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Energy and Metabolism

The Energy of Life

The living cell generates thousands of


different reactions
Metabolism
Is the totality of an organisms chemical
reactions
Arises from interactions between molecules
An organisms metabolism transforms matter
and energy, subject to the laws of
thermodynamics
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Metabolic Pathways

Biochemical pathways are the organizational units of metabolism


Metabolism is the total of all chemical reactions carried out by an
organism
A metabolic pathway has many steps that begin with a specific
molecule and end with a product, each catalyzed by a specific enzyme
Reactions that join small molecules together to form larger, more
complex molecules are called anabolic.
Reactions that break large molecules down into smaller subunits are
called catabolic.

Enzyme 1
A

Enzyme 3
D

B
Reaction 1

Starting
molecule

Enzyme 2
Reaction 2

Reaction 3
Product
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Metabolic Pathway

A sequence of chemical reactions, where the product of one


reaction serves as a substrate for the next, is called a
metabolic pathway or biochemical pathway
Most metabolic pathways take place in specific regions of
the cell.

Bioenergetics
Bioenergetics is the study of how organisms
manage their energy resources via
metabolic pathways
Catabolic pathways release energy by
breaking down complex molecules into
simpler compounds
Anabolic pathways consume energy to build
complex molecules from simpler ones

Energy

Energy is the capacity to do work or ability to


cause change. Any change in the universe
requires energy. Energy comes in 2 forms:
Potential energy is stored energy. No
change is currently taking place
Kinetic energy is currently causing
change. This always involves some type
of motion.

Forms of Energy

Kinetic energy is the


energy associated with
motion
Potential energy
Is stored in the
location of matter
Includes chemical
energy stored in
molecular structure
Energy can be converted
from one form to another

On the platform, a diver


has more potential energy.

Climbing up converts kinetic


energy of muscle movement

Diving converts potential


energy to kinetic energy.

In the water, a diver has


less potential energy.

to potential energy.

Laws of Energy Transformation


Thermodynamics is the study of energy
changes.
Two fundamental laws govern all energy
changes in the universe. These 2 laws are
simply called the first and second laws of
thermodynamics:

The First Law of Thermodynamics

According to the first law of thermodynamics


Energy cannot be created or destroyed
Energy can be transferred and transformed

Chemical
energy

For example, the chemical (potential) energy


in food will be converted to the kinetic
energy of the cheetahs movement

Second Law of Thermodynamics

The disorder (entropy) in the universe is continuously increasing.


Energy transformations proceed spontaneously to convert matter from a
more ordered, less stable form, to a less ordered, more stable form
Spontaneous changes that do not require outside energy increase the
entropy, or disorder, of the universe
For a process to occur without energy input, it must increase the entropy of
the universe

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Second Law of Thermodynamics

During each conversion, some of the energy dissipates into the


environment as heat.
During every energy transfer or transformation, some energy is
unusable, often lost as heat
Heat is defined as the measure of the random motion of molecules
Living cells unavoidably convert organized forms of energy to heat
According to the second law of thermodynamics, every energy transfer
or transformation increases the entropy (disorder) of the universe

Heat

co2

H2O

For example, disorder is added to the cheetahssurroundings in the form of heat


and the small molecules that are the by-products of metabolism.

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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
The evolution of more complex organisms does
not violate the second law of thermodynamics
Entropy (disorder) may decrease in an
organism, but the universes total entropy
increases

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Biological Order and Disorder

Living systems

Increase the entropy of the universe


Use energy to maintain order
A living systems free energy is energy that can
do work under cellular conditions
Organisms live at the expense of free energy
50m

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Free Energy

Free energy is the portion of a systems energy that is able


to perform work when temperature and pressure is uniform
throughout the system, as in a living cell
Free energy also refers to the amount of energy actually
available to break and subsequently form other chemical
bonds
Gibbs free energy (G) in a cell, the amount of energy
contained in a molecules chemical bonds (T&P constant)
Change in free energy - G
Endergonic - any reaction that requires an input of
energy
Exergonic - any reaction that releases free energy

