Intramitochondrial ATP concentrations are about 5 mM, and phosphateconcentration is about 10 mM. If ADP is five times more abundant thanAMP, calculate the molar concentrations of ADP and AMP at an energycharge of 0.85. Calculate AG for ATP hydrolysis at 37 °C under these condi-tions. The energy charge is the concentration of ATP plus half the concen-tration of ADP divided by the total adenine nucleotide concentration:[ATP] + 1/2[ADP][ATP] + [ADP] + [AMP]

According to the given information, the energy charge is the concentration of ATP plus half the ADP…

Answered: Intramitochondrial ATP concentrations…

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter26: Synthesis And Degradation Of Nucleotides

Section: Chapter Questions

Problem 10P

See similar textbooks

Similar questions

Intramitochondrial ATP concentrations are about 5 mM, and phosphate concentration is about 10 mM. If ADP is five times more abundant than AMP,calculate the molar concentrations of ADP and AMP at an energy charge of 0.85. Calculate ∆G for ATP hydrolysis at 37 °C under these conditions.The energy charge is the concentration of ATP plus half the concentration of ADP divided by the total adenine nucleotide concentration.
What is the smallest number of molecules of ATP and GTP consumed in the synthesis of a 200- residue protein, starting from amino acids? Assume that the hydrolysis of PP i is equivalent to the hydrolysis of ATP for this calculation.
Given the following data, calculate Keq for the denaturation reaction of the protein β-lactoglobin at 25oC: ΔH° = –88 kJ/mol ΔS° = 0.3 kJ/mol. The free energy of hydrolysis of ATP in systems free of Mg2+ is −35.7 kJ/mol. When the concentration of this ion is 5 mM, ΔG°observed is approximately −31 kJ/mol at pH 7 and 38°C. Suggest a possible reason for this effect.
If a small amount of ATP labeled with radioactive phosphorus in the terminal position, [γ-32P]ATP, is added to a yeast extract, about half of the 32P activity is found in Pi within a few minutes, but the concentration of ATP remains unchanged. Explain. If the same experiment is carried out using ATP labeled with 32P in the central position, [β-32P]ATP, the 32P does not appear inPi within such a short time. Why?
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.
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)?
The interconverison of DHAP and GAP greatly favors the formation of DHAP at equilibirum. Yet the conversion of DHAP by triose phosphate isomerase proceeds readily. Why?
Which arrestin is required for activation of phosphorylation of MDM2 during chronic Iso stimulation? use the following Figures 1and 2 respectively to explain please
Consider the complete oxidation of one mole of simple TAG containing behenic acid residues (22:0). I. For one mole of the fatty acid residue, determine the following: c. ATP yield obtained from FADH2 coming from the complete β-oxidation of the fatty acid residue d. net ATP yield of ATP in the complete oxidation of the fatty acid residue
Consider the complete oxidation of one mole of simple TAG containing behenic acid residues (22:0). I. For one mole of the fatty acid residue, determine the following: d. What is the number of net ATP yield of ATP in the complete oxidation of the fatty acid residue
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?
From the complete oxidation of glucose (glucose → 6CO2), how many total nucleotide triphosphates are yielded (be sure to deduct payback) as part of substrate level phosphorylation?

SEE MORE QUESTIONS

Recommended textbooks for you

Biochemistry

ISBN:

9781305577206

Author:

Reginald H. Garrett, Charles M. Grisham

Publisher:

Cengage Learning

Biochemistry

ISBN:

9781305577206

Author:

Reginald H. Garrett, Charles M. Grisham

Publisher:

Cengage Learning

SEE MORE TEXTBOOKS