1. An Introduction to Metabolism6
An Introduction to Metabolism

2. Overview: The Energy of Life
The living cell is a miniature chemical factory where thousands of reactions occur
The cell extracts energy and applies energy to perform work
Some organisms even convert energy to light, as in bioluminescence
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3. Figure 6.1
Figure 6.1 What causes these two squid to glow? 3

4. Concept 6.1: An organism’s metabolism transforms matter and energy
Metabolism is the totality of an organism’s chemical reactions
Metabolism is an emergent property of life that arises from interactions between molecules within the cell
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5. Metabolic Pathways
A metabolic pathway begins with a specific molecule and ends with a product
Each step is catalyzed by a specific enzyme
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6. Enzyme 1 Enzyme 2 Enzyme 3 Starting molecule A B C D Product
Figure 6.UN01
Enzyme 1
Enzyme 2
Enzyme 3
Starting
molecule A B C D
Product
Reaction 1
Reaction 2
Reaction 3
Figure 6.UN01 In-text figure, metabolic pathway schematic, p. 116 6

7. Catabolic pathways release energy by breaking down complex molecules into simpler compounds
Cellular respiration, the breakdown of glucose in the presence of oxygen, is an example of a pathway of catabolism
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8. The synthesis of protein from amino acids is an example of anabolism
Anabolic pathways consume energy to build complex molecules from simpler ones
The synthesis of protein from amino acids is an example of anabolism
Bioenergetics is the study of how organisms manage their energy resources
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9. Forms of Energy Energy is the capacity to cause change
Energy exists in various forms, some of which can perform work
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10. Kinetic energy is energy associated with motion
Thermal energy is kinetic energy associated with random movement of atoms or molecules
Heat is thermal energy in transfer from one object to another
Potential energy is energy that matter possesses because of its location or structure
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11. Energy can be converted from one form to another
Chemical energy is potential energy available for release in a chemical reaction
Energy can be converted from one form to another
Animation: Energy Concepts
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12. A diver has more potential energy on the platform.
Figure 6.2
Diving converts
potential energy to
kinetic energy.
A diver has more potential
energy on the platform.
Figure 6.2 Transformations between potential and kinetic energy
Climbing up converts the kinetic
energy of muscle movement
to potential energy.
A diver has less potential
energy in the water. 12

13. The Laws of Energy Transformation
Thermodynamics is the study of energy transformations
An isolated system, such as that approximated by liquid in a thermos, is isolated from its surroundings
In an open system, energy and matter can be transferred between the system and its surroundings
Organisms are open systems
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14. The First Law of Thermodynamics
According to the first law of thermodynamics, the energy of the universe is constant
Energy can be transferred and transformed, but it cannot be created or destroyed
The first law is also called the principle of conservation of energy
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15. (a) First law of thermodynamics (b) Second law of thermodynamics
Figure 6.3
Heat
Chemical
energy
Figure 6.3 The two laws of thermodynamics
(a) First law of thermodynamics
(b) Second law of thermodynamics 15

16. (a) First law of thermodynamics
Figure 6.3a
Chemical
energy
Figure 6.3a The two laws of thermodynamics (part 1: conservation of energy)
(a) First law of thermodynamics 16

17. (b) Second law of thermodynamics
Figure 6.3b
Heat
Figure 6.3b The two laws of thermodynamics (part 2: entropy)
(b) Second law of thermodynamics 17

18. The Second Law of Thermodynamics
During every energy transfer or transformation, some energy is unusable and is often lost as heat
According to the second law of thermodynamics
Every energy transfer or transformation increases the entropy of the universe
Entropy is a measure of disorder, or randomness
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19. Living cells unavoidably convert organized forms of energy to heat
Spontaneous processes occur without energy input; they can happen quickly or slowly
For a process to occur without energy input, it must increase the entropy of the universe
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20. Biological Order and Disorder
Cells create ordered structures from less ordered materials
Organisms also replace ordered forms of matter and energy with less ordered forms
Energy flows into an ecosystem in the form of light and exits in the form of heat
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21. Figure 6.4
Figure 6.4 Order as a characteristic of life 21

