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
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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
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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.