Introduction to Metabolism

Lessons connected to chap. 6 in Campbell et al,

”Biology” – 10. eds. 2015/ 2018 Global eds.,
2. February 2018 /Åge Eirik Mohus
 Kinetic and potential energy

The forms of
energy change:
from potential
to kinetic - to
heat…
… or from
chemical to
heat..

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 A mind-map for this lesson (you ought to make your own..)

i læreboka små trinn

Oppgaver/spørsmål Biokjemiske spor
på nett metabolsk nettverk

feed-back systemer Gibbs fri energi, G

allosteriske enzymer Kontroll totalenergi (entalpi), H
Fri energi
separate rom (orden) entropi, S
termodynamiske lover
Energi og liv
globulære proteiner
spesifikke nukleotid
katalyserer ATP-syklus
Enzymer
senker aktiveringsenergi ATP kopler reaksjoner
substrater energiformidler
inhibitorer +/- 7,3 kcal pr. mol

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 Overview
• The Energy of Life

• The Living Cell

– is a miniature factory where thousands of reactions
occur
– converts energy in many ways

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 Organization of the Chemistry of Life into
Metabolic Pathways

• A metabolic pathway has many steps

– that begins with a specific molecule and ends
with a product
– that are each 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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 Figure 6.1 The complexity of metabolism

The processes of
life are organized
in biochemical
pathways

An important
splitting of
metabolism: the
catabolic pathways
and the anabolic
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 Catabolism

• Catabolic pathways
– break down complex molecules into simpler
compounds
– release energy

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Anabolism

• Anabolic pathways
– build complicated molecules from simpler ones
– consume energy

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 Forms of Energy

• Energy
– is the capacity to cause change
– exists in various forms, of which some can
perform work

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 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

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 Energy is converted between forms
• Energy can be converted
– from one form to another
On the platform, a diver Diving converts potential
has more potential energy. energy to kinetic energy.

Climbing up converts kinetic In the water, a diver has

energy of muscle movement less potential energy.
Figure 8.2 to potential energy.

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 The Laws of Energy Transformation

• Thermodynamics
– is the study of energy transformations

• Concept 6.1: An organism’s metabolism

transforms matter and energy, subject to the
laws of thermodynamics

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 The First Law of Thermodynamics

• According to the first law of thermodynamics

– energy can be transferred and transformed
– energy cannot be created or destroyed

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 An example from biology
• An example of energy conversion

Chemical
energy

(a)
First law of thermodynamics: Energy
can be transferred or transformed but
Neither created nor destroyed. For
example, the chemical (potential) energy
in food will be converted to the kinetic
energy of the cheetah’s movement in (b).
Figure 8.3

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 The Second Law of Thermodynamics
• According to the second law of thermodynamics
– spontaneous changes that do not require outside energy, increase
the entropy (or disorder) of the universe

Heat
co2

+
H2O

(b)
Second law of thermodynamics: Every energy transfer or transformation increases
the disorder (entropy) of the universe. For example, disorder is added to the cheetah’s
surroundings in the form of heat and the small molecules that are the by-products
of metabolism.
Figure 8.3
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 Figure 6.3 Two laws of thermodynamics

The two important thermodynamical laws tell us that:

1. The amount of energy is conserved – only the forms
of energy will change
2. Energy transformations will affect the degree of order
(entropy)

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 Biological Order and Disorder
• Living systems
– increase the entropy of the universe
– use energy to maintain order
50µm

Figure 8.4

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 Free-Energy Change, ∆G

• A living system’s free energy (G)

– is energy that can do work under cellular
conditions

• Concept 6.2: The free-energy change of a

reaction tells us whether the reaction occurs
spontaneously

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 Free-Energy Change, ∆G

• The change in free energy, ∆G, during a

biological process
– is related directly to the enthalpy change (∆H)
and the change in entropy

∆G = ∆H – T∆S

( ∆H = ∆G + T∆S )

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Figure 6.5 The relationship of free energy to stability, work capacity, and
spontaneous change

∆G = ∆H – T∆S
∆G = G (end condition) – G (start condition)

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 Free Energy, Stability, and Equilibrium

• Organisms live at the expense of free energy

• During a spontaneous change
– free energy decreases, and the stability of a
system increases

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 Figure 6.6 Energy changes in exergonic and endergonic reactions

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 Figure 6.7 Disequilibrium and work in closed and open systems

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 The Structure and Hydrolysis of ATP
• ATP (adenosine triphosphate)
– Is the cell’s energy shuttle
– Provides energy for cellular functions

Adenine NH2

N C
C N
O O O HC
CH
C
-O O O O CH2
O
N
N

O - O - O -
H H

Phosphate groups H H Ribose

Figure 8.8 OH OH

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 Splitting of ATP
• Energy is released from ATP
– When the terminal phosphate bond is broken

P P P

Adenosine triphosphate (ATP)

H2O

P i
+ P P Energy

Figure 8.9 Inorganic phosphate Adenosine diphosphate (ADP)

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 Energy coupling
• A cell does three main kinds of work:
– Mechanical
– Transport
– Chemical