22. Figure 6.4a
Figure 6.4a Order as a characteristic of life (part 1: sea urchin) 22

23. Figure 6.4b
Figure 6.4b Order as a characteristic of life (part 2: succulent) 23

24. The evolution of more complex organisms does not violate the second law of thermodynamics
Entropy (disorder) may decrease in an organism, but the universe’s total entropy increases
Organisms are islands of low entropy in an increasingly random universe
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25. Concept 6.2: The free-energy change of a reaction tells us whether or not the reaction occurs spontaneously
Biologists want to know which reactions occur spontaneously and which require input of energy
To do so, they need to determine energy changes that occur in chemical reactions
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26. Free-Energy Change (G), Stability, and Equilibrium
A living system’s free energy is energy that can do work when temperature and pressure are uniform, as in a living cell
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27. ∆G = Gfinal state – Ginitial state
The change in free energy (∆G) during a chemical reaction is the difference between the free energy of the final state and the free energy of the initial state
∆G = Gfinal state – Ginitial state
Only processes with a negative ∆G are spontaneous
Spontaneous processes can be harnessed to perform work
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28. Free energy is a measure of a system’s instability, its tendency to change to a more stable state
During a spontaneous change, free energy decreases and the stability of a system increases
At equilibrium, forward and reverse reactions occur at the same rate; it is a state of maximum stability
A process is spontaneous and can perform work only when it is moving toward equilibrium
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29. More free energy (higher G) Less stable Greater work capacity
Figure 6.5
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
Figure 6.5 The relationship of free energy to stability, work capacity, and spontaneous change
Less free energy (lower G)
More stable
Less work capacity
(a) Gravitational
motion
(b) Diffusion
(c) Chemical
reaction 29

30. More free energy (higher G) Less stable Greater work capacity
Figure 6.5a
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
Figure 6.5a The relationship of free energy to stability, work capacity, and spontaneous change (part 1: free energy and spontaneity)
Less free energy (lower G)
More stable
Less work capacity 30

31. (a) Gravitational motion (b) Diffusion (c) Chemical reaction
Figure 6.5b
Figure 6.5b The relationship of free energy to stability, work capacity, and spontaneous change (part 2: gravitational motion, diffusion, and chemical reaction)
(a) Gravitational
motion
(b) Diffusion
(c) Chemical
reaction 31

32. Free Energy and Metabolism
The concept of free energy can be applied to the chemistry of life’s processes
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33. Exergonic and Endergonic Reactions in Metabolism
An exergonic reaction proceeds with a net release of free energy and is spontaneous; ∆G is negative
The magnitude of ∆G represents the maximum amount of work the reaction can perform
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34. Amount of energy released (G  0) Amount of energy required (G  0)
Figure 6.6
(a) Exergonic reaction: energy released, spontaneous
Reactants
Amount of
energy
released
(G  0)
Energy
Free energy
Products
Progress of the reaction
(b) Endergonic reaction: energy required,
nonspontaneous
Products
Figure 6.6 Free energy changes (ΔG) in exergonic and endergonic reactions
Amount of
energy
required
(G  0)
Energy
Free energy
Reactants
Progress of the reaction 34

35. Amount of energy released (G  0)
Figure 6.6a
(a) Exergonic reaction: energy released, spontaneous
Reactants
Amount of
energy
released
(G  0)
Energy
Free energy
Products
Figure 6.6a Free energy changes (ΔG) in exergonic and endergonic reactions (part 1: exergonic)
Progress of the reaction 35

36. Amount of energy required (G  0)
Figure 6.6b
(b) Endergonic reaction: energy required,
nonspontaneous
Products
Amount of
energy
required
(G  0)
Energy
Free energy
Reactants
Figure 6.6b Free energy changes (ΔG) in exergonic and endergonic reactions (part 2: endergonic)
Progress of the reaction 36

37. An endergonic reaction absorbs free energy from its surroundings and is nonspontaneous; ∆G is positive
The magnitude of ∆G is the quantity of energy required to drive the reaction
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38. Equilibrium and Metabolism
Reactions in a closed system eventually reach equilibrium and then do no work
Cells are not in equilibrium; they are open systems experiencing a constant flow of materials
A defining feature of life is that metabolism is never at equilibrium
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39. Closed and open hydroelectric systems can serve as analogies
A catabolic pathway in a cell releases free energy in a series of reactions
Closed and open hydroelectric systems can serve as analogies
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40. (a) An isolated hydroelectric system
Figure 6.7
G  0
G  0
(a) An isolated hydroelectric system
(b) An open
hydroelectric
system
G  0
Figure 6.7 Equilibrium and work in isolated and open systems
G  0
G  0
G  0
(c) A multistep open hydroelectric system 40

