CAMPBELL

BIOLOGY TENTH
EDITION

Reece • Urry • Cain • Wasserman • Minorsky • Jackson

8
An Introduction
to Metabolism

Lecture Presentation by
Nicole Tunbridge and
Kathleen Fitzpatrick

© 2014 Pearson Education, Inc.

Concept 8.1: An organism’s metabolism

transforms matter and energy, subject to the
laws of thermodynamics

 Metabolism
 Metabolism is an emergent property of life that
arises from orderly interactions between
molecules

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Organization of the Chemistry of Life into
Metabolic Pathways

 Metabolic pathway

Enzyme 1 Enzyme 2 Enzyme 3

A B C D
Reaction 1 Reaction 2 Reaction 3
Starting Product
molecule

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 Cellular respiration

 Fermentation

 Catabolic pathways

 Anabolic pathways

 Bioenergetics
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Forms of Energy

 Energy
 Energy exists in various forms,
some of which can perform work

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 Kinetic energy
 Heat (thermal energy)

 Potential energy
 Chemical energy

 Energy can be converted

from one form to another

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The Laws of Energy Transformation

 Thermodynamics
 An isolated system, such as that approximated by
liquid in a thermos, is unable to exchange energy
or matter with its surroundings
 In an open system, energy and matter can
be transferred between the system and its
surroundings

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The First Law of Thermodynamics

 First law of thermodynamics, the

energy of the universe is constant
 The first law is also called the
principle of conservation of energy

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The Second Law of Thermodynamics

 During every energy transfer or

transformation, some energy is
unusable, and is often lost
as heat
 Second law of thermodynamics

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 Living cells unavoidably convert organized

forms of energy to heat
 Spontaneous processes occur without
energy input; they can happen quickly or slowly

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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

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Concept 8.2: 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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Free-Energy Change, G

 Free energy
∆G = ∆H - T∆S
 Negative ∆G
 Positive ∆G

 Only processes with a negative ∆G are

spontaneous

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Free Energy, Stability, and Equilibrium

 Free energy is a measure of a system’s instability,

its tendency to change to a more stable state
 What happens during spontaneous change?
 Equilibrium is a state of maximum stability

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Free Energy and Metabolism

 The concept of free energy can be applied to the

chemistry of life’s processes

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(a) Exergonic reaction: energy released,

spontaneous
Exergonic and Reactants
Endergonic Reactions Amount of
in Metabolism energy
Free energy

released
Energy (∆G < 0)
Products

 Exergonic
reaction Progress of the reaction

(b) Endergonic reaction: energy required,

 Endergonic nonspontaneous

reaction Products

Amount of
Free energy

energy
required
Energy (∆G > 0)
Reactants

Figure 8.6
© 2014 Pearson Education, Inc. Progress of the reaction

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 Equilibrium and Metabolism
(a)An open hydro-
 Cells are open electric system ∆G < 0
systems
experiencing a
constant flow of
materials
 Metabolism is ∆G < 0
∆G < 0
(always/sometimes ∆G < 0
/never) at
equilibrium
 Catabolism and
(b) A multistep open hydroelectric
anabolism system

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Concept 8.3: 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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The Structure and Hydrolysis of ATP

 ATP (adenosine triphosphate) is the cell’s

energy shuttle
 ATP is composed of ribose (a sugar), adenine
(a nitrogenous base), and three phosphate groups
Adenine

Triphosphate group Ribose

(3 phosphate groups)

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 The bonds between the phosphate groups of

ATP’s tail can be broken by hydrolysis

Adenosine triphosphate
(ATP)
H2O

Energy

Inorganic Adenosine diphosphate

phosphate (ADP)

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 How the Hydrolysis of ATP Performs Work

 The three types of cellular work (mechanical,

transport, and chemical) are powered by the
hydrolysis of ATP

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Figure 8.10

NH3 NH2
Glu Glu
∆GGlu = +3.4 kcal/mol

Glutamic acid Ammonia Glutamine

(a) Glutamic acid conversion to glutamine

NH3

1 P 2
ADP NH2 ADP Pi
Glu ATP Glu Glu
Glutamic acid Phosphorylated Glutamine
intermediate
(b) Conversion reaction coupled with ATP hydrolysis

∆GGlu = +3.4 kcal/mol

NH3 NH2
Glu ATP ADP Pi
Glu

∆GGlu = +3.4 kcal/mol

∆GATP = −7.3 kcal/mol
+ ∆GATP = −7.3 kcal/mol

Net ∆G = −3.9 kcal/mol

(c) Free-energy change for coupled reaction
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  Transport and mechanical work in the cell are also
powered by ATP hydrolysis
 ATP hydrolysis leads to a change in protein shape
and binding ability

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Figure 8.11

Transport protein Solute

ATP ADP Pi

P Pi

Solute transported
(a) Transport work: ATP phosphorylates transport proteins.

