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
Photoautotrophs convert light energy in to
chemical energy through photosynthesis.
Some organisms even convert chemical energy
to light, as in bioluminescence

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 Flow of Energy in Living Things

Energy - the capacity to do work

kinetic - energy of motion

potential - stored energy

Thermodynamics - changes in heat

calorie - heat required to raise the

temperature of one gram of water one

degree Celsius
kilocalorie = 1000 calories

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 Metabolism is the totality of an organisms chemical
reactions
A metabolic pathway begins with a specific
molecule and ends with a product
Each step is catalyzed by a specific enzyme

Enzyme 1 Enzyme 2 Enzyme 3

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

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 Bioenergetics is the study of how organisms
manage their energy resources
Anabolic pathways consume energy to build
complex molecules from simpler ones
The synthesis of protein from amino acids is
an example of anabolism

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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 Forms of Energy
Energy is the capacity to cause change
Energy exists in various forms, some of which
can perform work
Kinetic energy is energy associated with motion
Heat (thermal energy) is kinetic energy associated
with random movement of atoms or molecules
Potential energy is energy that matter possesses
because of its location or structure
Chemical energy is potential energy available for
release in a chemical reaction
Energy can be converted from one form to another
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A diver has more potential Diving converts
energy on the platform potential energy to
than in the water. kinetic energy.

Climbing up converts the kinetic A diver has less potential

energy of muscle movement energy in the water
to potential energy. than on the platform.
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 The Laws of Energy Transformation

Thermodynamics is the study of energy

transformations
A 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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 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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 Laws of Thermodynamics

First Law of Thermodynamics

Energy cannot be created or destroyed,

but only change form.

During each conversion, some of the

energy dissipates into the environment

as heat.
Heat is defined as the measure of the

random motion of molecules.

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 Laws of Thermodynamics

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.

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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
According to the second law of
thermodynamics
Every energy transfer or transformation
increases the entropy (disorder) of the
universe

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 Free-Energy Change, G
A living systems free energy is energy that
can do work when temperature and pressure
are uniform, as in a living cell

The change in free energy (G) (Gibbs free

energy) during a process is related to the
change in enthalpy, or change in total energy
(H), change in entropy (S), and temperature
in Kelvin (T)
G = H TS
Only processes with a negative G are
spontaneous. Spontaneous processes can be
harnessed to perform work
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 Free Energy, Stability, and Equilibrium

Free energy is a measure of a systems

instability, its tendency to change to a more
stable state
During a spontaneous change, free energy
decreases and the stability of a system
increases
Equilibrium 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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 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

Less free energy (lower G)

More stable
Less work capacity

(a) Gravitational motion (b) Diffusion (c) Chemical reaction

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 Exergonic and Endergonic Reactions in
Metabolism

An exergonic reaction proceeds with a net

release of free energy and is spontaneous
An endergonic reaction absorbs free energy
from its surroundings and is nonspontaneous

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(a) Exergonic reaction: energy released, spontaneous

Reactants

Amount of
energy
released
(G 0)

Free energy
Energy
Products

Progress of the reaction

(b) Endergonic reaction: energy required, nonspontaneous

Products

Amount of
energy
required
(G 0)
Free energy

Energy
Reactants

Progress of the reaction

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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 defining feature of life is that metabolism is
never at equilibrium
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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 G 0 G 0

(a) An isolated hydroelectric system

(b) An open hydro-

electric system G 0

G 0
G 0
G 0

(c) A multistep open hydroelectric system

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 Metabolism
Metabolism - refers to the sum of all chemical reactions within living
organisms

Catabolism refers to the enzymes regulated chemical reactions that

release energy in living cells
- The reactions are exergonic- produce more energy that they consume
- It involves breakdown of complex organic compounds into simpler ones.
- They are hydrolytic reactions meaning they use water and chemical
bonds are broken down.

Anabolism - refers to the enzymes regulated chemical reactions that

consumes energy in living cells
- These reactions are endergonic- consume more energy than they
produce
- It involves the building of complex molecules from simpler ones
- - these reactions generate the energy necessary for growth
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 Activation Energy

Activation energy refers to the extra energy

required to destabilize existing chemical
bonds and initiate a chemical reaction.
catalyst - substance that lowers the

activation energy
cannot violate laws of thermodynamics.

direction of a chemical reaction is

determined solely by the difference in

free energy between the reactants
and the products

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Activation Energy and Catalysis

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 Activation Energy
Activation energy
Energy needed to allow the

reactants to form products

Necessary for a chemical

Energy Level
Activation
reaction to proceed Z
Energy
Activation energy is needed

even for breakdown reaction X+Y

to get them going
Time

In the laboratory, we heat the reactants in order to provide

activation energy for a chemical reaction
Inside the cell, a different mechanism is required as heating up
the reactants is not possible
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Enzymes Are Biological Catalysts

Figure 5.2 23
 Enzymes Are Biological Catalysts

Enzymes are proteins that carry out most

catalysis in living organisms.
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.