41. (a) An isolated hydroelectric system
Figure 6.7a
G  0
G  0
Figure 6.7a Equilibrium and work in isolated and open systems (part 1: isolated system)
(a) An isolated hydroelectric system 41

42. (b) An open hydroelectric system G  0 Figure 6.7b
Figure 6.7b Equilibrium and work in isolated and open systems (part 2: open system) 42

43. (c) A multistep open hydroelectric system
Figure 6.7c
G  0
G  0
G  0
Figure 6.7c Equilibrium and work in isolated and open systems (part 3: multistep system)
(c) A multistep open hydroelectric system 43

44. Concept 6.3: ATP powers cellular work by coupling exergonic reactions to endergonic reactions
A cell does three main kinds of work
Chemical
Transport
Mechanical
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45. Most energy coupling in cells is mediated by ATP
To do work, cells manage energy resources by energy coupling, the use of an exergonic process to drive an endergonic one
Most energy coupling in cells is mediated by ATP
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46. The Structure and Hydrolysis of ATP
ATP (adenosine triphosphate) is composed of ribose (a sugar), adenine (a nitrogenous base), and three phosphate groups
In addition to its role in energy coupling, ATP is also used to make RNA
Video: ATP Space-filling Model
Video: ATP Stick Model
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47. (a) The structure of ATP
Figure 6.8
Adenine
Phosphate groups
Ribose
(a) The structure of ATP
Adenosine triphosphate (ATP)
Figure 6.8 The structure and hydrolysis of adenosine triphosphate (ATP)
Energy
Inorganic
phosphate
Adenosine diphosphate (ADP)
(b) The hydrolysis of ATP 47

48. (a) The structure of ATP
Figure 6.8a
Adenine
Phosphate groups
Ribose
Figure 6.8a The structure and hydrolysis of adenosine triphosphate (ATP) (part 1: structure)
(a) The structure of ATP 48

49. Adenosine triphosphate (ATP)
Figure 6.8b
Adenosine triphosphate (ATP)
Figure 6.8b The structure and hydrolysis of adenosine triphosphate (ATP) (part 2: hydrolysis)
Energy
Inorganic
phosphate
Adenosine diphosphate (ADP)
(b) The hydrolysis of ATP 49

50. Energy is released from ATP when the terminal phosphate bond is broken
The bonds between the phosphate groups of ATP can be broken by hydrolysis
Energy is released from ATP when the terminal phosphate bond is broken
This release of energy comes from the chemical change to a state of lower free energy, not from the phosphate bonds themselves
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51. How the Hydrolysis of ATP Performs Work
The three types of cellular work (mechanical, transport, and chemical) are powered by the hydrolysis of ATP
In the cell, the energy from the exergonic reaction of ATP hydrolysis can be used to drive an endergonic reaction
Overall, the coupled reactions are exergonic
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52. Phosphorylated intermediate
Figure 6.9
GGlu  3.4 kcal/mol
Glutamic acid
Ammonia
Glutamine
(a) Glutamic acid conversion to glutamine
Glutamic acid
Phosphorylated
intermediate
Glutamine
(b) Conversion reaction coupled with ATP hydrolysis
GGlu  3.4 kcal/mol
Figure 6.9 How ATP drives chemical work: energy coupling using ATP hydrolysis
GGlu  3.4 kcal/mol
GATP  −7.3 kcal/mol
GATP  −7.3 kcal/mol 
(c) Free-energy change for coupled reaction
G  −3.9 kcal/mol
Net 52

53. GGlu  3.4 kcal/mol Glutamic acid Ammonia Glutamine
Figure 6.9a
Glutamic acid
Ammonia
Glutamine
GGlu  3.4 kcal/mol
(a) Glutamic acid conversion to glutamine
Figure 6.9a How ATP drives chemical work: energy coupling using ATP hydrolysis (part 1: a nonspontaneous reaction) 53

54. Phosphorylated intermediate Phosphorylated intermediate
Figure 6.9b
Glutamic acid
Phosphorylated
intermediate
Figure 6.9b How ATP drives chemical work: energy coupling using ATP hydrolysis (part 2: phosphorylation)
Phosphorylated
intermediate
Glutamine
(b) Conversion reaction coupled with ATP hydrolysis 54