Vesicle Cytoskeletal track

ATP ADP Pi
ATP

Motor protein Protein and vesicle moved

(b) Mechanical work: ATP binds non-covalently to motor
proteins and then is hydrolyzed.
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 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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Figure 8.12

ATP H2O

Energy from Energy for cellular

catabolism work (endergonic
(exergonic, energy- ADP Pi energy-consuming
releasing processes) processes)

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Concept 8.4: Enzymes speed up metabolic
reactions by lowering energy barriers

 catalyst
 enzyme

 Hydrolysis of sucrose by the enzyme sucrase is

an example of an enzyme-catalyzed reaction

Sucrase

Sucrose Glucose Fructose

(C12H22O11) (C6H12O6) (C6H12O6)

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The Activation Energy Barrier

 Every chemical reaction between molecules

involves bond breaking and bond forming
 activation energy (EA)
 How is it often supplied to the reaction?

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Figure 8.13

A B

C D
Transition state

A B
EA
Free energy

C D

Reactants
A B
∆G < O
C D

Products

Progress of the reaction

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How Enzymes Speed Up Reactions

 How do enzymes catalyze reactions?

 The effect on free energy?

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Figure 8.14

Course of
reaction EA
without without
enzyme enzyme EA with
enzyme
is lower
Free energy

Reactants

Course of ∆G is unaffected
reaction by enzyme
with enzyme

Products

Progress of the reaction

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Substrate Specificity of Enzymes

 substrate

 enzyme-substrate complex

 What about specificity?

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  active site
 Induced fit of a substrate brings chemical groups
of the active site into positions that enhance their
ability to catalyze the reaction.
Substrate

Active site

Enzyme Enzyme-substrate
complex
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Catalysis in the Enzyme’s Active Site

 In an enzymatic reaction, the substrate binds to

the active site of the enzyme

 How the active site lowers the EA

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Figure 8.16-4

1 Substrates enter 2 Substrates are

active site. held in active
site by weak
interactions.

Substrates
Enzyme-substrate
complex

5 Active site
is available
for new
substrates.

Enzyme

4 Products are
released. 3 Substrates are
converted to
Products products.

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Effects of Local Conditions on Enzyme Activity

 What can affect the activity of an enzyme?

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Figure 8.17
Optimal temperature for Optimal temperature for
typical human enzyme enzyme of thermophilic
(37C) (heat-tolerant)

Rate of reaction
bacteria (77C)

0 20
60 40
80 100 120
Temperature (C)
(a) Optimal temperature for two enzymes

Optimal pH for pepsin Optimal pH for trypsin

(stomach (intestinal
enzyme) enzyme)
Rate of reaction

0 1 5 2 6 3 4 7 8 9 10
pH
(b) Optimal pH for two enzymes
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Effects of Local Conditions on Enzyme Activity

 Cofactors are non-protein enzyme helpers

 coenzyme

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Enzyme Inhibitors

 Competitive inhibitors
 Noncompetitive inhibitors

(a) Normal binding (b) Competitive inhibition (c) Noncompetitive

inhibition

Substrate
Active site
Competitive
inhibitor
Enzyme

Noncompetitive
inhibitor
Figure 8.18

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The Evolution of Enzymes

 Enzymes are proteins encoded by genes

 How do changes (mutations) in genes affect

enzymes?

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Concept 8.5: Regulation of enzyme activity
helps control metabolism

 Chemical chaos would result if a cell’s metabolic

pathways were not tightly regulated

 How do cells regulate enzyme activity?

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Allosteric Regulation of Enzymes

 Allosteric regulation

 Allosteric regulation may inhibit or stimulate an

enzymes activity.

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 Allosteric Activation and Inhibition

 Most allosterically regulated enzymes are made

from polypeptide subunits

 Each enzyme has active and inactive forms

 What about phosphorylation?

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Figure 8.20

(a) Allosteric activators and inhibitors

Allosteric enzyme Active site

with four subunits (one of four)

Regulatory
site (one Activator
of four) Active form Stabilized
active form

Oscillation
Non-
functional
active site

Inhibitor
Inactive form Stabilized
inactive form
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  Cooperativity is a form of allosteric regulation
that can amplify enzyme activity

 Why is cooperativity considered allosteric?

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(b) Cooperativity: another type

of allosteric activation

Substrate

Inactive form Stabilized

active form

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 Feedback Inhibition

 feedback inhibition
 Feedback inhibition prevents a cell from wasting
chemical resources by synthesizing more product
than is needed

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Figure 8.21
Active site available Threonine
in active site

Enzyme 1
(threonine
Isoleucine deaminase)
used up by
cell
Intermediate A
Feedback
inhibition Active
site no Enzyme 2
longer
available; Intermediate B
pathway
is halted. Enzyme 3

Intermediate C
Isoleucine
binds to Enzyme 4
allosteric
site.
Intermediate D

Enzyme 5

End product
(isoleucine)
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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

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