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Exergonic reactions

Reactants have more free energy than the products


Involve a net release of energy and/or an increase in
entropy
Occur spontaneously (without a net input of energy)
Reactants

Free energy

Amount of
energy
released
(G <0)
Energy

Products

Progress of the reaction


(a) Exergonic reaction: energy released

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Endergonic Reactions

Reactants have less free energy than the products


Involve a net input of energy and/or a decrease in
entropy
Do not occur spontaneously
Products

Free energy

Energy

Amount of
energy
released
(G>0)

Reactants

Progress of the reaction


(b) Endergonic reaction: energy required

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Energy released Energy supplied

Product
Energy
must be
supplied.
Reactant

Reactant

Energy is
released.
Product

Endergonic

Exergonic
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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 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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Equilibrium and Metabolism

Reactions in a closed system eventually reach equilibrium


G < 0

G = 0

(a) A closed hydroelectric system. Water flowing downhill turns a turbine


that drives a generator providing electricity to a light bulb, but only until
the system reaches equilibrium.

Cells in our body experience a constant flow of materials


in and out, preventing metabolic pathways from reaching
equilibrium
(b) An open hydroelectric
system. Flowing water
keeps driving the generator
because intake and outflow
of water keep the system
from reaching equlibrium.

G < 0

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An Analogy For Cellular Respiration


Glucose Catabolism
G < 0
G < 0
G < 0

(c) A multistep open hydroelectric system. Cellular respiration is

analogous to this system: Glucoce is brocken down in a series


of exergonic reactions that power the work of the cell. The product
of each reaction becomes the reactant for the next, so no reaction
reaches equilibrium.

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Energy Coupling
Living organisms have the ability to couple
exergonic and endergonic reactions:
Energy released by exergonic reactions is
captured and used to make ATP from ADP
and Pi
ATP can be broken back down to ADP and
Pi, releasing energy to power the cells
endergonic reactions.

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The Structure and Hydrolysis of ATP

ATP (adenosine triphosphate)


Is the cells energy shuttle
Provides energy for cellular functions
Adenine
N
O

-O
O

O
O

CH2

Phosphate groups

HC

O
O

NH2

H
OH

CH

Ribose

OH

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The Structure and Hydrolysis of ATP

Energy is released from ATP when the terminal phosphate

bond is broken

Adenosine triphosphate (ATP)


H2O

Inorganic phosphate

Energy

Adenosine diphosphate (ADP)


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Cellular Work

A cell does three main kinds of work


Mechanical
Transport
Chemical
Energy coupling is a key feature in the way cells
manage their energy resources to do this work
ATP powers cellular work by coupling exergonic
reactions to endergonic reactions

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Energy Coupling - ATP / ADP Cycle

Releasing the third phosphate from ATP to make ADP generates


energy (exergonic):
Linking the phosphates together requires energy - so making ATP from
ADP and a third phosphate requires energy (endergonic),
Catabolic pathways drive the regeneration of ATP from ADP and
phosphate
ATP hydrolysis to
ADP + P i yields energy

ATP synthesis from


ADP + P i requires energy

ATP

Energy from catabolism


(exergonic, energy yielding
processes)

Energy for cellular work


(endergonic, energyconsuming processes)

ADP + P

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How ATP Performs Work

ATP drives endergonic reactions by


phosphorylation, transferring a phosphate group
to some other molecule, such as a reactant
The recipient molecule is now phosphorylated
The three types of cellular work (mechanical,
transport, and chemical) are powered by the
hydrolysis of ATP

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How ATP Performs Work

ATP drives endergonic reactions by phosphorylation, transferring a


phosphate to other molecules - hydrolysis of ATP

Motor protein
Protein moved
(a) Mechanical work: ATP phosphorylates motor proteins
Membrane
protein