55. (c) Free-energy change for coupled reaction G  −3.9 kcal/mol Net
Figure 6.9c
GGlu  3.4 kcal/mol
GGlu  3.4 kcal/mol
GATP  −7.3 kcal/mol
GATP  −7.3 kcal/mol 
Figure 6.9c How ATP drives chemical work: energy coupling using ATP hydrolysis (part 3: coupled free energy)
(c) Free-energy change for coupled reaction
G  −3.9 kcal/mol
Net 55

56. The recipient molecule is now called a phosphorylated intermediate
ATP drives endergonic reactions by phosphorylation, transferring a phosphate group to some other molecule, such as a reactant
The recipient molecule is now called a phosphorylated intermediate
ATP hydrolysis leads to a change in a protein’s shape and often its ability to bind to another molecule
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57. Protein and vesicle moved
Figure 6.10
Transport protein
Solute
Solute transported
(a) Transport work: ATP phosphorylates transport proteins.
Vesicle
Cytoskeletal track
Figure 6.10 How ATP drives transport and mechanical work
Motor protein
Protein and
vesicle moved
(b) Mechanical work: ATP binds noncovalently to motor proteins
and then is hydrolyzed. 57

58. The Regeneration of ATP
ATP is a renewable resource that is regenerated by addition of a phosphate group to adenosine diphosphate (ADP)
The energy to phosphorylate ADP comes from catabolic reactions in the cell
The ATP cycle is a revolving door through which energy passes during its transfer from catabolic to anabolic pathways
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59. Energy from catabolism (exergonic, energy- releasing processes)
Figure 6.11
Energy from
catabolism
(exergonic, energy-
releasing processes)
Energy for cellular
work (endergonic,
energy-consuming
processes)
Figure 6.11 The ATP cycle 59

60. Concept 6.4: Enzymes speed up metabolic reactions by lowering energy barriers
A catalyst is a chemical agent that speeds up a reaction without being consumed by the reaction
An enzyme is a catalytic protein
Hydrolysis of sucrose by the enzyme sucrase is an example of an enzyme-catalyzed reaction
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61. Sucrose (C12H22O11) Glucose (C6H12O6) Fructose (C6H12O6)
Figure 6.UN02
Sucrase
Sucrose
(C12H22O11)
Glucose
(C6H12O6)
Fructose
(C6H12O6)
Figure 6.UN02 In-text figure, hydrolysis of sucrose, p. 125 61

62. The Activation Energy Barrier
Every chemical reaction between molecules involves bond breaking and bond forming
The initial energy needed to start a chemical reaction is called the free energy of activation, or activation energy (EA)
Activation energy is often supplied in the form of thermal energy that the reactant molecules absorb from their surroundings
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63. Progress of the reaction
Figure 6.12 A B C D
Transition state A B EA
Free energy C D
Reactants A B
Figure 6.12 Energy profile of an exergonic reaction
G  0 C D
Products
Progress of the reaction 63

64. How Enzymes Speed Up Reactions
Enzymes catalyze reactions by lowering the EA barrier
Enzymes do not affect the change in free energy (∆G); instead, they hasten reactions that would occur eventually
Animation: How Enzymes Work
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65. Progress of the reaction
Figure 6.13
Course of
reaction
without
enzyme EA
without
enzyme
EA with
enzyme
is lower
Reactants
Free energy
Course of
reaction
with enzyme
G is unaffected
by enzyme
Figure 6.13 The effect of an enzyme on activation energy
Products
Progress of the reaction 65

66. Substrate Specificity of Enzymes
The reactant that an enzyme acts on is called the enzyme’s substrate
The enzyme binds to its substrate, forming an enzyme-substrate complex
The active site is the region on the enzyme where the substrate binds
Enzyme specificity results from the complementary fit between the shape of its active site and the substrate shape
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67. Enzymes change shape due to chemical interactions with the substrate
This induced fit of the enzyme to the substrate brings chemical groups of the active site into positions that enhance their ability to catalyze the reaction
Video: Enzyme Induced Fit
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68. Substrate Active site Enzyme Enzyme-substrate complex Figure 6.14
Figure 6.14 Induced fit between an enzyme and its substrate
Enzyme
Enzyme-substrate
complex 68