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 Mechanism of enzyme actions
The surface of the substrate contacts a specific region of
the surface of the enzyme called the active site.
A temporary intermediate compound forms, called an
enzyme substrate complex.
The substrate molecule is transformed by the
rearrangement of existing atoms, the breakdown of the
substrate molecule or the combination with another
substrate molecule.
The transformed substrate molecule are released from the
enzyme molecule since they no longer fit in the active site
The unchanged enzyme is now free to react with other
substrate molecules.

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 Enzymes

Most enzymes are globular proteins with one

or more active sites.
Substrates bind to the enzyme at these

active sites, forming an enzyme-substrate

complex.

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 Enzymes
- Enzymes consist of protein portion called a
apoenzyme and a non protein portion called a
cofactor.

- Apoenzymes are inactive and must be activate by

a cofactor

- Together, the apoenzyme and cofactor forms a

holoenzyme which is active

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Enzymes

Figure 5.3 28
 Substrate Specificity of Enzymes

The reactant that an enzyme acts on is called the

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

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 Substrate

Active site

Enzyme Enzyme-substrate
complex
(a) (b)

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 Catalysis in the Enzymes 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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Figure 8.15-1
1 Substrates enter active site.
2 Substrates are held
in active site by weak
interactions.

Substrates
Enzyme-substrate
complex

Active
site

Enzyme

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Figure 8.15-2
1 Substrates enter active site.
2 Substrates are held
in active site by weak
interactions.

Substrates
Enzyme-substrate
complex 3 Active site can
lower EA and speed
up a reaction.

Active
site

Enzyme

4 Substrates are
converted to
products.
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 Figure 8.15-3
1 Substrates enter active site.
2 Substrates are held
in active site by weak
interactions.

Substrates
Enzyme-substrate
complex 3 Active site can
lower EA and speed
up a reaction.

6 Active
site is
available
for two new
substrate
molecules.
Enzyme

5 Products are 4 Substrates are

released. converted to
products.
Products
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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.

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 Factors Influencing Enzyme Activity

Enzymes can be denatured by temperature

and pH

Figure 5.6 36
 Factors Affecting Enzyme Activity

Inhibitors and activators

inhibitor - substance that binds to an

enzyme and decreases its activity

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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 Factors Influencing Enzyme Activity

Competitive inhibition

Figure 5.7a, b 38
 Factors Influencing Enzyme Activity

Noncompetitive inhibition

Figure 5.7a, c 39
 Factors Influencing Enzyme Activity

Feedback
inhibition

Figure 5.8 40
 Classes of enzymes
Class Type of chemical examples
reaction catalysed

oxidoreductase Oxidation/reduction Oxidase, dehydrogenase

transferase Transfer of functional Acetate kinase, alanine

groups such as amino deaminase
group, acetyl group or
phosphate group

hydrolase hydrolysis Lipase, sucrase

lyase Removal of group of Oxalate decarboxylase

atoms without hydrolysis

isomerase Rearrangement of atoms Glucose phosphate

within a molecule isomerase

ligase Joining of two molecules Acetyl Co-A, DNA ligase

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 Co Enzymes
coenzymes are organic molecules that are required by certain
enzymes to carry out catalysis.

1. NAD+ ---- nicotinamide adenine dinucleotide - they assist

enzymes by accepting hydrogen atoms removed from
substrate (catabolic reactions)

2. NADP+----- nicotinamide adenine dinucleotide phosphate-

contains more energy than NAD which can later be used to
generate ATP (anabolic reactions)

3. FAD---- Flavin adenine dinucleotide (electron carriers)

4. Coenzymes A (CoA)----- Oxidizing reactions 42

 Flow of Energy in Living Things

Oxidation - Reduction
Oxidation occurs when an atom or

molecule loses an electron.

Reduction occurs when an atom or

molecule gains an electron.

Redox reactions occur because every

electron that is lost by an atom through

oxidation is gained by some other atom
through reduction.

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 Oxidation-Reduction
Oxidation is the removal of electrons.
Reduction is the gain of electrons.
Redox reaction is an oxidation reaction
paired with a reduction reaction.

OIL RIG: Oxidation is loss of e-, reduction is gain of e- Figure 5.9 44

 The Structure and Hydrolysis of ATP

ATP (adenosine triphosphate) is the cells

energy shuttle
ATP is composed of ribose (a sugar), adenine
(a nitrogenous base), and three phosphate
groups.
ATP stores energy derived from catabolic
reactions and release it later to drive anabolic
reactions and perform cellular functions.

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 Adenine

Phosphate groups
Ribose

(a) The structure of ATP

Adenosine triphosphate (ATP)

Energy

Inorganic
Adenosine diphosphate (ADP)
phosphate

(b) The hydrolysis of ATP

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 ATP Generation
(a) Substrate level phosphorylation
- ATP is usually generated when high energy phosphate is
directly transferred from phosphorylated compound (a
substrate) to ADP
(b) Oxidative phosphorylation
- Electrons are transferred from organic compound to one
group of electron carriers (NAD + or FAD).
- The electrons are passed through a series of different
electron carriers to molecules of oxygen or other oxidized
inorganic molecules. The sequence of electron carriers is
called the electron transport chain
(c) Photophosphorylation
- Occurs in photosynthetic cells, which contain light trapping
pigments such as chlorophyll
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 ATP H2O

Energy from Energy for cellular

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

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 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 noncovalently to motor
proteins and then is hydrolyzed.
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