ADP

ATP

Solute

Solute transported

(b) Transport work: ATP phosphorylates transport proteins

Glu +

NH3

Reactants: Glutamic acid


and ammonia

NH2

Glu
Product (glutamine)
made

(c) Chemical work: ATP phosphorylates key reactants

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Activation Energy

All reactions, both endergonic and exergonic, require an input of energy to


get started. This energy is called activation energy
The activation energy, EA

Is the initial amount of energy needed to start a chemical reaction


Activation energy is needed to bring the reactants close together and weaken
existing bonds to initiate a chemical reaction.
Is often supplied in the form of heat from the surroundings in a system.
A

Transition state

Free energy

EA

Reactants

G < O
C

Products
Progress of the reaction
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Reaction Rates

In most cases, molecules do not have enough


kinetic energy to reach the transition state when
they collide.
Therefore, most collisions are non-productive, and
the reaction proceeds very slowly if at all.
What can be done to speed up these reactions?

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Increasing Reaction Rates

Activation Energy and Catalysis


Energy supplied

Add Energy (Heat) - molecules move faster so they collide


more frequently and with greater force.
Add a catalyst a catalyst reduces the energy needed to
reach the activation state, without being changed itself.
Proteins that function as catalysts are called enzymes.

Energy released

Activation
energy
Activation
energy
Reactant

Reactant

Product

Uncatalyzed

Product

Catalyzed
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Copyright The McGraw-Hill Companies, Inc. Permission required for reproduction or display.

Enzymes Lower the EA Barrier


An enzyme catalyzes reactions by lowering
the EA barrier
Course of
reaction
without
enzyme

Free energy

EA
without
enzyme

EA with
enzyme
is lower

Reactants

G is unaffected
by enzyme

Course of
reaction
with enzyme

Products
Progress of the reaction

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Enzymes Are Biological Catalysts

Enzymes are proteins that carry out most catalysis in living


organisms.
Unlike heat, enzymes are highly specific. Each enzyme
typically speeds up only one or a few chemical reactions.
Unique three-dimensional shape enables an enzyme to
stabilize a temporary association between substrates.
Because the enzyme itself is not changed or consumed in
the reaction, only a small amount is needed, and can then
be reused.
Therefore, by controlling which enzymes are made, a cell
can control which reactions take place in the cell.

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Substrate Specificity of Enzymes

Almost all enzymes are globular proteins with one or more active sites on their
surface.
The substrate is the reactant an enzyme acts on
Reactants bind to the active site to form an enzyme-substrate complex.
The 3-D shape of the active site and the substrates must match, like a lock and key
Binding of the substrates causes the enzyme to adjust its shape slightly, leading to
a better induced fit.
Induced fit of a substrate brings chemical groups of the active site into positions
that enhance their ability to catalyze the chemical reaction
When this happens, the substrates are brought close together and existing bonds
are stressed. This reduces the amount of energy needed to reach the transition
state.
Substate

Active site

Enzyme

Enzyme- substrate
complex

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The Catalytic Cycle Of An Enzyme


1 Substrates enter active site; enzyme
changes shape so its active site
embraces the substrates (induced fit).

Substrates

Enzyme-substrate
complex

6 Active site
Is available for
two new substrate
Mole.
Enzyme

5 Products are
Released.
Figure 8.17

Products

2 Substrates held in
active site by weak
interactions, such as
hydrogen bonds and
ionic bonds.
3 Active site (and R groups of
its amino acids) can lower EA
and speed up a reaction by
acting as a template for
substrate orientation,
stressing the substrate bonds
and stabilizing the
transition state,
providing a favorable
microenvironment,
participating directly in the
catalytic reaction.

4 Substrates are
Converted into
Products.

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The Catalytic Cycle Of An Enzyme


1 The substrate, sucrose, consists
of glucose and fructose bonded together.
Glucose
2 The substrate binds to the enzyme,
forming an enzyme-substrate
complex.

Bond

H2O

Active site
Enzyme

Fructose

4 Products are
released, and the
enzyme is free to
bind other
substrates.

3 The binding of the substrate


and enzyme places stress on
the glucose-fructose bond,
and the bond breaks.

