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Key Concepts
8.1 An organisms metabolism transforms matter and energy, subject to the laws of
thermodynamics
8.2 The free-energy change of a reaction tells us whether the reaction occurs
spontaneously
8.3 ATP powers cellular work by coupling exergonic reactions to endergonic reactions
8.4 Enzymes speed up metabolic reactions by lowering energy barriers
8.5 Regulation of enzyme activity helps control metabolism
Interactive Question 8.1
a. capacity to cause change
b. kinetic
c. motion
d. potential
e. position
f. conserved
g. created nor destroyed
h. first
i. transformed or transferred
j. entropy
k. second
Interactive Question 8.2
Complete the table to show how the free energy of a system or reaction relates to its
stability, tendency for spontaneous change, equilibrium, and capacity to do work.
Stability
Spontaneous
Equilibrium
Work capacity
Free energy
Measure of determined by
Energy available to do work
G = H - TS
G is
H is
T is
S is
free energy
change in total
absolute
change
available
energy of system
temperature
in
to do work
entropy
when
when
measure of
G is negative
G is positive
disorder or
usually
reaction is
randomness
decrease in H, reaction is
endergonic
increase in S
spontaneous
exergonic
Interactive Question 8.4
Label the three components (a through c) of the ATP molecule shown below.
a. adenine
b. ribose
c. 3 phosphate groups
d. Indicate which bond is likely to break. By what chemical mechanism is the bond
broken?
A hydrolysis reaction breaks the terminal phosphate bond and releases a molecule
of inorganic phosphate: ATP + H2O ADP + Pi
e. Explain why this reaction releases so much energy?
The negatively charged phosphate groups are crowded together, and their mutual
repulsion makes this area instable. The chemical change to a more stable state of
lower free energy accounts for the relatively high release of energy.
Interactive Question 8.5
In this graph of an exergonic reaction with and without an enzyme catalyst, label the parts
a through e.
a. free energy
b. transition state
c. EA (free energy of activation) without enzyme
d. EA with enzyme
e. G of the reaction
Interactive Question 8.6
Outline a catalytic cycle using the diagrammatic enzyme below. Sketch two appropriate
substrate molecules and two products, identify the enzyme-substrate complex, and
describe the key steps of the cycle. (see pg. 153)
11. At equilibrium,
b. free energy is at a minimum (147)
12. In cooperativity,
c. a molecule bound to the active site f one subunit of an enzyme affects
the active site of other subunits (157)
13. When a cell breaks down glucose, only about 40% of the energy is captured in
ATP molecules. The remaining 60% of the energy is
b. lost as heat because of the second law of thermodynamics (149)
14. An endergonic reaction could be described as one that will
b. produce products with more free energy than the reactants (146)
15. What is most directly responsible for the specificity of a protein enzyme?
e. the R groups of the amino acids in its active site (158)
16. Which of the following parameters does an enzyme raise?
d. speed of reaction (150)
17. Zinc, an essential trace element, may be found bound to the active site of some
enzymes. What would be the most likely function of such zinc ions?
b. a cofactor necessary for catalysis (155)
18. Which line in the diagram above indicates the G of the enzyme-catalyzed
reaction of L M + N?
D (152)
19. Which line in the diagram indicates the activation energy of the noncatalyzed
reaction?
C (152)
20. Which of the following terms would best describe this reaction?
b. -G (152)
21. A reaction that is spontaneous
e. is exergonic (146)
22. In the metabolic pathway, ABCDE, what effect would molecule E likely
have on the enzyme that catalyzes AB?
a. allosteric inhibitor (156)
Fill in the Blanks
1. the totality of an organisms chemical processes (metabolism)
2. pathways that require energy to combine molecules together (anabolic)
3. the energy of motion (kinetic)
4. enzymes that change between two conformations, depending on whether an
activator or inhibitor is bound to them (allosteric)
5. term for the measure of disorder or randomness (entropy)
6. the energy that must be absorbed by molecules to reach the transition state (free
energy of activation)
7. inhibitors that decrease an enzymes activity by binding to the active site
(competitive inhibition)
8. organic molecules that bind to enzymes and are necessary for their functioning
(coenymes)
9. regulatory device in which he product of a pathway binds to an enzyme early in
the pathway (feedback inhibition)
10. more reactive molecules created by the transfer of a phosphate group from ATP
(phosphorylated intermediate)