10/13/2014

Life Sciences 2
Lecture 4
Energy, Enzymes, and Metabolism

Energy, Enzymes, and Metabolism

In living organisms, thousands of enzyme
catalyzed reactions occur
Catalysis occur due to the 33-D
D shape of the
proteins involved
Metabolism is the combination of all of
these reactions

Enzymes and Energetic

Energy and the Laws of Thermodynamics

Chemical Reactions and Equilibrium
Reaction Rates and the Energy Barrier
Enzymes

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Energy and the Laws of

Thermodynamics
Bioenergetics is the flow of energy in
biochemical systems
Energy is defined as the capacity to do work
Forms of Energy: Heat, light, electrical, and
chemical

Energy and the Laws of

Thermodynamics
Energy can be considered as one of two
basic types:
Kinetic Energy
Potential Energy

Energy and the Laws of

Thermodynamics
Kinetic energy
is the energy
associated with
motion

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Energy and the Laws of

Thermodynamics
Potential
energy is the
energy
gy of state
or position

Energy and the Laws of

Thermodynamics
Energy before and
after transformation is
equal

After energy
transformation The
amount of energy
available to do work is
less.

Energy and the Laws of

Thermodynamics
With repeated energy transformations
usable energy decreases and unusable
energy increases.

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Energy and the Laws of

Thermodynamics
With repeated energy transformations
usable energy decreases and unusable
energy increases. (Entropy)
This occurs in a closed system.

Energy and the Laws of

Thermodynamics

In a closed system, no energy or matters

enters or leave

Energy and the Laws of

Thermodynamics
First law: within closed systems energy is
neither destroyed nor created
No change in quantity
Not all energy can be used. The usable
portion of energy is decreasing
Quality of energy changes

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Energy and the Laws of

Thermodynamics
Open systems can be part of larger closed
system
An open system can increase its order and
complexity using free energy from the
closed sytem
Where does living matter gets its energy
from?

Definitions:
G = H- TS
Usable
energy

Unusable
energy

Enthalpy (H): Total Energy of the System

Entropy (S): Amount of disorder in the System
Free Energy (G): Amount of Useable Energy
Temperature(T): Amplifies entropy of the system

Applying the second law of thermodynamics:

Reactions spontaneously go from high levels of
useful energy (G) to low level of useful energy
G tends to decrease.
decrease S tends to increase.
increase
H is constant, but the quality changes
All things tend towards disorder

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Diffusion

Less Entropy (S)

Order

More Entropy
Disorder

Chemical Reactions Release or

Take Up Energy
Exergonic Reaction: release of energy

Endergonic Reaction: uptake of energy

Chemical Reactions Release or Take Up Energy

Starch

Glucose

Starch

Glucose

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Chemical Reactions Release or Take Up Energy

Glucose

CO2

Glucose

CO2

Exergonic Reaction:
Energy is released as the reaction proceeds to
form products. G is negative

Ball has potential energy. When releases it rolls

down the hill spontaneously. Its Energy decreases.

Exergonic Reaction:
Spontaneous reaction, that goes to completion over
time without any energy input. It releases energy
by breaking bonds.
G product < G reactant ==> G is negative
Glucose +O2 -> 6 CO2 + H2O + energy
The energy produced can be used to form ATP, but
some is lost as heat.
Entropy increases, usually in the form of heat or
light

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Endergonic Reaction:
A reaction that requires input of free energy to
proceed. It is NOT spontaneous.
G reactant < G product ==> G is positive
ADP + Pi -> ATP
Glucose + Glocuse + -> Glycogen

Exergonic Reaction:

Chemical Equilibrium and Free Energy are

related
All chemical reactions are reversible
A-->B ((forward reaction))
A<--B (reverse reaction)
Chemical equilibrium occur when rate of the
forward reaction and the rate of the reverse
reaction is equal.