69. Catalysis in the Enzyme’s Active Site
In an enzymatic reaction, the substrate binds to the active site of the enzyme
The active site can lower an EA barrier by
Orienting substrates correctly
Straining substrate bonds
Providing a favorable microenvironment
Covalently bonding to the substrate
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70. Substrates are 2 Substrates enter 1 held in active site by
Figure 2
Substrates are
held in active site by
weak interactions. 1
Substrates enter
active site.
Substrates
Enzyme-substrate
complex
Figure The active site and catalytic cycle of an enzyme (steps 1-2) 70

71. Substrates are 2 Substrates enter 1 held in active site by
Figure 2
Substrates are
held in active site by
weak interactions. 1
Substrates enter
active site.
Substrates
Enzyme-substrate
complex
Figure The active site and catalytic cycle of an enzyme (step 3) 3
Substrates are
converted to
products. 71

72. 2 Substrates are held in active site by weak interactions. 1
Figure 2
Substrates are
held in active site by
weak interactions. 1
Substrates enter
active site.
Substrates
Enzyme-substrate
complex
Figure The active site and catalytic cycle of an enzyme (step 4) 4
Products are
released. 3
Substrates are
converted to
products.
Products 72

73. 2 Substrates are held in active site by weak interactions. 1
Figure 2
Substrates are
held in active site by
weak interactions. 1
Substrates enter
active site.
Substrates
Enzyme-substrate
complex
Active
site is
available
for new
substrates. 5
Figure The active site and catalytic cycle of an enzyme (step 5)
Enzyme
Products are
released. 4 3
Substrates are
converted to
products.
Products 73

74. Effects of Local Conditions on Enzyme Activity
An enzyme’s activity can be affected by
General environmental factors, such as temperature and pH
Chemicals that specifically influence the enzyme
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75. Effects of Temperature and pH
Each enzyme has an optimal temperature in which it can function
Each enzyme has an optimal pH in which it can function
Optimal conditions favor the most active shape for the enzyme molecule
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76. Optimal temperature for typical human enzyme (37C)
Figure 6.16
Optimal temperature for
typical human enzyme
(37C)
Optimal temperature for
enzyme of thermophilic
(heat-tolerant)
bacteria (77C)
Rate of reaction 20 40 60 80
100
120
Temperature (C)
(a) Optimal temperature for two enzymes
Optimal pH for pepsin
(stomach
enzyme)
Optimal pH for trypsin
(intestinal
enzyme)
Figure 6.16 Environmental factors affecting enzyme activity
Rate of reaction 1 2 3 4 5 6 7 8 9 10 pH
(b) Optimal pH for two enzymes 76

77. Optimal temperature for typical human enzyme (37C)
Figure 6.16a
Optimal temperature for
typical human enzyme
(37C)
Optimal temperature for
enzyme of thermophilic
(heat-tolerant)
bacteria (77C)
Rate of reaction
Figure 6.16a Environmental factors affecting enzyme activity (part 1: temperature) 20 40 60 80
100
120
Temperature (C)
(a) Optimal temperature for two enzymes 77

78. (b) Optimal pH for two enzymes
Figure 6.16b
Optimal pH for pepsin
(stomach
enzyme)
Optimal pH for trypsin
(intestinal
enzyme)
Rate of reaction
Figure 6.16b Environmental factors affecting enzyme activity (part 2: pH) 1 2 3 4 5 6 7 8 9 10 pH
(b) Optimal pH for two enzymes 78

79. Cofactors Cofactors are nonprotein enzyme helpers
Cofactors may be inorganic (such as a metal in ionic form) or organic
An organic cofactor is called a coenzyme
Coenzymes include vitamins
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80. Enzyme Inhibitors
Competitive inhibitors bind to the active site of an enzyme, competing with the substrate
Noncompetitive inhibitors bind to another part of an enzyme, causing the enzyme to change shape and making the active site less effective
Examples of inhibitors include toxins, poisons, pesticides, and antibiotics
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81. (b) Competitive inhibition (c) Noncompetitive inhibition
Figure 6.17
(a) Normal binding
(b) Competitive inhibition
(c) Noncompetitive
inhibition
Substrate
Active site
Competitive
inhibitor
Enzyme
Figure 6.17 Inhibition of enzyme activity
Noncompetitive
inhibitor 81

