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General Biology (Group 8) How The Hydrolysis of ATP Perform Work ATP Hydrolysis

1) ATP hydrolysis releases chemical energy stored in ATP through the breakdown of its phosphoanhydride bonds, producing ADP, Pi, and energy. This energy is then used to do mechanical work like muscle contraction. 2) The hydrolysis of ATP is exergonic due to the stabilization of products and relief of electrostatic repulsions, releasing enough energy (-28 to -34 kJ/mol under standard conditions) to power biochemical reactions. 3) In human cells, the actual free energy change for ATP hydrolysis is much greater than standard conditions due to non-equilibrium concentrations, producing -64 to -69 kJ/mol of energy to fuel cellular work.

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55 views2 pages

General Biology (Group 8) How The Hydrolysis of ATP Perform Work ATP Hydrolysis

1) ATP hydrolysis releases chemical energy stored in ATP through the breakdown of its phosphoanhydride bonds, producing ADP, Pi, and energy. This energy is then used to do mechanical work like muscle contraction. 2) The hydrolysis of ATP is exergonic due to the stabilization of products and relief of electrostatic repulsions, releasing enough energy (-28 to -34 kJ/mol under standard conditions) to power biochemical reactions. 3) In human cells, the actual free energy change for ATP hydrolysis is much greater than standard conditions due to non-equilibrium concentrations, producing -64 to -69 kJ/mol of energy to fuel cellular work.

Uploaded by

Claire M
Copyright
© © All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
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General Biology ( Group 8 )

How the hydrolysis of ATP perform work

ATP hydrolysis

is the catabolic reaction process by which chemical energy that has


been stored in the high-energy phosphoanhydride bonds in adenosine
triphosphate (ATP) is released by splitting these bonds, for example in muscles,
by producing work in the form of mechanical energy. The product is adenosine
diphosphate(ADP) and an inorganic phosphate, orthophosphate (Pi). ADP can
be further hydrolyzed to give energy, adenosine monophosphate (AMP), and
another orthophosphate (Pi) ATP hydrolysis is the final link between the energy
derived from food or sunlight and useful work such as muscle contraction, the
establishment of electrochemical gradients across membranes, and
biosynthetic processes necessary to maintain life.
The description and typical textbook labeling anhydridic bonds as "high
energy . . bonds" can be very misleading to students. These bonds are in fact
relatively weak. They do involve high energy electrons but the bonds themselves
are quite easy to break. As noted below, energy is released by the hydrolysis of
ATP when these weak bonds are broken – requiring a small input of energy,
followed by the formation of new bonds and the release of a larger amount of
energy as the total energy of the system is lowered and becomes more stable.
Hydrolysis of the phosphate groups in ATP is especially exergonic, because
the resulting orthophosphate group is greatly stabilized by multiple resonance
structures, making the products (ADP and Pi) much lower in energy than the
reactant (ATP). The high negative charge density associated with the three
adjacent phosphate units of ATP also destabilizes the molecule, making it higher
in energy. Hydrolysis relieves some of these electrostatic repulsions, liberating
useful energy in the process by causing conformational changes in enzyme
structure.
In humans, approximately 60 percent of the energy released from the
hydrolysis of one mole of ATP produces metabolic heat rather than fuel the
actual reactions taking place. Due to the acid-base properties of ATP, ADP, and
inorganic phosphate, the hydrolysis of ATP has the effect of lowering the pH of
the reaction medium. Under certain conditions, high levels of ATP hydrolysis can
contribute to lactic acidosis.

How much energy ATP hydrolysis produces


Hydrolysis of the terminal phosphoanhydridic bond is a highly exergonic
process. The amount of released energy depends on the conditions in a
particular cell. Specifically, the energy released is dependent on concentrations
of ATP, ADP and Pi. As the concentrations of these molecules deviate from
values at equilibrium, the value of Gibbs free energy change (ΔG) will be
increasingly different. In standard conditions ( ATP, ADP and Pi concentrations
are equal to 1M, water concentration is equal to 55M) the value of ΔG is
between -28 to -34 kJ/mol.
The range of the ΔG value exists because this reaction is dependent on
the concentration of Mg2+ cations, which stabilize the ATP molecule. The cellular
environment also contributes to differences in the ΔG value since ATP hydrolysis
is dependent not only on the studied cell, but also on the surrounding tissue and
even the compartment within the cell. Variability in the ΔG values is therefore to
be expected.
The relationship between Gibbs free energy and chemical equilibrium is
revealing. This relationship is defined by the equation ΔG=-RTln(Keq). The
standard value of ΔG for this reaction is, as mentioned, between -28 and -34
kJ/mol; however, experimentally determined concentrations of the involved
molecules reveal that the reaction is not at equilibrium. Given this fact, a
comparison between the equilibrium constant, K, and the reaction quotient, Q,
provides insight. K takes into consideration reactions taking place in standard
conditions, but in the cellular environment the concentrations of the involved
molecules (namely, ATP, ADP, and Pi) are far from the standard 1M. In fact, the
concentrations are more appropriately measured in mM, which is smaller than
M by three orders of magnitude. Using these nonstandard concentrations, the
calculated value of Q is much less than one. By relating Q to ΔG using the
equation ΔG=ΔG0+RTln(Q), where ΔG0 is the standard change in Gibbs free
energy for the hydrolysis of ATP, the magnitude of ΔG is much greater than the
standard. The nonstandard conditions of the cell actually result in a more
favorable reaction.
In one particular study, to determine the ΔG in vivo in humans, the
concentration of ATP, ADP, and Pi was measured using nuclear magnetic
resonance. In human muscle cells at rest, the concentration of ATP was found to
be around 4 mM and the concentration of ADP was around 9 μM. Inputing
these values into the above equations yields the -64 kJ/mol ΔG. After ischemia,
when the muscle is recovering from exercise, the concentration of ATP is as low
as 1 mM and the concentration of ADP is around 7 μmol/l. Therefore, the
absolute ΔG would be as high as -69 kJ/mol.
By comparing the standard value of ΔG and the experimental value of
ΔG, one can see that the energy released from the hydrolysis of ATP, as
measured in humans, is almost twice as much as the energy produced in
standard conditions.

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