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Gl
Glucose
11-Phospahe
Ph
h <
<-->
> Glucose
Gl
6 Ph
Phospahe
h
When the reaction reaches equilibrium there
will be 0.001 M G1-P and 0.019 M G6-P
Keq = 0.19/0.01= 19
Keq= [Products]/[Reactants]

Equilibrium Constant:
Keq is the ratio of products and reactants at
equilibrium.
High
g value means that reaction ggoes to
completion

Rate of a reaction:
Is equal to the product of the rate constant
and the concentration of the reactant
A->B
Rate of reaction is Kf x [A]
Each molecule of A is converted to B at rate
Kf. This rate is specific to the reaction

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Equilibrium in a reaction exists when the rate

of the forward reaction equals the rate of the
reverse reaction
Kf A->B = Kr B->A

G and Equilibrium:
Keq >1 more products than reactants. This is an
exergonic reaction with a negative G
Keq <1 more reactants than products. Therfore,
the reverse reaction dominates and it is an
endergonic reaction with a positive G

Conclusion:
Keq = [G6-p]/[G1-p] = 0.019/0.001 = 19
This reaction goes to the right = forward (to
completion (exergonic).
For complex reactions:
A+B <--> C+D
Keq= [C] x [D]/[A] x[B]

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Reaction Rates and the Energy Barrier

Thermodynamics: relates to G. This
determines the direction but not the speed of the
reaction
Kinetics: describes the rate of the reaction
Glucose +O2 -> 6 CO2 + H2O + energy
G = -686 kcal/mole

Sugar + Oxygen

Sugar + Oxygen

No reaction will happen.

Sugar + Oxygen

Heat + CO2

+ Spark
(Activation Energy Ea)

Activation Energy
Even though some chemical reactions have
a negative G, they can not proceed
without an aid
G determines the direction of a reaction
but not its rate
To initiate a reaction, Ea is needed

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Activation Energy

Reaction Rates are affected by motion of

molecules to go from reactant to product
Activation Energy is the amount of energy
required to push the reactant to proceed and
overcome the energy barrier
Rate constant (Kf or Kr) is related to the
activation energy barrier

The rate of the reaction depends on the

activation energy. How can we increase the
reaction rate?

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Add heat: This will increase the motion of the

motion of the molecules.
Increase the concentration of the reactants.
Lower the activation energy: Biological
systems use protein catalysts (enzymes) to
lower activation energy and speed the reaction
rate (this does not change G).

What is a catalyst?
When oxygen and sulfur dioxide are mixed in
the presence of a filament of platinum, they
from sulfurous acid. This combination takes
place
l
only
l if the
th platinum
l ti
is
i present;
t
nevertheless the newly formed acid contains no
trace of platinum and the platinum itself is
unaffected and unchanged

Enzymes:
Cells can control the speed of reactions by using
protein catalysts called enzymes.
Enzymes enhance
E
h
the
th speed
d off bi
biochemical
h i l
reactions

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Substrate fits precisely into the active site

Nonsubstrate does not

Enzymes is a protein with a binding site capable of

binding one or substrate molecules

Enzymes:
The enzymes are not changed
They alter the rate of the reaction
They do not change G
They lower the activation energy of the reaction

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Enzymes have different ways of causing their

substrate to enter the transition state

Specificity of the enzyme for the substrate is

determined by the proteins tertiary structure

Hexokinase

An enzyme binds to a substrate at the active site

to form enzyme-substrate complex

The fit of a substrate to the enzyme is highly

specific based on shape, H-bonds, hydrophobic
interactions

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Which substrate-enzyme binding mechanism is

this?

Enzymes catalyze reactions at very specific

conditions:

Enzymes catalyze reactions at very specific

conditions:

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Reaction rate levels off when enzymes are

saturated

Have you seen this before?

is reached when all carriers are saturated

How are enzymes regulated?

Cofactors: Copper or zinc are essential for
enzyme functioning
Coenzymes: organic molecules required for the
action of certain enzymes (NAD, FAD)
Prosthetic groups: Permanently bound to
enzymes (heme groups)

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How are enzymes regulated?

Inhibitors
Feedbackloops
Allosteric regulation

Enzymes can be inhibited

Reversible inhibition

Enzymes can be inhibited

Reversible inhibition

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Enzymes can be inhibited

Reversible inhibition

Enzymes can be inhibited

Reversible inhibition

Enzymes can be inhibited by feedback

control:
A-->B-->C-->D
D the final product inhibits the enzyme that
catalyzes the reaction A-->B

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Enzymes can be inhibited by

Allosteric Control:
Off

On

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