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 The ATP cycle

14. Endergonic reactions, such as photosynthesis, proceed
glucose (C6H12O6) + 6 O2
Endergonic reactions, such
as photosynthesis, proceed
only with a net input of energy.
Cells can store energy in the
products of such reactions.
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.
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 activation energy
without enzyme
activation energy
with 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 1 2 3 4 5 6 7 89 10 11 pH
Fig. 5.11, p. 79

24. Figure 6.17 Inhibition of enzyme activity

25. X X 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, can’t
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. Excess molecules of end product bind to molecules
enzyme 2
enzyme 3
enzyme 4
enzyme 5
Excess molecules of end
product bind to molecules
of an enzyme that catalyzes
this pathway’s 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 Cooperativity

30. Figure 6.21 Organelles and structural order in metabolism