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Factors Affecting Enzyme Activity


Temperature - rate of an enzyme-catalyzed
reaction increases with temperature, but
only up to an optimum temperature.
pH - ionic interactions also hold enzymes
together.
Inhibitors and Activators

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Effects of Temperature and pH


Each enzyme has an optimal temperature in
which it can function
Optimal temperature for
typical human enzyme

Optimal temperature for


enzyme of thermophilic
(heat-tolerant)
bacteria

Rate of reaction

20

40
Temperature (C)
(a) Optimal temperature for two enzymes

80

100

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Effects of Temperature and pH


Each enzyme has an optimal pH in which it can
function
Optimal pH for pepsin
(stomach enzyme)

Optimal pH
for trypsin
(intestinal
enzyme)

Rate of reaction

3
4
0
2
1
(b) Optimal pH for two enzymes

Figure 8.18
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Factors Affecting Enzyme Activity

Inhibitor - substance that binds to an enzyme


and decreases its activity feedback
Competitive inhibitors - compete with the
substrate for the same active site
Noncompetitive inhibitors - bind to the
enzyme in a location other than the active
site
Allosteric sites - specific binding sites
acting as on/off switches
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Enzyme Inhibitors

Competitive inhibitors bind to the active site of an enzyme,

competing with the substrate


A substrate can
bind normally to the
active site of an
enzyme.

Substrate
Active site

Enzyme

(a) Normal binding


A competitive
inhibitor mimics the
substrate, competing
for the active site.

Competitive
inhibitor

(b) Competitive inhibition

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Enzyme Inhibitors

Noncompetitive inhibitors bind to another part


of an enzyme, changing the function

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

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Regulation Of Enzyme Activity Helps


Control Metabolism

Chemical chaos would result if a cells metabolic


pathways were not tightly regulated
To regulate metabolic pathways, the cell switches
on or off the genes that encode specific enzymes
Allosteric regulation is the term used to describe
any case in which a proteins function at one site is
affected by binding of a regulatory molecule at
another site
Enzymes change shape when regulatory
molecules bind to specific sites, affecting function
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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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Allosteric Regulation of Enzymes

Allosteric regulation may either inhibit or stimulate an


enzymes activity
Allosteric enyzme
with four subunits

Active site
(one of four)

Regulatory
site (one
of four)

Activator
Active form

Stabilized active form


Allosteric activater
stabilizes inactive form

Oscillation

Nonfunctional
active
site

Allosteric activater
stabilizes active from

Inactive form

Inhibitor

Stabilized inactive
form

(a) Allosteric activators and inhibitors. In the cell, activators and inhibitors
dissociate when at low concentrations. The enzyme can then oscillate again.

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Cooperativity

Is a form of allosteric regulation that can amplify


enzyme activity
Binding of one substrate molecule to
active site of one subunit locks
all subunits in active conformation.

Substrate

Inactive form

Stabilized active form

(b) Cooperativity: another type of allosteric activation. Note that the


inactive form shown on the left oscillates back and forth with the active
form when the active form is not stabilized by substrate.
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Factors Affecting Enzyme Activity

Activators - substances that bind to allosteric


sites and keep the enzymes in their active
configurations - increases enzyme activity
Cofactors - chemical components that
facilitate enzyme activity
Coenzymes - organic molecules that
function as cofactors

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Regulation of Biochemical Pathways


Biochemical pathways must be coordinated
and regulated to operate efficiently.
Advantageous for cell to temporarily shut
down biochemical pathways when their
products are not needed
Feedback Inhibition

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Feedback Inhibition

In feedback inhibition the


end product of a metabolic
pathway shuts down the
pathway
When the cell produces
increasing quantities of a
particular product, it
automatically inhibits its
ability to produce more

Active site
available

Initial substrate
(threonine)
Threonine
in active site
Enzyme 1
(threonine
deaminase)

Isoleucine
used up by
cell

Intermediate A
Feedback
inhibition

Active site of
enzyme 1 no
longer binds
threonine;
pathway is
switched off

Enzyme 2
Intermediate B
Enzyme 3
Intermediate C

Isoleucine
binds to
allosteric
site

Enzyme 4
Intermediate D
Enzyme 5

End product
(isoleucine)

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