11. Figure 8.2
A diver has more potential
energy on the platform
than in the water.
Diving converts
potential energy to
kinetic energy.
Climbing up converts the kinetic
energy of muscle movement
to potential energy.
A diver has less potential
energy in the water
than on the platform.
28. Figure 8.5
• More free energy (higher G)
• Less stable
• Greater work capacity
In a spontaneous change
• The free energy of the system
decreases (∆G < 0)
• The system becomes more
stable
• The released free energy can
be harnessed to do work
• Less free energy (lower G)
• More stable
• Less work capacity
(a) Gravitational motion (b) Diffusion (c) Chemical reaction
29. Figure 8.5a
• More free energy (higher G)
• Less stable
• Greater work capacity
In a spontaneous change
• The free energy of the system
decreases (∆G < 0)
• The system becomes more
stable
• The released free energy can
be harnessed to do work
• Less free energy (lower G)
• More stable
• Less work capacity
33. Figure 8.6
(a) Exergonic reaction: energy released, spontaneous
(b) Endergonic reaction: energy required, nonspontaneous
Reactants
Energy
Products
Progress of the reaction
Amount of
energy
released
(∆G < 0)
Reactants
Energy
Products
Amount of
energy
required
(∆G > 0)
Progress of the reaction
FreeenergyFreeenergy
34. Figure 8.6a
(a) Exergonic reaction: energy released, spontaneous
Reactants
Energy
Products
Progress of the reaction
Amount of
energy
released
(∆G < 0)
Freeenergy
35. Figure 8.6b
(b) Endergonic reaction: energy required, nonspontaneous
Reactants
Energy
Products
Amount of
energy
required
(∆G > 0)
Progress of the reaction
Freeenergy
37. Figure 8.7
(a) An isolated hydroelectric system
(b) An open hydro-
electric system
(c) A multistep open hydroelectric system
∆G < 0
∆G < 0
∆G < 0
∆G < 0
∆G < 0
∆G = 0
43. Figure 8.8
(a) The structure of ATP
Phosphate groups
Adenine
Ribose
Adenosine triphosphate (ATP)
Energy
Inorganic
phosphate
Adenosine diphosphate (ADP)
(b) The hydrolysis of ATP
50. Figure 8.10
Transport protein Solute
ATP
P P i
P iADP
P iADPATP
ATP
Solute transported
Vesicle Cytoskeletal track
Motor protein Protein and
vesicle moved
(b) Mechanical work: ATP binds noncovalently to motor
proteins and then is hydrolyzed.
(a) Transport work: ATP phosphorylates transport proteins.
52. Figure 8.11
Energy from
catabolism (exergonic,
energy-releasing
processes)
Energy for cellular
work (endergonic,
energy-consuming
processes)
ATP
ADP P i
H2O
63. Figure 8.15-2
Substrates
Substrates enter active site.
Enzyme-substrate
complex
Substrates are held
in active site by weak
interactions.
Active site can
lower EA and speed
up a reaction.
1
2
3
Substrates are
converted to
products.
4
Enzyme
Active
site
64. Figure 8.15-3
Substrates
Substrates enter active site.
Enzyme-substrate
complex
Enzyme
Products
Substrates are held
in active site by weak
interactions.
Active site can
lower EA and speed
up a reaction.
Active
site is
available
for two new
substrate
molecules.
Products are
released.
Substrates are
converted to
products.
1
2
3
45
6
67. Figure 8.16
Optimal temperature for
typical human enzyme (37°C)
Optimal temperature for
enzyme of thermophilic
(heat-tolerant)
bacteria (77°C)
Temperature (°C)
(a) Optimal temperature for two enzymes
RateofreactionRateofreaction
120100806040200
0 1 2 3 4 5 6 7 8 9 10
pH
(b) Optimal pH for two enzymes
Optimal pH for pepsin
(stomach
enzyme)
Optimal pH for trypsin
(intestinal
enzyme)
68. Figure 8.16a
Optimal temperature for
typical human enzyme (37°C)
Optimal temperature for
enzyme of thermophilic
(heat-tolerant)
bacteria (77°C)
Temperature (°C)
(a) Optimal temperature for two enzymes
Rateofreaction
120100806040200
69. Figure 8.16b
Rateofreaction
0 1 2 3 4 5 6 7 8 9 10
pH
(b) Optimal pH for two enzymes
Optimal pH for pepsin
(stomach
enzyme)
Optimal pH for trypsin
(intestinal
enzyme)
74. Figure 8.18
Two changed amino acids were
found near the active site.
Active site
Two changed amino acids
were found in the active site.
Two changed amino acids
were found on the surface.
78. Figure 8.19
Regulatory
site (one
of four)
(a) Allosteric activators and inhibitors
Allosteric enzyme
with four subunits
Active site
(one of four)
Active form
Activator
Stabilized active form
Oscillation
Non-
functional
active site
Inactive form
Inhibitor
Stabilized inactive
form
Inactive form
Substrate
Stabilized active
form
(b) Cooperativity: another type of allosteric activation
79. Figure 8.19a
Regulatory site
(one of four)
(a) Allosteric activators and inhibitors
Allosteric enzyme
with four subunits
Active site
(one of four)
Active form
Activator
Stabilized active form
Oscillation
Nonfunctional
active site
Inactive form
Inhibitor
Stabilized inactive form
83. Figure 8.20
Caspase 1 Active
site
Substrate
SH SH
SH
Known active form Active form can
bind substrate
Allosteric
binding site
Allosteric
inhibitor
Hypothesis: allosteric
inhibitor locks enzyme
in inactive form
Caspase 1
Active form Allosterically
inhibited form
Inhibitor
Inactive form
EXPERIMENT
RESULTS
Known inactive form
84. Figure 8.20a
Caspase 1 Active
site
Substrate
SH SH
SH
Known active form Active form can
bind substrate
Allosteric
binding site
Allosteric
inhibitor
Hypothesis: allosteric
inhibitor locks enzyme
in inactive form
EXPERIMENT
Known inactive form
87. Figure 8.21
Active site
available
Isoleucine
used up by
cell
Feedback
inhibition
Active site of
enzyme 1 is
no longer able
to catalyze the
conversion
of threonine to
intermediate A;
pathway is
switched off. Isoleucine
binds to
allosteric
site.
Initial
substrate
(threonine)
Threonine
in active site
Enzyme 1
(threonine
deaminase)
Intermediate A
Intermediate B
Intermediate C
Intermediate D
Enzyme 2
Enzyme 3
Enzyme 4
Enzyme 5
End product
(isoleucine)
89. Figure 8.22
Mitochondria
The matrix contains
enzymes in solution that
are involved in one stage
of cellular respiration.
Enzymes for another
stage of cellular
respiration are
embedded in the
inner membrane.
1 µm