answer ii only (i)Calculate the physiological AG (not AG.') for the reaction:Phosphocreatine + ADP creatine + ATPGiven;Phosphocreatine + H20 → creatine + PiADP + Pi → ATP + H:0AG,' = -43 kJ/molAG.' =+30.5 kJ/molat 25°C as it occurs in the cytosol of neurons, in which phosphocreatine is present at4.7 mM, creatine at 1.0 mM, ADP at 0.20 mM, and ATP at 2.6 mM.(R= 8.315 JK' mol"')(ii)Calculate the free energy change at standard conditions for the following reaction:Acetaldehyde + NADH + H* + Ethanol + NADThe half- reactions are:Acetaldehyde + 2H + 2e + EthanolNAD + 2H + 2e +E"= - 0.20VNADH + H-E°"= - 0.32V(F= 96.485 kJ/V/mol)

Answer - Half reactions Acetaldehyde+2H+ + 2e- → Ethanol (E=-0.20V ) NAD+ 2H++ 2e_ →NADH + H+ (E=…

Answered: (ii) Calculate the free energy change…

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter18: Glycolysis

Section: Chapter Questions

Problem 17P

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In considering active transport by Na + -K + -ATPase at body temperature (37 o C), 3 Na+ are pumped out of the cell and 2 K + are pumped in for each ATP that is hydrolyzed to ADP + P i . Given that underyour experimental conditions, the DG for ATP hydrolysis is -10 kcal/mol, and that V is -60 mV, and that the pump maintains the internal Na + at 10mM, external Na + at 120 mM, internal K + at 120 mM and external K + at 8mM, what is the efficiency of the pump (i.e., what fraction of the energy available from ATP hydrolysis is required to drive transport at the provided levels)?
1. a. Calculate the physiological DG of the reaction shown below at 37°C, as it occurs in the cytosol ofneurons, with phosphocreatine at 4.7 mM, creatine at 1.0 mM, ADP at 0.73 mM, and ATP at 2.6mM. The standard free energy change for the overall reaction is –12.5 kJ/mol. Phosphocreatine + ADP ® creatine + ATP b. The enzyme phosphoglucomutase catalyzes the conversion of glucose 1-phosphate to glucose6-phosphate. Calculate the standard free energy change of this reaction if incubation of 20 mMglucose 1-phosphate (no glucose-6 phosphate initially present) yields a final equilibrium mixtureof 1.0 mM glucose 1-phosphate and 19 mM glucose 6-phosphate at 25°C and pH 7.0. c. If the rate of a nonenzymatic reaction is 1.2 x 10–2 μM s–1, what is the rate of the reaction at 37℃ inthe presence of an enzyme that reduces the activation energy by 30.5 kJ/mol?
If intracellular [ATP] = 5 mM, [ADP] = 0.5 mM, and [Pi] = 1.0 mM, calculate the concentration of AMP at pH 7 and 25°C under the condition that the adenylate kinase reaction is at equilibrium.
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Calculate the actual, physiological ΔG for the reaction at 37 °C, as it occurs in the cytosol of neurons, with phosphocreatine at 4.7 mM, creatine at 1.0 mM, ADP at 0.73 mM, and ATP at 2.6 mM.
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In a rat cardiomyocyte, the levels of creatine, phosphocreatine, and free phosphate were found to be 37.6mM, 40.3mM, and 8.02mM, respectively. Given that the standard free energy change is –43.0 kJ/mol, what is the true free energy change for phosphocreatine hydrolysis in the cardiomyocyte described above?
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(ii) Calculate the free energy change at standard conditions for the following reaction: Acetaldehyde + NADH + H* + Ethanol + NAD The half- reactions are: Acetaldehyde + 2H + 2e Ethanol NAD + 2H + 2e - NADH + H- E"= - 0.20V E"= - 0.32V (F= 96.485 kJ/V/mol)