1. Chapter 8 Pictures

2. Potential and Kinetic Energy

3. 2nd Law of Thermodynamics
Kinetic Energy
25% drives the pistons
75% lost as heat
Potential Energy-Fuel
*In every chemical reaction, some energy is lost as heat.

4. Theoretical metabolic pathway
Enzyme 1
Enzyme 2
Enzyme 3 A B C D
Reaction 1
Reaction 2
Reaction 3
Starting molecule
Product

6. Fig 5.2. Catabolic vs. Anabolic Reactions
Condensation → reactions (anabolic)
Hydrolysis → reactions (catabolic)

7. Catabolic Rxns – O-O O + O + Energy Anabolic Rxns- O + O + Energy O-O
Figure 8.6

8. Fig 8.14 Energy Profile for a Catabolic (Exergonic) Reaction
ALL rxns require
some input of energy
In exergonic rxns
∆G is a negative
number

9. Question 8.1 fructose + + H2O glucose Example 2: Sucrose hydrolysis
(very slow reaction)
Example 1: Baking soda
+ vinegar (fast reaction)

10. Examples of an exergonic and endergonic reaction+
Ammonia
Glutamic Acid
Glutamine
ΔG = kcal/mol +
Ammonia
Glutamic Acid
Glutamine
ΔG = kcal/mol

11. Chemical Equilibrium

12. An organism in metabolic equilibrium

13. Equilibrium
ATP

14. Metabolic Disequilibrium
Food
ATP
ATP
ATP
Waste Products

15. Fig 8.3

16. Chapter 8-ATP

17. ATP = Currency of the Cell

18. Fig 8.11

19. Fig 8.9 ATP hydrolysis

20. Fig 8.8

21. Coupled Reactions

22. Fig 8.10
ATP hydrolysis
ATP synthesis

24. Question 8.2

25. Chapter 8 - Enzymes

26. Fig 8.13. Enzyme-catalyzed reaction: hydrolysis by sucrase

27. Metabolic Map

28. Fig 8.13. Enzyme-catalyzed reaction: hydrolysis by Sucrase

29. Fig 8.14 Energy Profile Energy (heat) absorbed from Energy (heat)
the surroundings
Energy (heat)
released by
the reaction

30. Progress of the reaction
Course of
reaction
without
enzyme
Fig 8.15 Energy Profile +/- Enzyme EA
without
enzyme
EA with
enzyme
is lower
Reactants
Free energy
Course of
reaction
with enzyme
∆G is unaffected
by enzyme
Products
Progress of the reaction

32. Fig 8.17

33. Fig 8.16

34. (a) Optimal temperature for two enzymes
Fig 8.18a
Optimal temperature for
typical human enzyme
Optimal temperature for
enzyme of thermophilic
(heat-tolerant)
bacteria
Rate of reaction 20 40 80
100
Temperature (Cº)
(a) Optimal temperature for two enzymes

35. (b) Optimal pH for two enzymes
Fig 8.18b
Optimal pH for pepsin
(stomach enzyme)
Optimal pH
for trypsin
(intestinal
enzyme)
Rate of reaction 1 2 3 4 5 6 7 8 9
(b) Optimal pH for two enzymes

36. Question 8.3

37. (b) Competitive inhibition
Figure 8.19
(b) Competitive inhibition
A competitive
inhibitor mimics the
substrate, competing
for the active site.
Competitive
inhibitor
A substrate can
bind normally to the
active site of an
enzyme.
Substrate
Active site
Enzyme
(a) Normal binding
Fig 8.19 a, b

38. (c) Noncompetitive inhibition
Fig 8.19c
Figure 8.19
A noncompetitive
inhibitor binds to the
enzyme away from
the active site, altering
the conformation of
the enzyme so that its
active site no longer
functions.
Noncompetitive inhibitor
(c) Noncompetitive inhibition

39. Fig 8.21

40. Question 8.4