Biochemistry: Concepts and Connections (2nd Edition)
2nd Edition
ISBN: 9780134641621
Author: Dean R. Appling, Spencer J. Anthony-Cahill, Christopher K. Mathews
Publisher: PEARSON
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Chapter 14, Problem 7P
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 ΔG for ATP hydrolysis at 37oC under these conditions. The energy charge is the concentration of ATP plus half the concentration of ADP divided by the total adenine
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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.
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] )
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?
Chapter 14 Solutions
Biochemistry: Concepts and Connections (2nd Edition)
Ch. 14 - Prob. 1PCh. 14 - When pure reduced cytochrome c is added to...Ch. 14 - Freshly prepared mitochondria were incubated with...Ch. 14 - Prob. 4PCh. 14 - Prob. 5PCh. 14 - Prob. 6PCh. 14 - Intramitochondrial ATP concentrations are about 5...Ch. 14 - Prob. 8PCh. 14 - Prob. 9PCh. 14 - Years ago there was interest in using uncouplers...
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- The enzyme mutase which is important for the synthetic of tyrosine and phenylalanine in saccharomyces cerevisiae has been studied as an example of an allosteric enzyme. Tyrosine acts as a negative effector for this enzyme. What effects would you see on the action of the enzyme were you to increase the concentration of tyrosine? The chorismate mutase would shift to its R conformation The curve showing the kinetics or chorismate mutase would shift to the right The curve showing the kinetics of chorismate mutase would shift to the left The chorismate mutase would become saturated more rapidlyarrow_forwardIn the following situations, what is the free energy change if 1 mole of Na+is transported across a membrane from a region where the concentration is1 μM to a region where it is 100 mM?(Assume T = 37 °C.) (a) In the absence of a membrane potential. (b) When the transport is opposed by a membrane potential of 70 mV. (c) In each case, will hydrolysis of 1 mole of ATP suffice to drive the transport of 1 mole of ion, assuming pH 7.4 and the following cytoplasmic concentrations: ATP = 4.60 mM, Pi = 5.10 mM, ADP = 310 μM?arrow_forwardA.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?arrow_forward
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