Figure 6.1

1
Figure 6.1  The complexity of metabolism
2
Figure 6.2 Transformations between kinetic and
potential energy
3
Figure 6.2x1 Kinetic and potential energy dam
4
Figure 6.2x2 Kinetic and potential energy
cheetah at rest and running
5
Figure 6.3  Two laws of thermodynamics
6
Figure 6.4 Order as a characteristic of life
7
Figure 6.5 The relationship of free energy to
stability, work capacity, and spontaneous change
8
Figure 6.6  Energy changes in exergonic and
endergonic reactions
9
Figure 6.7 Disequilibrium and work in closed and
open systems
10
Figure 6.8 The structure and hydrolysis of ATP
11
Figure 6.8x ATP
12
Figure 6.9  Energy coupling by phosphate transfer
13
Figure 6.10 The ATP cycle
14
glucose (C6H12O6) 6 O2
Exergonic reactions, such as aerobic respiration,
end with a net output of energy. Such
reactions help cells access energy stored in
chemical bonds of reactants.
Endergonic reactions, such as photosynthesis,
proceed only with a net input of energy. Cells
can store energy in the products of such
reactions.
energy in
energy out
6 CO2 6 H2O
Fig. 5.3, p. 74
15
Figure 6.11 Example of an enzyme-catalyzed
reaction Hydrolysis of sucrose
16
Figure 6.12 Energy profile of an exergonic
reaction
17
Figure 6.13 Enzymes lower the barrier of
activation energy
18
product glucose-6-phosphate
activation energy with enzyme
activation energy without enzyme
Energy
starting substances glucose and phosphate
Time
Fig. 5.6, p. 76
19
Figure 6.14 The induced fit between an enzyme
and its substrate
20
Enzyme Action Hexokinase
21
Figure 6.15 The catalytic cycle of an enzyme
22
Figure 6.16 Environmental factors affecting
enzyme activity
23
glycogen phosphorylase
trypsin
pepsin
Enzyme activity
7
8
9
11
1
2
3
4
5
6
10
pH
Fig. 5.11, p. 79
24
Figure 6.17 Inhibition of enzyme activity
25
allosteric activator
allosteric inhibitor
allosteric binding site vacant
enzyme active site
allosteric binding site vacant active site can
bind substrate
X
substrate cannot bind
X
active site altered, cant bind substrate
active site altered, substrate can bind
Fig. 5.8, p. 78
26
Figure 6.18 Allosteric regulation of enzyme
activity
27
Figure 6.19 Feedback inhibition
28
enzyme 3
enzyme 5
enzyme 4
enzyme 2
Excess molecules of end product bind to
molecules of an enzyme that catalyzes this
pathways first step. The greater the excess, the
more enzyme molecules are inhibited, and the
less product is synthesized.
enzyme 1
end product
substrate
Fig. 5.9, p. 78
29
Figure 6.20 Cooperativity
30
Figure 6.21 Organelles and structural order in
metabolism