• Concept 6.3: ATP powers cellular work by

coupling exergonic reactions to endergonic
reactions
• Energy coupling
– Is a key feature in the way cells manage their
energy resources to do this work
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 ATP and reaction coupling
• ATP hydrolysis
– Can be coupled to other reactions
Endergonic reaction: ∆G is positive, reaction
is not spontaneous

NH2

+ NH3 ∆G = +3.4 kcal/mol

Glu Glu
Glutamic Ammonia Glutamine
acid

Exergonic reaction: ∆ G is negative, reaction

is spontaneous

ATP + H2O ADP + P ∆G = –7.3 kcal/mol

Coupled reactions: Overall ∆G is negative;

Figure 8.10 together, reactions are spontaneous ∆G = –3.9 kcal/mol
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 Figure 6.9 Energy coupling by phosphate transfer

ATP transfers
phosphate and
thereby
delivers a
package og
free energy…

… and the
reaction will
proceed!

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 How ATP Performs Work

• ATP drives endergonic reactions

– By phosphorylation, transferring a phosphate
to other molecules

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 The Principle Side of Cellular Work
• The three types of cellular work: mechanical, transport, chemical
– are all powered by the hydrolysis of ATP

P i
P

Motor protein Protein moved

(a) Mechanical work: ATP phosphorylates motor proteins

Membrane
protein
ADP
ATP +
P i

P P i

Solute Solute transported

(b) Transport work: ATP phosphorylates transport proteins

P
NH2
Glu + NH3 + P i
Glu

Reactants: Glutamic acid Product (glutamine)

and ammonia made

Figure 8.11 (c) Chemical work: ATP phosphorylates key reactants

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 The Regeneration of ATP
• Catabolic pathways
– Drive the regeneration of ATP from ADP and
phosphate
ATP synthesis from ATP hydrolysis to
ADP + P i requires energy ADP + P i yields energy

ATP
Hvilken rolle har ADP i
stoffskiftet?

Energy from catabolism Energy for cellular work

(exergonic, energy yielding (endergonic, energy-
processes) consuming processes)
ADP + P i
Figure 8.12

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 Enzymes

• A catalyst
– is a chemical agent that speeds up a reaction
without being consumed by the reaction

• An enzyme
– is a catalytic protein

Concept 6.4: Enzymes speed up metabolic

reactions by lowering energy barriers

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Figure 6.11 Example of an enzyme-catalyzed reaction: Hydrolysis of sucrose

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 The Activation Barrier

• Every chemical reaction between molecules

– involves both bond breaking and bond forming

• The activation energy, EA

– is the initial amount of energy needed to start a
chemical reaction
– is often supplied in the form of heat from the
surroundings in a system

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 Figure 6.12 Energy profile of an exergonic reaction

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 Figure 6.13 Enzymes lower the barrier of activation energy

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 Substrate Specificity of Enzymes

• The substrate
– Is the reactant an enzyme acts on

• The enzyme
– Binds to its substrate, forming an enzyme-
substrate complex

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 The Active Site of an Enzyme
• The active site
– is the region on the enzyme where the
substrate binds

Substate

Active site

Enzyme

Figure 8.16 (a)

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 Figure 6.14 The induced fit between an enzyme and its substrate

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 Enzymatic catalysis
• The catalytic cycle of an enzyme
1 Substrates enter active site; enzyme
changes shape so its active site 2 Substrates held in
embraces the substrates (induced fit). active site by weak
interactions, such as
hydrogen bonds and
ionic bonds.

3 Active site (and R groups of

Substrates Enzyme-substrate its amino acids) can lower EA
complex and speed up a reaction by
• acting as a template for
substrate orientation,
6 Active site • stressing the substrates
Is available for and stabilizing the
two new substrate transition state,
Mole. • providing a favorable
microenvironment,
Enzyme
• participating directly in the
catalytic reaction.

5 Products are
Released. 4 Substrates are
Converted into
Figure 8.17 Products Products.
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 Figure 6.16 Environmental factors affecting enzyme activity

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 Figure 6.17 Inhibition of enzyme activity

Competitive inhibition:
when substrate and
inhibitor compete for
binding to the active site

Non-competitive
inhibition: when an
inhibitor binds to the
enzyme on a site different
from the active site (to a
regulator site)

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 Regulation and control

• A cell’s metabolic pathways

– must be tightly regulated

• Concept 6.5: Regulation of enzyme activity

helps control metabolism

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 Allosteric Regulation of Enzymes

• Allosteric regulation
– is the term used to describe any case in which
a protein’s function at one site is affected by
binding of a regulatory molecule at another site

• Many enzymes are allosterically regulated

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 Figure 6.19 Feedback inhibition

Negative feedback as
metabolic regulation:
Here it is shown how
important non-
competitive inhibition
is for ”order” in the
metabolic pathways!

It is also called
allosteric regulation.
(Are you now able to
explain these difficult
terms?)
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 Figure 6.21 Organelles and structural order in metabolism

Different shelfs
and rooms create
order – so also in
cells!

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