of B is 0.50 M? 9:26 PM 35% 77°F 6/14/2021
[References) The AG" for the reaction ATP + H₂O ADP + P + H+ is -30.5 kJ mol'¹, Other organophosphate species also undergo hydrolysis of the phosphate moiety via a similar reaction. Determine the value of AG for the following reactions and indicate if the reaction will proceed spontaneously in the direction written if the reactants and products are initially in a 1:1 molar ratio. a. ATP + Glucose ADP+ Glucose-1-phosphate AG⁹¹ = kJ mol-1 The reaction is (The hydrolysis reaction for glucose-1-phosphate is Glucose-1-phosphate + H₂0 Glucose + P + H+; AG-20.9 kJ mol ¹.) b. ATP + Glutamate Carbamoyl phosphate + ADP AG The reaction is kJ mol-1 (The hydrolysis reaction for carbamoyl phosphate is Carbamoyl phosphate + H₂0 Glutamate + P, + H+ ; AG¹ = -51.4 kJ mol ¹.) Submit Answer Try Another Version 3 item attempts remaining
1. A reaction in which a substrate is converted to a product is catalyzed by an enzyme. The reaction was determined to have ket = 10,000. s', KM = 90.0 µM, and a standard Gibbs free energy change of -13.8 kJ mol. Answer the following questions about experiments performed with 2.00 nM enzyme. R= 8.3145 J mol K. !3! a) Calculate the change in free energy for this reaction at room temperature (25.0°C) under the following conditions, and indicate whether the forward reaction is favored or not. i. [(S] = 2.00 µM and [P] = 2.00 nM. !! it. [S] = 2.00 uM and (P) = 2.00 uM.
Calculating ATP Yield 'Assumes an ATP equivalence: 2.5 ATP per NADH and 1.5 ATP per FADH2. * Assumes an ATP equivalence: 3 ATP per NADH and 2 ATP per FADH2. CH3(CH,) COOH ** 1st Formula 2nd Formula Capric Acid (7 x C) - 6 (8.5 x C) -7 Carbons = 10 (7 x 10) - 6 = 64ATP (8.5 x 10) - 7 = 78ATP 1. Palmitic Acid is a saturated long-chain fatty acid with a 16-carbon backbone. It is found naturally in palm oil and palm kernel oil, as well as in butter, cheese, milk and meat. Its chemical formula is CH;(CH2)14COOH. Calculate ATP using the first formula.
You are evaluating the kinetics of an enzyme catalyzed reaction containing 5.5 μM total enzyme and 11.2 μM substrate. At this substrate concentration, you determine that the Vo = 88.6 μmol mL-¹. s-¹. If the Vmax 833.3 mM s the KM is: . == " 30.9 μΜ 10.4 μΜ Ο 124.6 μΜ 234 μΜ 94.5 μM

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