a) (1)Calculate the physiological AG (not AG.) for the reaction:Phosphocreatine + ADP - creatine + ATPGiven;Phosphocreatine + H;0 - 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)Caleulate the free energy change at standard conditions for the following reaction:Acetaldehyde + NADH + H* + Ethanol + NAD*The half- reactions are:Acetaldehyde + 2H + 2e +EthanolE°- - 0.20VNAD-+ 2H- + 2e ++NADH + H-E=-0.32V(F= 96.485 kJ/V/mol)

A system's free energy is equal to the sum of its enthalpy (H) and the product of its temperature…

Answered: (i) Calculate the physiological AG (not…

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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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?
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)?
Neutral sphingomyelinase 2 converts sphingomyelin into ceramide and phosphorcholine. What kind of enzyme is it? Assume Vmax is 35 µM min-1. When you provide 3.0 x 10-5 M of sphingomyelin, you observe an initial velocity of 6.0 µM min-1. Calculate the KM.
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.
Which arrestin is required for activation of phosphorylation of MDM2 during chronic Iso stimulation? use the following Figures 1and 2 respectively to explain please
A.What is the Result of the sodium potassium ATPase activity in the cell? B.What mechanism does the sodium potassium ATPase use to achieve this result? C. Why is the above-mentioned change in affinity critical for the sodium potassium ATPase to perform its function?
How many net ATP are produced from the complete oxidation of one molecule of 1,3-bisphosphoglycerate (1,3 BPG) in a neuron?
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?
If instead of using 3.5 µM myoglobin (receptor) you used half of this (that is, 1.75 µM myoglobin), what would be that value of the Kd, that you calculated ( how would it change)? Please explain so I can solve on my own :) (How does changing concentration of the receptor in a ligand-receptor binding experiment affect the dissociation constant?)
The phosphoryl group transfer potentials for glucose-1-phosphate and glucose-6-phosphate are 20.9 kJ/mol and 13.8 kJ/mol, respectively. (a) What is the equilibrium constant for the reaction shown below at 25 °C? (b) If a mixture was prepared containing 1 m glucose-6-phosphate and 1 x 10-3 M glucose-1-phosphate, what would be the thermodynamically favored direction for the reaction?
A bacterial enzyme catalyzes the hydrolysis of maltose as shown in the reaction given below: Maltose + H2O -> 2 glucose If the reaction has a Km of 0.135 mM and a V max of 65 m mol/min. What is the reaction velocity when the concentration of maltose is 1.0 mM?
The standard free energy change for the reaction catalyzed by phosphoglucomutase is -7.1kJ/mol, (a) calculate ΔG at 37°C when the concentration of glucose-1-phosphate is 1-mM and the concentration of glucose-6-phosphate is 25-mM, (b) Is the reaction spontaneous under these conditions?

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