Chapter 8:

An Introduction
to Metabolism

Important Point:

Metabolism (Overview)

Metabolism = Catabolism + Anabolism

Catabolic reactions are energy yielding

They are involved in the breakdown of
more-complex molecules into simpler
ones
Anabolic reactions are energy requiring
They are involved in the building up of
simpler molecules into more-complex
ones
We can consider these bioenergetics in
terms of the physical laws of
thermodynamics

1st & 2nd Laws of Thermodynamics

Energy can be
transferred or
transformed but neither
created nor destroyed.
p. 143, Campbell & Reece (2005)

Every energy transfer or

transformation increases the
disorder (entropy) of the
universe. p. 143, Campbell & Reece (2005)
Note especially the waste heat

Organisms are Energy Transducers

Organisms take in energy & transduce it to new

forms (1st law)
As energy transducers, organisms are less than
100% efficient (2nd law)
Organisms employ this energy to:
Grow
Protect Themselves
Repair Themselves
Compete with other Organisms
Make new Organisms (I.e., babies)
In the process, organisms generate waste
chemicals & heat
Organisms create local regions of order at the
expense of the total energy found in the
Universe!!! We are Energy Parasites!

Water Fall Analogy

Get it?

Laws of Thermodynamics

First Law of Thermodynamics:

Energy can be neither created nor destroyed

Therefore, energy generated in any system is

energy that has been transformed from one state
to another (e.g., chemically stored energy
transformed to heat)

Second Law of Thermodynamics:

Efficiencies of energy transformation never equal

100%

Therefore, all processes lose energy, typically as

heat, and are not reversible unless the system is
open & the lost energy is resupplied from the
environment

Conversion to heat is the ultimate fate of

chemical energy

Movements Toward Equilibrium

Increase
stability

Downhill

G < 0

Greater
entropy

Entropy!

Free Energy & Spontaneity

What is the name
of this molecule?

Movement Toward Equilibrium

Work
Potential
energy

Equilibrium
Spontaneous

Forward
reaction

Movement Toward Equilibrium

Viable organisms exist in a
chemical disequilibrium that
is maintained via the
harnessing of energy
obtained from the
organisms environment
(e.g., you eat to live)

Waterfall Analogy

Potential Energy

Kinetic Energy
Stayring of a turbine
generator, Priest Rapids
Dam, 1958

Gravity (center Earth)

Waste Heat
(once reaches
Bottom)

Movement Toward Equilibrium

Food

Potential
energy

Forward
reaction

Spontaneous

Waste
heat

Work

Movement Toward Equilibrium in Steps

Note that Spontaneity is not

a measure of speed of a
process, only its direction

Exergonic Reactions
Food
Energy
released

Movement toward
equilibrium

Endergonic Reactions
Work
Energy
required

Exergonic Reaction (Spontaneous)

Decrease in Gibbs free energy (-G)
Increase in stability
Spontaneous (gives off net energy upon going forward)
Downhill (toward center of gravity well, e.g., of Earth)
Movement towards equilibrium
Coupled to ATP production (ADP phosphorylation)
Catabolism

Endergonic Rxn (Non-Spontaneous)

Increase in Gibbs free energy (+G)
Decrease in stability
Not Spontaneous (requires net input of energy to go forward)
Uphill (away from center of gravity well, e.g., of Earth)
Movement away from equilibrium
Coupled to ATP utilization (ATP dephosphorylation)
Anabolism

Coupling Reactions

Minus the
cut for the
2nd law

Exergonic
reactions can
supply energy
for endergonic
reactions

Energy Coupling in Metabolism

Catabolic reactions provide the energy that

drives anabolic reactions forward

Catabolic
reaction

Anabolic
reaction

Adenosine Triphosphate (ATP)

Call this A

Energy Coupling via ATP

Hydrolysis of ATP

Movement
toward
equilibrium

Coupled Reactions

How that reaction really works

Various Pi Transfers

Summary of Metabolic Coupling

Endergonic
reaction
Exergonic
reaction

Exergonic
reaction
Endergonic
reaction

Get it? Exergonic processes drive Endergonic processes

Movement Toward Equilibrium

Food

Exergonic
Endergonic

Coupling the Biosphere

Anabolic
process

Catabolic
process

Chemically
stored energy

Enzyme Catalyzed Reaction

Question: Is
this reaction
endergonic or
is it exergonic?

Enzyme

Activation Energy (EA)

Anything that
doesnt require
an input of
energy to get
started has
already
happened!

Low- (i.e., body-) Temp. Stability

Why don't energy-rich molecules, e.g., glucose,

spontaneously degrade into CO2 and Water?

To be unstable, something must have the

potential to change into something else,
typically something that possesses less free
energy (e.g., rocks)

To be unstable, releasing somethings ability to

change into something else must also be
relatively easy (i.e., little input energy)

Therefore, stability = already low free energy

Alternatively, stability = high activation energy

Things, therefore, can be high in free energy

but still quite stable, e.g., glucose

Catalysis

Lowering of
activation
energy

Catalysis

At a given
temperature,
catalyzed reactions
can run faster
because less energy
is required to achieve
the transition state

This is instead of
adding heat; heat is
an inefficient means
of speeding up
reactions since it
simply is a means of
increasing the
random jostlings of
molecules

Enzyme-mediated Catalysis

= Subtle
application
of energy

Mechanisms of Catalysis

Active sites can hold two or more

substrates in proper orientations so that
new bonds between substrates can form
Active sites can stress the substrate into
the transition state
Active sites can maintain conducive
physical environments (e.g., pH)

Active sites can participate directly in the

reaction (e.g., forming transient covalent
bonds with substrates)
Active sites can carry out a sequence of
manipulations in a defined temporal order
(e.g., step A step B step C)

Catalysis as Viewed in 3D

Active site is
site of
catalysis

The rest of an
enzyme is involved
in supporting active
site, controlling
reaction rates,
attaching to other
things, etc.

Induced Fit (Active Site)

Induced fit not only allows the enzyme to bind

the substrate(s), but also provides a subtle
application of energy (e.g., bending chemical
bonds) that causes the substrate(s) to
destabilize into the transition state

Enzyme Saturation

Enzyme Activity at Saturation is a

Function of Enzyme Turnover Rate

Enzyme Saturation
Turnover rate

Non-Specific Inhibition of Enzyme Activity

Reduced rate of
chemical
reaction
Reduced
enzyme fluidity

Turnover
rate
Change in
R group
ionization

Instability
& shape
change
(too fluid)
Denatured?

Change in
R group
ionization
Even at saturation, rates
of enzymatic reactions
can be modified

Activators of Catalysis
Metal Ion or =
Organic Molecule

Dont worry about

apoenzyme and
holoenzyme

= Organic
Cofactor
Polypeptide

Specific Inhibition

Competitive
inhibitors can
be competed
off by
supplying
sufficient
substrate
densities

Non-competitive
inhibitors cannot
be competed off
by substrate

Allosteric Interactions

Reversible
interactions,
sometimes
on,
sometimes
off, dependent
on binding
constant and
density of
effector

Cooperativity
Cooperativity
is when the
activity of
other
subunits are
increased by
substrate
binding to
one subunits
active site

Feedback Inhibition

Energy-Metabolism Regulation

Enzyme Localization

Organization of
Electron
Transport
Chain of
Cellular
Respiration:
Substrate
Enzyme
Product
Enzyme chains
are co-localized

Enzymes in single pathway

may be co-localized so that
the product of one enzyme
increases the local
concentration of the substrate
for another

The End