82. The Evolution of Enzymes
Enzymes are proteins encoded by genes
Changes (mutations) in genes lead to changes in amino acid composition of an enzyme
Altered amino acids in enzymes may alter their substrate specificity
Under new environmental conditions a novel form of an enzyme might be favored
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83. Concept 6.5: Regulation of enzyme activity helps control metabolism
Chemical chaos would result if a cell’s metabolic pathways were not tightly regulated
A cell does this by switching on or off the genes that encode specific enzymes or by regulating the activity of enzymes
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84. Allosteric Regulation of Enzymes
Allosteric regulation may either inhibit or stimulate an enzyme’s activity
Allosteric regulation occurs when a regulatory molecule binds to a protein at one site and affects the protein’s function at another site
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85. Allosteric Activation and Inhibition
Most allosterically regulated enzymes are made from polypeptide subunits
Each enzyme has active and inactive forms
The binding of an activator stabilizes the active form of the enzyme
The binding of an inhibitor stabilizes the inactive form of the enzyme
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86. (a) Allosteric activators and inhibitors
Figure 6.18
(a) Allosteric activators and inhibitors
(b) Cooperativity: another type of allosteric
activation
Allosteric enzyme
with four subunits
Active site
(one of four)
Substrate
Regulatory
site (one
of four)
Activator
Active form
Stabilized
active form
Inactive form
Stabilized
active form
Oscillation
Figure 6.18 Allosteric regulation of enzyme activity
Non-
functional
active site
Inhibitor
Inactive
form
Stabilized
inactive form 86

87. (a) Allosteric activators and inhibitors
Figure 6.18a
(a) Allosteric activators and inhibitors
Allosteric enzyme
with four subunits
Active site
(one of four)
Regulatory
site (one
of four)
Activator
Active form
Stabilized
active form
Oscillation
Figure 6.18a Allosteric regulation of enzyme activity (part 1: activation and inhibition)
Non-
functional
active site
Inhibitor
Inactive
form
Stabilized
inactive form 87

88. Stabilized active form
Figure 6.18b
(b) Cooperativity: another type of allosteric
activation
Substrate
Figure 6.18b Allosteric regulation of enzyme activity (part 2: cooperativity)
Inactive form
Stabilized
active form 88

89. Cooperativity is a form of allosteric regulation that can amplify enzyme activity
One substrate molecule primes an enzyme to act on additional substrate molecules more readily
Cooperativity is allosteric because binding by a substrate to one active site affects catalysis in a different active site
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90. Feedback Inhibition
In feedback inhibition, the end product of a metabolic pathway shuts down the pathway
Feedback inhibition prevents a cell from wasting chemical resources by synthesizing more product than is needed
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91. End product (isoleucine)
Figure 6.19
Active site available
Threonine
in active site
Enzyme 1
(threonine
deaminase)
Isoleucine
used up by
cell
Intermediate A
Feedback
inhibition
Enzyme 2
Intermediate B
Enzyme 3
Intermediate C
Isoleucine
binds to
allosteric
site.
Figure 6.19 Feedback inhibition in isoleucine synthesis
Enzyme 4
Intermediate D
Enzyme 5
End product
(isoleucine) 91

92. Specific Localization of Enzymes Within the Cell
Structures within the cell help bring order to metabolic pathways
Some enzymes act as structural components of membranes
In eukaryotic cells, some enzymes reside in specific organelles; for example, enzymes for cellular respiration are located in mitochondria
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93. Mitochondria The matrix contains enzymes in solution
Figure 6.20
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.
Figure 6.20 Organelles and structural order in metabolism
1 m 93

94. The matrix contains enzymes in solution that are involved in
Figure 6.20a
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.
Figure 6.20a Organelles and structural order in metabolism (TEM)
1 m 94

95. Figure 6.UN03
Figure 6.UN03 Skills exercise: making a line graph and calculating a slope 95

96. Progress of the reaction
Figure 6.UN04
Course of
reaction
without
enzyme EA
without
enzyme
EA with
enzyme
is lower
Reactants
Free energy
Course of
reaction
with enzyme
G is unaffected
by enzyme
Figure 6.UN04 Summary of key concepts: enzymes and activation energy
Products
Progress of the reaction 96