Coupled Reactions
The free energy change (G) of a reaction determines its spontaneity. A reaction is
spontaneous if G is negative (if the free energy of the products is less than the free
energy of the reactants).
Note that the standard free energy change (Go') of a reaction may be positive, for
example, and the actual free energy change (G) negative, depending on cellular
concentrations of reactants and products. Many reactions for which Go' is positive are
spontaneous because other reactions cause depletion of products or maintenance of high
substrate concentrations.
At equilibrium, G equals zero. K'eq, the ratio [C][D]/[A][B] at equilibrium, is called the
equilibrium constant. An equilibrium constant greater than one (more products than
reactants at equilibrium) indicates a spontaneous reaction (negative G°').
The variation of equilibrium constant with Go' is shown in the table below.
Keq Go' (kJ/mol) Starting with 1 M reactants and products,
the reaction:
100 = 1 0 is at equilibrium
Energy coupling
A spontaneous reaction may drive a non-spontaneous reaction.
Free energy changes of coupled reactions are additive.
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BT 403 / Thermodynamics – Unit 5 / Coupled Reactions
Coupled reaction: ATP + glucose ADP + glucose-6-P .. Go' = 17 kJoules/mol
The structure of the enzyme active site, from which water is excluded, prevents the
individual hydrolytic reactions, while favoring the coupled reaction.
R = gas constant, T =
temperature, Z = charge
on the ion, F = Faraday
constant, and =
voltage across the
membrane.
Since free energy changes are additive, the spontaneous direction for the coupled
reaction will depend on the relative magnitudes of:
G for the ion flux (G varies with the ion gradient and voltage.)
G for the chemical reaction (Go' is negative in the direction of ATP
hydrolysis. The magnitude of G depends also on concentrations of ATP, ADP,
and Pi .)
ATP has special roles in energy coupling and phosphate transfer. The free energy of
hydrolysis of phosphate from ATP is intermediate among the examples listed in the
table below. ATP can thus act as a phosphate donor, and ATP can be synthesized by
transfer of phosphate from other compounds, such as phosphoenolpyruvate (PEP).
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BT 403 / Thermodynamics – Unit 5 / Coupled Reactions
Phosphocreatine 43.1
Pyrophosphate 33.5
Glucose-6-phosphate 13.8
Glycerol-3-phosphate 9.2
A high activation energy barrier usually causes hydrolysis of a "high energy bond" to
be extremely slow in the absence of an enzyme catalyst. This "kinetic stability" is
essential to the role of ATP and other compounds with ~ bonds. If ATP would rapidly
hydrolyze in the absence of a catalyst, it could not serve its important roles in energy
metabolism and phosphate transfer. Phosphate is removed from ATP only when the
reaction is coupled to some other reaction useful to the cell, such as transport of ions or
phosphorylation of glucose.
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