BIOENERGETICS:

The Flow of Energy in the Cell

Department of Biochemistry

BIOENERGETICS
Objectives:
State the laws of thermodynamics and how energy is
transferred between molecules
Describe how enzymes function and are controlled
during biochemical pathways
Describe how ATP is used to store and transfer energy

Energy
Ability to cause specific changes
Needed to drive chemical reactions involved in
the formation of cellular components and to
power the many activities that those
components carry out.

Energy
What are some of the reasons that cells require
energy?

Energy
From where do organisms get the energy they
need?

Chemical Energy
Energy released when organic and inorganic
compounds are oxidized
Measured in terms of:
Kilocalories (kcal)
Kilojoules (kJ)
1 kcal = 4.184 kJ

BIOENERGETICS
Energy
Types of
Kinetic- energy of motion
Potential- energy stored

Forms of
Electrical, nuclear, wind, sound, etc.
Three most common in living systems are light, chemical,
and heat

Kinds of Energy Changes

1. Synthetic Work

Changes in chemical bonds

2. Mechanical Work

Changes in the location or orientation of a cell or a

subcellular structure
3. Concentration Work

Movement of molecules across a membrane against

concentration gradient
4. Electrical Work

Movement of ions across a membrane against an

electrochemical gradient

Continued..
5. Heat
An increase in temperature that is useful to warm
blooded animals

6. Bioluminescence
The production of light

Deductions
Most organisms obtain energy either from
sunlight or from organic food molecules
Energy flows through the biosphere
continuously
The flow of Energy through the biosphere is
accompanied by a flow of matter

Bioenergetics
Concerns the application of thermodynamic
principles to reactions and processes in the
biological world

BIOENERGETICS
Thermodynamics
Unit of energy is the calorie (c) = amount of energy to
raise the temp. of 1 gram (1 cm3) of water 1 Celsius
degree.
C (used by nutritionists) = kilocalorie
1000 grams (1 liter) of water

BIOENERGETICS
Oxidation/Reduction
If electrons are transferred in a chemical reaction,
any atom/molecule that loses electrons is said to be
oxidized.
(oxygen is usually the atom that pulls electrons away from
other atoms/molecules)
..any atom that gains electrons is said to be reduced.

BIOENERGETICS
REDOX (cont.)
Memory aid LEO goes GER
Lose Electrons OxidizedGain Electrons Reduced
if an electron is transferred from one level to another, it will gain energy if it
ends up in a higher energy level in the new atom.

ee-

Bioenergetics
What does the first law of thermodynamics say?
What do we mean by the internal energy of a
system?
energy stored = energy in energy out

LAWS OF THERMODYNAMICS
First law of thermodynamics- also known as
laws of conservation of energy states that
energy can neither be created or destroyed, one
form of energy can be converted to another
form but the total amount of energy remains
constant

First Law of Thermodynamics

Energy is neither created nor destroyed. It can
only change from one form to another.
Energy out

= Energy in

Energy stored

BIOENERGETICS
Free energy
Energy in chemical bonds (free energy) = G
Energy within a cell available to do work =H
Temperature = T
G = H TS
Change in free energy

G = H T S (see Fig 8.4)

Positive G reactions
products contain more free energy than reactants
Negative
G reactions
Products contain less free energy than reactants

BIOENERGETICS IS THE STUDY OF

ENERGY CHANGES IN A BIOCHEMICAL
REACTION

Bioenergetics
What is enthalpy and how is it related to internal
energy?
H = E + PV or H = E + PV
What happens to H in an exothermic reaction?
an endothermic reaction?

Bioenergetics
What does the second law of thermodynamics
tell us?
For what purpose do cell biologist make use of
this law?

Second law of thermodynamicsTotal entropy of the system must increase if a

process is to occur spontaneously

Second Law of Thermodynamics

In

every physical or chemical change, the universe

always tends toward greater disorder or
randomness.

Restatement of Second Law

All

processes or reactions that occur

spontaneously result in an increase in the total
entropy of the universe.

third law of thermodynamics- the entropy of

the perfect crystals of a compound rises with in
temperature from a minimum or 0 value

Bioenergetics
What is the relationship between entropy and
thermodynamic spontaneity?
How can the order within a cell or the entropy of
a reaction decrease?

Bioenergetics
To determine whether a particular reaction will
take place in a cell we use the concept of free
energy.
What is the relationship between the change in
free energy, enthapy and entropy?
G = H - TS

Free Energy
Energy released that is available to do useful
work.

Free Energy Change (G)

The free energy change (G) of a reaction
determines its spontaneity.
A reaction is spontaneous if G is negative (if
the free energy of the products is less than
the free energy of the reactants).

