Chapter 11

1. The respiratory quotient is the ratio between CO 2 produced and O 2 uptake.

a. 1.33

b. 0.7

c. 0.69

d. 0.7

e. 1.0

2. a. In such reactions, which are known as futile reactions, a loss of ATP is observed.

b. This is a substrate level phosphorylation, in which PEP acts as phosphate donor.

Because NAD+-dependent enzymes usually act to dehydrogenate (oxidize) substrates, an

[NAD+]/[NADH] ratio greater than unity tends to drive reactions in that direction. Similarly,
[NADP+]/[NADPH] ratios less than unity provide concentrations that tend to drive these reactions
in the direction of substrate reduction.

3. a. 0

b. 1

c. 4

4. Negative Δ G values always indicate that the reaction is an exergonic one, and these reactions
(catabolic) are thermodynamically favored because they drive the reaction forward. However, any
exergonic reaction releases more free energy than that consumed by an unfavorable reaction. In the
above example, the reaction producing −130 kJ/mol is the biologically favorable one (see page 340
& 341).

5. ∆G = ∆G°′ + RTln([ADP][P i ]/[ATP])

= −30500 J/mol + (8.315 J/mol•K)(310 K)ln(1 × 10−3 M)(1 × 10−3 M)/(3 × 10−3 M)
= −51134 J/mol = −51.14 kJ/mol

6. a.
Treatment % Change in flux
Inhibitor that reduces activity of X by 10% 10% decrease
Activator that increases activity of X by 10% 10% increase

b. Metabolic flux rate = rate of X − rate of Y = 100 − 80 = 20 pmol/106 cells/sec in the direction
of B  →C
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Chapter 11

c.

Direction of flux
Change in flux Treatment (B → C or C  → B) % Change in flux
Inhibitor that reduces
90 − 80 = 10
activity of X by 10% B 
→C 50% decrease
Activator that increases
110 − 80 = 30
activity of X by 10% B 
→C 50% increase
Doubling the activity of 400% change
100 − 160 = −60
enzyme Y C 
→B (decrease)

d. A substrate cycle allows amplification of a small change in an enzyme’s activity;

for example, a 10% change in activity gives a 50% change in flux.

7. a.
 -DG ° '   16700J/mol 
   
=K e= e  RT   (8.315 J/mol �K)(298K) 

[ADP][glucose-6-phosphate]
= 845
=
[ATP][glucose]
Since [ATP] = [ADP]: [glucose-6-P]/[glucose] = 845 under physiological conditions.

b. K = [glucose][Pi]/[glucose-6-P] = 262
[glucose]/[glucose-6-P] = 262/(1 × 10−3 M) = 262,000

c. Any condition where the [glucose]/[glucose-6-P] ratio is between 262,000 and 0.0012 (1/845)

d. The relative concentrations of allosteric regulators that exert kinetic control over the enzymes in
the opposing pathways

8. a. Energy charge = 0.0055 + (0.5 × 0.0051)/0.0055 + 0.0051 + 0.0018 = 0.65

b. With ADP being the substrate for oxidative phosphorylation, its concentration must be relatively
high in order to maintain the ATP synthase reaction at V max or close to it.

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Chapter 11

c.  [ succinate][ ATP ][CoA − SH ] 

DG = DG° '+ RT ln  <0
 [ succinyl − CoA][ ADP ][ Pi ] 
 [ succinate][ ATP][CoA −−D SH ]  G° '
ln  <
 [ succinyl − CoA][ ADP ][ Pi ]  RT
 [0.0055][CoA − SH ]  2900
ln  <
 [0.0051][0.05]  (8.315)(298)
ln 21.6[CoA − SH ] < 1.17
21.6[CoA − SH ] < e1.17
3.223
[CoA − SH ] <
21.6
[CoA − SH ] < 0.149 M

The reaction will be exergonic at any concentration below 0.149 M.

9. The most direct way is to purify the enzyme to homogeneity and determine both its molecular
weight and turnover number. Then, from the activity observed in a crude extract, one can calculate the
number of active enzyme molecules needed to achieve that activity (assuming that the extract does not
contain inhibitors of the activity). Another approach is to treat the extract with a specific antibody to
the enzyme of interest and quantitate the protein immunoprecipitated. One still needs to know the
molecular weight to convert this value to number of molecules of enzyme.

 600 cpm/pmol 
10. a. 20%  × 100 
 3000 cpm/pmol 

b. 1500 cpm dTTP incorporated per minute per 106 cells, corrected for the 20% fraction calculated
in part (a) (1500/0.2) = 7500 cpm/106 cells/min;

7500 cpm 1pmol 6.02 × 1011 molecules

× ×
106 cells �min 3000 cpm 1pmol
= 1.5 × 106 molecules/min/cell

c. Prepare an acid extract of the cells (e.g., 5% trichloroacetic acid), separate the nucleotides by
ion-exchange HPLC, and determine in the dTTP fraction its radioactivity and its mass, the latter from
UV absorbance.

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Chapter 11

11. a. N = 1 µmol orthophosphate = 6.02 × 1017 molecules/µmol

0.693 0.693 0.693

l= = = = 3.39 ×10−−
5
min 1
t1/2 14.2 days 2.04 ×10 min
4

dN/dt = (6.02 ×1017 molecules/µmol)(3.39 ×10−−

5
min 1 )
= 2.04 ×1013 dpm/µmol
(2.04 ×1013 dpm/µmol)(1 mCi / 2.2 ×109 dpm)
= 9274 mCi /µmol

b. (10 mCi/µmol)(3.67 × 107 dps/mCi) = 3.67 × 108 dps/µmol = dN/dt = λ N

0.693 0.693 0.693

l= = = 8
= 1.8 ×109 sec −1
t1/2 12.1 years 3.8×10 sec
N = (3.67 ×108dps/µmol)/l
= (3.67 ×108dps/µmol)/(1.8 ×109 sec −1 )
= 2.04 ×1017 atoms
(1 µmol leucine)(6.02 ×1017 molecules/µmol)(13 H/molecule)
= 7.83 ×1018 H atoms (at physiological pH)
% radioactive = (100%) × (2.04 ×1017 atoms) / (7.83 ×1018 H atoms) = 2.6%

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Chapter 11

12.

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