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CHEN 282 – Spring 2011

Homework #2
Due Tuesday, February 15, 2011

1. The standard free energy change of reaction of ATP + H2O à ADP + Pi is -7.3
kcal/mol (25ºC, 1 atm, pH = 7.0). If the reaction started with 10 mM of ATP and
no ADP or Pi, what is the final concentration of each species (ATP, ADP, and Pi)
at equilibrium at standard conditions? The gas constant is 1.99 cal/(mol*K).

2. The ΔGo for glucose-6-phosphate à glucose + Pi is -3.1 kcal/mol.

a. Hexokinase catalyzes the first step in glycolysis (phosphorylation of
glucose – look in Lecture 5 notes). What is the overall reaction catalyzed
by hexokinase?
b. The standard free energy change for the hydrolysis of ATP is -7.3
kcal/mol. Calculate the standard free energy change (ΔGo) of the
hexokinase-catalyzed reaction.
c. What is the free energy change for the overall reaction at 25ºC if the
steady-state concentration of glucose = 0.5mM, glucose-6-phosphate =
1mM, ATP = 3mM, and ADP = 0.06mM inside the cell?

3. If the actual number of ATP that can be generated from one molecule of NADH is
2.5 and from one molecule of FADH is 1.5 via oxidative phosphorylation in E.
coli, what is the efficiency of glucose oxidation via aerobic respiration compared
to the direct oxidation of glucose (686 kcal/mol)?

4. E. coli is a facultative anaerobe, meaning it can grow with or without O2. The
presence of oxygen inhibits fermentation in E. coli. What could be the reason for
this observed phenomenon?

5. (Problem 3.3 in text) The enzyme, fumarase, has the following kinetic constants:
k1 k2
S + E # ES $ P + E
where k1 = 109 M-1 s-1
k-1 = 4.4 x 104 s-1
k2 = 103 s-1
a. What is the value of the Michaelis constant (Km) for this enzyme? Use
quasi-steady-state assumption.
b. At an enzyme concentration of 10-6 M, what will be the initial rate of
product formation at a substrate concentration of 10-3 M?
6. (Modified problem 3.6 in text) During a test of kinetics of an enzyme-catalyzed
reaction, the following data were recorded:

Eo (g/L) T (ºC) S (mmol/ml) v (mmol/ml-min)

1.6 30 0.1 2.63
1.6 30 0.033 1.92
1.6 30 0.02 1.47
1.6 30 0.01 0.96
1.6 30 0.005 0.56
1.6 49.6 0.1 5.13
1.6 49.6 0.033 3.70
1.6 49.6 0.01 1.89
1.6 49.6 0.0067 1.43
1.6 49.6 0.005 1.11

a. Using the most accurate means possible (based on what we discussed in

lecture), determine the maximum velocity of the reaction at 30ºC and
49.6ºC and an enzyme concentration of 1.6 g/L.
b. Determine the Michaelis-Menten constant for the reaction at 30ºC and