Bioenergetics

Bioenergetics
How can we determine from the value of G
whether a reaction will occur spontaneously?
What enables us to characterize reactions as
endergonic or exergonic?

GIBBS FREE ENERGY CHANGE[G]expresses the total amount of energy capable

of doing work, during a reaction with constant
temperature and pressure
G = H - T S

If G is negative then the reaction is said to be

exergonic reaction
If G is zero the system is at equilibrium.
If G is positive the reaction proceeds only
with the free energy being gainedendergonic . it posses low equilibrium
constants

ENTHALPY
-is the heat content of the reacting system.
H= E+P V
Similarly H is negative reaction may be
exothermic.
If H is positive reaction is endothermic,
if H is zero the reaction is isothermic
The units of G &H are joules/mole or calorie/mole

ENTROPY
Is a qualitative expression for the randomness
and disorder in a system
When the product of the reaction is less
complex & more disordered than the reactant it
is said to proceed with a gain in entropy.
The units of entropy are joules/mole.kelvin

STANDARD FREE ENERGY CHANGE

When the reactant and the products are present
in a concentration of 1mol /l it is known as
standard free energy change - G

For a biochemical reaction ,a standard state

is defined as having a ph of 7 ,temp 25
deg pressure at 1 atm and reactant and
products at 1 mol conc- standard
transformed constants G

Standard free energy change differentiated

from actual free energy change
G is measured under standard conditions
stated above & has the constant value for given
reaction
where as G is measured at the conditions
prevailing during the reaction, such as the
conditions of the concentration, pH &
temperature which are not standard.

Relationship between the G & G

The actual free energy change & the G of a
chemical reaction A B are related to each
other.
G = G + RT log (B) / (A)
Where T is the absolute temperature measured
in Kelvin, R is a gas constant, & (A) (B) are the
actual concentrations of the reaction substrate &
product respectively

The standard free energy change is related

to the equilibrium constant
In a reversible chemical reaction A B,
In this state no net chemical transformation
occurs, so that equilibrium concentration of the
both A & B are invariable, their ratio is termed as
equilibrium constant. (Keq)
Keq= (B) / (A)

At equilibrium G = 0
Therefore G = G + RT log Keq
0 = G + RT log Keq
G = - RT log Keq
When Keq = 1, log Keq = 0 hence G = 0
The product contains the same amount of free
energy as the reactant. Therefore reaction
stands at equilibrium

Keq

The reaction

>1.0

negative

1.0

zero

Proceeds
forward
Is at
equilibrium

<1.0

positive

Proceeds in
reverse

Standard free change of a reaction catalyzed by

enzymes
Ex: glucose-1-phosphate glucose-6-phosphate
(enzyme phosphoglucomutase)
Keq = (glucose-6-phosphate) / (glucose-1phosphate)
= 19mM / 1mM = 19
from this value of equilibrium constant we can calculate
the standard free energy change
G = - RT log Keq
= - (8.315)(298)(19)
= - 7.3KJ/mol

Standard free energy changes are additive

In case of two sequential reactions, A B & B
C. each reaction has its own equilibrium
constant & its own standard free energy change
(1)
A B
G1
(2)
BC
G2
SUM A C
G1 + G2

Ex: glucose + Pi glucose 6- phosphate +

H2O
G = 13.8 kJ/mol
The hydrolysis of ATP to ADP is exergonic.
ATP + H2O ADP + Pi
G = -30.5 kJ/mol

These 2 reactions share the common

intermediates Pi & H2O may be expressed as a
sequential reaction.
ATP+ glucose ADP + glucose-6-phosphate
G total = G1 + G2
= 13.8 + (-30.5)
= -16.7 kJ/mol
the overall reaction is exergonic

Bioenergetics

Bioenergetics
How can we use the equilibrium constant to
determine whether a reaction can occur in a
specific direction?
Keq = [product]eq/[reactant]eq for
glucose-6-PO4

fructose-6-PO4

Keq = [fructose-6-PO4]eq/[glucose-6-PO4]eq = 0.5

Bioenergetics
reactions proceed toward equilibrium

Bioenergetics
How do we actually calculate G?
aA + bB
cC + dD
G = -RTlnKeq + RT ln [C]c[D]d/[A]a[B]b
R = 1.987 cal/mol-oK
T at 25oC = 298oK

Bioenergetics
What is the difference between G and Go?
How does this affect the actual calculation?
since Go = - RT ln Keq
G = Go + 592 ln [C]c[D]d/[A]a[B]b

Bioenergetics

Bioenergetics
How does the cell biologist use the value of G ?

