Biosc 1000

Lecture 10 Sample Problem Answers

1. If the G of the reaction of AB is -12.5 kJ/mol, what predictions can we make
about the direction of the reaction and the equilibrium?
If the free energy of the reaction of AB is -12.5kJ/mol, then the reaction is
thermodynamically favorable (because G<0). So, the reaction will proceed in
the forward direction (A B)
2. Based upon the structure of ATP, what factors contribute to its high phosphoryl
transfer potential?
Three factors contribute to the high phosphoryl transfer potential of ATP:
a. Resonance stabilization: The products of ATP hydrolysis, ADP and Pi
have more resonance structures and therefore, greater resonance stability
than ATP.
Resonance structure for Pi

Unfavorable resonance structure for ATP

b. Electrostatic repulsion: hydrolysis of ATP results in separation of the

negative charges on the phosphates, reducing the energetically
unfavorable repulsion of like charges.
c. Stabilization due to hydration: more water can for favorable electrostatic
interactions with the products ADP and Pi than just with ATP, because
more negatively charged oxygen species are exposed to water in the case
of ADP and Pi

Page 1 of 3

Biosc 1000

3. Under biologic standard conditions, the free energy of hydrolysis of L-glycerol

phosphate is -9.2 kJ/mol and for ATP hydrolysis is -30.5 kJ /mol. Show that when ATP
is used as a phosphoryl donor for the formation of L-glycerol phosphate, the value of the
equilibrium constant is altered by more that 105.
Given G= -9.2kJ/mol for hydrolysis of L-glycerol phosphate
Therefore, G = + 9.2kJ/mol for phophorylation of L-glycerol
And G= -30.5kJ/mol for hydrolysis of ATP
G= -RTlnK ; where R= 8.31 x 10-3 kJ/(mol x K) and T= 310 K
Not coupled to ATP hydrolysis:
G= -RTlnK
+9.2 = -2.58 ln K
K= e9.2/-2.58
K = e-3.56
K = 0.028 = 2.8 x 10-2
Coupled to ATP hydrolysis:
G= -RTlnK
+9.2 + (-30.5) = -2.58 lnK
K= e-21.3/-2.58
K= e8.25
K= 3849.9 = 3.8 x 103

Page 2 of 3

Biosc 1000

4. Many important reactions are driven to completion by the hydrolysis of

pyrophosphate (such as the attachment of amino acids to tRNA). Yet, the standard free
energy of hydrolysis for pyrophosphate is only -19.3 kJ/mol, a rather low value among
phosphoryl transfer agents. Why should a reaction with such a small G be used in
critically important reactions?
Hydrolysis of pyrophosphate drives a reaction to completion by removing the
product of the reaction, thus preventing accumulation of reaction product and
making ATP hydrolysis irreversible.

Page 3 of 3