8 Energy, Enzymes, and

Metabolism
8 Energy, Enzymes, and Metabolism

• 8.1 What Physical Principles Underlie

Biological Energy Transformations?
• 8.2 What Is the Role of ATP in
Biochemical Energetics?
• 8.3 What Are Enzymes?
• 8.4 How Do Enzymes Work?
• 8.5 How Are Enzyme Activities Regulated?
8.1 What Physical Principles Underlie Biological Energy
Transformations?

Energy: is the capacity to do work.

Transformation of energy is required by

living things.

The first of thermodynamics

A fundamental law is that energy can be
transformed fom one form to another but
cannot be created or destroyed.
8.1 What Physical Principles Underlie Biological Energy
Transformations?

All forms of energy can be placed in two

categories:

• Potential energy is stored energy—such

as concentration gradient,

• Kinetic energy is the energy of

movement
Figure 8.1 Energy Conversions and Work
8.1 What Physical Principles Underlie Biological Energy
Transformations?

Metabolism: Sum total of all chemical

reactions in an organism.

1) Anabolic reactions: synthesis (building)

of complex molecules from simple
molecules; energy input is required.

2) Catabolic reactions: breaking down of

complex molecules into to simpler ones;
energy is released. (ex. DIGESTION)
8.1 What Physical Principles Underlie Biological Energy
Transformations?
Change in energy can be measured in calories or joules.

Change in free energy (ΔG) in a reaction is the difference in

free energy of the products and the reactants.

ΔGreaction = Gproducts - Greactants

• If ΔG is negative, free energy is released-exergonic

reaction.

• If ΔG is positive, free energy is consumed-endergonic reaction

If free energy is not available, the reaction does not occur.

8.1 What Physical Principles Underlie Biological Energy
Transformations?

Exergonic reactions release free energy (–ΔG):

Catabolism (breakdown)
8.1 What Physical Principles Underlie Biological Energy
Transformations?

Endergonic reactions consume free energy

(+ΔG): Anabolism (creation)
8.1 What Physical Principles Underlie Biological Energy
Transformations?

In principle, chemical reactions can run in

both directions.

Forward and reverse reactions are

balanced.
A B
The concentrations of A and B determine
which direction will be favored.

At chemical equilibrium, ΔG = 0
Recap

• What is the difference between potential energy and

kinetic energy
• What is the difference between anabolism and
catabolism?
• What is the difference between endergonic and exergonic
reactions and the importance of ΔG?
8.2 What Is the Role of ATP in Biochemical Energetics?

Currency of biological energy is ATP

• ATP (adenosine
triphosphate) captures
and transfers free
energy.
• ATP releases a large
amount of energy when
hydrolyzed.
• ATP can phosphorylate,
or donate phosphate
groups to other
molecules.
Figure 8.6 Coupling of Reactions

Exergonic and endergonic reactions are coupled.

8.3 What Are Enzymes?

Catalysts speed up the rate of a reaction.

The catalyst is not altered by the reactions.

Most biological catalysts are enzymes

(proteins) that act as a framework in which
reactions can take place.
8.3 What Are Enzymes?

Activation energy:

Some reactions require energy to start the

reaction - activation energy (Ea).

• Changes the reactants into unstable forms

(higher free energy)—transition state
intermediates.

• Enzymes lower the energy barrier by bringing

the reactants together.
Figure 8.8 Activation Energy Initiates Reactions (Part 1)
Figure 8.8 Activation Energy Initiates Reactions (Part 2)
8.3 What Are Enzymes?

Enzymes:
•Biological catalysts and are
highly specific.

•Reactants are called substrates.

•Substrate molecules bind to the

active site of the enzyme.

•The three-dimensional shape of

the enzyme determines the
specificity.
8.3 What Are Enzymes?
Binding of a substrate to the active site of an
enzyme produces an enzyme-substrate
complex (ES)

E + S → ES → E + P
E = Enzyme, S = Substrate, P = Product

The enzyme may change when bound to the

substrate, but returns to its original form.
Figure 8.9 Enzyme and Substrate
8.3 What Are Enzymes?
• Enzymes lower the energy barrier for reactions.

• The final equilibrium does not change, and ΔG does

not change.
Recap

• Explain how the structure of an enzyme

makes that enzyme specific.

• What is the relationship between an

enzyme and the equilibrium point of a
reaction?
8.4 How Do Enzymes Work?

Enzymes can speed up reactions by several

mechanisms:

1. Orient substrates
2. Induce strain in the
substrate
3. Temporarily add chemical
groups to substrates
Figure 8.11 Life at the Active Site (A)

Enzymes orient substrate molecules, bringing

together the atoms that will bind.
Figure 8.11 Life at the Active Site (B)

Enzymes can stretch the bonds in substrate

molecules, making them unstable.
Figure 8.11 Life at the Active Site (C)

Enzymes can temporarily add chemical

groups to substrates.

Enzyme adds charges to the substrate.

Figure 8.12 Some Enzymes Change Shape When Substrate Binds to Them

Many enzymes change shape when they bind

to the substrate—induced fit.
Figure 8.13 Catalyzed Reactions Reach a Maximum Rate

The rate of a catalyzed reaction depends on

substrate concentration.
At saturation, all enzymes are bound to substrate
—maximum rate.
8.5 How Are Enzyme Activities Regulated?

Thousands of chemical
reactions are
occurring in cells
simultaneously.
The reactions are
organized in metabolic
pathways. Each
reaction is catalyzed
by a specific enzyme.
8.5 How Are Enzyme Activities Regulated?

Enzymes are regulated by inhibitors:

Molecules that bind to the enzyme and
slow reaction rates.
Two kinds:
1. Irreversible inhibition
2. Reversible inhibition
a. Competitive
b. Non-competitive
8.5 How Are Enzyme Activities Regulated?

Irreversible inhibition: Inhibitor covalently

binds to side chains in the active site—
permanently inactivates the enzyme.
8.5 How Are Enzyme Activities Regulated?

Reversible inhibition:
a) Competitive inhibitors compete with
the natural substrate for binding sites.
When concentration of competitive
inhibitor is reduced, it detaches from the
active site.
b) Noncompetitive inhibitors: Bind to the
enzyme at a different site (not the active
site).
The enzyme changes shape and alters the
active site.
Figure 8.16 Reversible Inhibition (A)
8.5 How Are Enzyme Activities Regulated?

Effect of pH & temperature on enzyme activity:

• pH influences the ionization of functional
groups.
• Every enzyme has an optimal temperature. At high
temperatures, non-covalent bonds begin to break.
Enzyme can lose its tertiary structure and become
denatured.