BIOENERGETICS
Activation energy:
Energy required to break bonds so new bonds can be
created
Match/spare to light a fire
Rate of rxn depends on the amount of act. E necessary
Ex. If AE is large reaction will proceed slowly

BIOENERGETICS
Catalysis:
process of putting stress on bonds to get the
bonds to break more easily

Will this increase, decrease the reaction

time/rate????

Catalysts
Enzymes

Chemical reactions within organisms are

regulated by catalysts
Most of the catalyst agents are enzymes

Some catalysts are RNA

Enzymes (type of protein) bind to a

molecule (substrate) stressing bonds
Brings reactants together correctly, or
stresses chemical bonds
Stresses break bonds easily decreasing
activation energy

Enzymes

Lets look at an example of the effect of

enzymes:
CO2 + H2O = H2CO3 (carbonic acid in
vertebrate RBC)

Without enzymes, a cell produces about

200 molecules in an hour, not useful to
cell.
With an enzyme called carbonic
anhydrase, a cell can produce 600,000
molecules every second!

Enzymes

In this example the enzyme increases the

reaction 10 million times!
Almost all enzymes end with what three
letters?

ase

A very important fact of enzymes are they

are not consumed in the reaction

Enzymes

How do enzymes work?

What type of question is this, proximate or

ultimate?

Enzymes bind to a molecule at the active

site and form an enzyme-substrate complex
Amino acid side groups of enzyme interact
chemically w/ substrate stressing or
distorting particular bond, lowering the
activation energy.
This interaction may facilitate the binding
of other substrates

Factors Affecting Enzymes

The rate of an enzyme-catalyzed

reaction is affected by:
Concentration of substrate
Concentration of enzyme
Temperature
Salt
pH
Inhibitors/activators

Enzymes

Concentrations are easily understood

Temperature:

pH:

increase in temperature increases reaction rate more flexible

Up to certain point, temperature optimum
Above To, enzyme denatures
most enzymes are optimized at a pH (optimum)
between 6-8 (salt is similar)

Inhibitor:

molecule binds to an enzyme decreasing its activity

Enzymes

Inhibitor
Competitive: compete w/ substrate
Noncompetitive: bind to allosteric site and
turn off, change shape

Activators - bind to allosteric sites but

dont turn them off, actually increase
enzyme activity
Enzymes often assisted by cofactors

BIOENERGETICS
Catalysts = chemicals that catalyze rxns
Cannot violate the Laws of Thermodynamics
Accelerates the rxn both forward and backward
Direction of rxn depends on

BIOENERGETICS
Enzymes (organic catalysts)
1. Usually are proteins (RNA) with specialized shapes
2. Permit temporary associations with reactants
3. Act by lowering the A.E. required for rxn
Bring two reactants together in the correct orientation
Stress particular bonds of a substrate

4. Example: formation of carbonic acid from CO2 and water

1.
2.
3.
4.

Reaction proceeds in either direction

Reaction is slow because of a great activation energy
Carbonic anhydrase: enzyme speeds reaction
Enzymes given the name of their substrate w/ ase

BIOENERGETICS

BIOENERGETICS
Enzymes (cont.)
Thousands of enzymes exist
Each enzyme is specific for the substrate it acts on
Lock and Key hypothesis

Different cells will contain a different complement of

enzymes

BIOENERGETICS
Enzyme function
Globular proteins contain surface clefts called active sites
Enzymes are specific for their substrates
Intermediate is enzyme-substrate complex
The substrate must fit precisely into the active site
Amino side groups of the enzyme react w/ substrate
Bond is stressed or distorted, then the A.E. is decreased

Substrate binding causes enzyme to slightly change shape

induced fit hypothesis
substrate may act as an activator

BIOENERGETICS

BIOENERGETICS
Factors affecting enzyme activity
1. Temperature
a. Lower temps. dont allow enough flexibility for the enzyme to
change shape as easily
b. Higher temps. tend to weaken bonds and break themdenaturing the enzyme

BIOENERGETICS
2. pH
a. many amino acids (glutamic acid, lysine, etc) making up
enzymes have charged side groups. These often aid
enzymes bonding with their substrates.
Any pH changes would interfere with the interaction of the enzyme and substrate bonding.

BIOENERGETICS

BIOENERGETICS
3. Inhibitors and Activators
a. competitive inhibitors
molecules that attach to the active site of the enzyme will
block the action of the enzyme
b. noncompetitive inhibitors
molecules that attach to another site (other
than the active site) allosteric site but change
the shape of the enzyme so that it cannot bind
with its substrate.

BIOENERGETICS

BIOENERGETICS

BIOENERGETICS
Many biochemical pathways use the product as a noncompetitive inhibitor on an enzyme in the pathway to
control the production;
enzyme 1
enzyme 2
enzyme 3
Substrate 1
substrate 2
substrate 3
product
Product inhibits enzyme 1 to slow its catalytic activity on substrate 1 thus slowing the pathway. How
does the pathway speed up?

BIOENERGETICS
Enzyme cofactors
Cofactors are substances that are included on an
enzyme to complete the shape of that enzyme and
allow it to bind to its substrate.
Many minerals are cofactors on enzymes
Vitamins are nonprotein complexes that act as
cofactors on enzymes (coenzymes)

BIOENERGETICS
ATP= Adenosine TriPhosphate
Most energy in the cell is stored here
Some specialized cells store either fat or
starch/glycogen

BIOENERGETICS
ATP structure
Composed of 3 subunits
Five carbon sugar is the backbone (Ribose)
Three phosphates attached to the ribose
Adenine is a nitrogen base attached to the ribose
N atoms have unshared electrons
These weakly attract H atoms

BIOENERGETICS- ATP molecule

BIOENERGETICS
How ATP stores energy
Key is in the phosphate groups
They are negatively charged
Covalent bonds are weak and unstable
When bonds break, energy is released
Usually only the outermost PO4 is released
ATP

ADP + Pi + 7.3 kcal.

BIOENERGETICS
How ATP powers energy-requiring rxns
Cells use ATP in endergonic reactions
These are not spontaneous- products posses more
energy than the reactants
Cell activities can be powered by ATP
Terminal PO4 bond is more exergonic (stores more energy)
than the others)
Activation energy in most rxns is < 7.3 kcal

BIOENERGETICS
How ATP powers energy-requiring rxns
Instability of PO4 bond makes this a poor long-term
energy storage molecule
Cells dont stockpile ATP- create only when needed
Cells usually contain a pool of ATP, ADP and
phosphate

BIOENERGETICS
Metabolism
1. Biochemical pathways
a. Metabolism
1. Sum of all chemical rxns carried out in an organism
2. Anabolism- expend energy to make or transform bonds
3. Catabolism- harvest energy when bonds are broken

BIOENERGETICS
b. Reactions in biological systems occur in sequence
1. Product of one reaction becomes the substrate for another
2. Organized units of metabolism
3. Location of enzymes helps map out model of pathway

BIOENERGETICS
c. How biochemical pathways evolved
1. First primitive biochemical processes
1. a. energy-rich molecules scavenged from the environment
2. b. molecules existed in the existing organic soup

2. Catalyzed reactions were simple one-step processes

3. Without energy-rich molecules only cells that synthesized own
energy survived
4. Energy utilizing rxn became coupled to energy-producing
reaction
5. Evolution of pathway works sequentially
a. Occur one step at a time
b. Final reactions generally evolve in reverse, initial rxn evolves last

BIOENERGETICS
d. How biochemical pathways are regulated
1. Output of pathways must be controlled
2. Primitive organisms evolved feedback mechanisms
3. End product binds to allosteric site on enzyme that
catalyzes first reaction
a. Binding to enzyme shuts down first reaction
b. Effectively shuts down whole pathway
c. Increase in cell product inhibits production of more product
This mechanism is called feedback inhibition

Cellular Energy - ATP

91

ATP

Components:
1. adenine: nitrogenous base
2. ribose: five carbon sugar
3.phosphate group: chain of 3

adenine

phosphate group

ribose

92

Adenosine Triphosphate

Three phosphate
groups-(two with
high energy
bonds
Last phosphate
group (PO4)
contains the
MOST energy
93

Breaking the Bonds of ATP

Process is called
phosphorylation
Occurs continually in
cells
Enzyme ATP-ase can
weaken & break last
PO4 bond releasing
energy & free PO4
94

How does ATP work ?

Organisms use enzymes to

break down energy-rich glucose
to release its potential energy
This energy is trapped and
stored in the form of adenosine
triphosphate(ATP)
95

How Much ATP Do Cells Use?

It is estimated
that each cell will
generate and
consume
approximately
10,000,000
molecules of ATP
per second
96

Coupled Reaction - ATP

The exergonic
hydrolysis of ATP is
coupled with the
endergonic
H2O
dehydration process
by transferring a
phosphate group to
another molecule.
H2O

ATP

ADP + P
97

Hydrolysis of ATP
ATP + H2O

ADP + P

(exergonic)

Adenosine triphosphate (ATP)

P

P
Hydrolysis
(add water)

Adenosine diphosphate (ADP)

98

Hyrolysis is Exergonic

Energy
Used by
Cells

99

Dehydration of ATP
ADP + P

(endergonic)

ATP + H2O
Dehydration
(Remove H2O
P

Adenosine diphosphate (ADP)

Adenosine triphosphate (ATP)

P

P
100

Dehydration is Endergonic
Energy is
restored
in
Chemical
Bonds

101