BIOENERGETICS

1
What is Bioenergetics?
The study of
energy in living
systems
(environments)
and the
organisms
(plants and
animals) that
utilize them
2
 Energy
 Required by
all organisms
 May be
Kinetic or
Potential
energy

3
 Kinetic Energy
 Energy of
Motion
 Heat and
light energy
are
examples
4
 Potential Energy
 Energy of
position
 Includes
energy
stored in
chemical
bonds
5
 Two Types of
Energy Reactions

6
 Endergonic Reactions
 Chemical reaction that requires
a net input of energy.
energy
 Absorbs free energy and stores
it Light
 Photosynthesis SUN Energy
photons

6CO2 + 6H2O  C6H12O6 + 6O2

(glucose)
7
Exergonic Reactions
 Chemical reactions that
releases energy
 Cellular Respiration
Energy

C6H12O6 + 6O2  6CO2 + 6H2O+ ATP

(glucose)

8
Metabolic Reactions
of Cells

9
What is Metabolism?
 The sum total
of the chemical
activities of all
cells.
cells
 Managing the
material and
energy
resources of
the cell
10
Two Types of Metabolism
 Catabolic
Pathways
 Anabolic
Pathways

11
 Catabolic Pathway
 Metabolic reactions which release
energy (exergonic) by breaking down
complex molecules in simpler
compounds
 Hydrolysis = add a water molecule to
break apart chemical bonds
energy
 Cellular Respiration
C6H12O6 + 6O2  6CO2 + 6H2O + ATP
(glucose)
12
 Anabolic Pathway
 Metabolic reactions, which consume
energy (endergonic), to build
complicated molecules from simpler
compounds.
 Dehydration synthesis = removal of a water
molecule to bond compounds together
 Photosynthesis light
SUN energy

6CO2 + 6H2O  C6H12O6 + 6O2

(glucose)
13
Energy Coupling
 The transfer of energy from
catabolism to anabolism

 Energy from exergonic reactions drive

endergonic reactions and vice versa

 EX. Photosynthesis – cellular respiration

cycle

14
Energy Transformation
 Governed by the Laws of
Thermodynamics.

15
1st Law of Thermodynamics
 Energy can be transferred and
transformed, but it cannot be
created or destroyed.
 Also known as the law of
Conservation of Energy.

16
 2nd Law of Thermodynamics
 Each energy transfer or
transformation increases the
entropy of the universe.

Entropy = a measure of
disorder or randomness

HEAT is energy in its most random state.

17
Summary
 The quantity of energy in the
universe is constant, but its quality is
not.

18
Free Energy
The portion of a system's energy
that can perform work.
G = H - TS
G = free energy of a system
H = total energy of a system
T = temperature in oK
S = entropy of a system
19
 Free Energy of a System
 If the system has:
 more free energy
 it is less stable
 It has greater work capacity

 Metabolic equilibrium = zero free energy so it can do no

work DEAD CELL
 Metabolic disequilibrium = produces free energy to do
work
 More unstable produces more free energy
 EX. Greater concentration/ temperature differences
20
Free Energy Changes

21
Spontaneous Process
 If the system is unstable, it has a
greater tendency to change
spontaneously to a more stable state.
 This change provides free energy for
work.

22
Chemical Reactions
 Are the source of energy for living systems.
 Are based on free energy changes.

Reaction Types
Exergonic: chemical reactions with a net
release of free energy.
Endergonic: chemical reactions that
absorb free energy from the
surroundings.

23
Exergonic/Endergonic

24
3 main kinds of cellular work
 Mechanical - muscle contractions
 Transport - pumping across
membranes
 Chemical - making polymers

All cellular work is

powered by
ATP
25
Cell Energy
 Couples an exergonic process to drive
an endergonic one.
 ATP is used to couple the reactions
together.

26
Cellular Energy -
ATP

27
 ATP
 Components:
1. adenine: nitrogenous base
2. ribose: five carbon sugar
3.phosphate group: chain of 3

adenine phosphate group

P P P
ribose

28
 Adenosine Triphosphate
 Three phosphate
groups-(two with
high energy bonds
 Last phosphate
group (PO4) contains
the MOST energy
 All three phosphate
groups are
negatively charged
(repel each other
making it very
unstable)
29
Breaking the Bonds of ATP
Occurs continually in cells
 Enzyme ATP-ase can
weaken & break last PO4
bond releasing energy &
free PO4

 Phosphorylated = a
phosphate group attaches
to other molecules making
them more unstable and
more reactive (energy
boost to do work)

30
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)
31
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
32
Coupled Reaction - ATP
 The exergonic
hydrolysis of ATP
is coupled with the
endergonic
dehydration H2O
process by
transferring a
phosphate group to
another molecule.
H2O
33
 Hydrolysis of ATP
ATP + H2O  ADP + P (exergonic)

Adenosine triphosphate (ATP)

P P P

Hydrolysis
(add water)

P P + P
Adenosine diphosphate (ADP)
34
Hyrolysis is Exergonic

Energy
Used
by
Cells

35
Dehydration of ATP
ADP + P  ATP + H2O (endergonic)

Dehydration
(Remove H2O

P P + P
Adenosine diphosphate (ADP)

Adenosine triphosphate (ATP)

P P P
36
Dehydration is Endergonic

Energy
is
restored
in
Chemical
Bonds

37
ATP in Cells
 A cell's ATP content is recycled
every minute.
 Humans use close to their body
weight in ATP daily.

 No ATP production equals quick

death.

38
 What Are Enzymes?
 Most enzymes are
Proteins (tertiary
and quaternary
structures)
 Act as Catalyst to
accelerates a
reaction
 Not permanently
changed in the
process

39
 Enzymes
 Are specific for
what they will
catalyze
 Are Reusable
 End in –ase
-Sucrase
-Lactase
-Maltase

40
How do enzymes Work?

Enzymes work by
weakening bonds
which lowers
activation energy

41
Activation Energy
 Energy needed to convert potential
energy into kinetic energy.
Activation Energy

Potential Energy

42
 Enzymes Without Enzyme
With Enzyme

Free Free energy of activation

Energy
Reactants

Products

Progress of the reaction

43
44
45
Enzyme-Substrate Complex
The substance (reactant) an
enzyme acts on is the
substrate

Substrate Joins Enzyme

46
 Active Site
Active
Site
Substrate Enzym
e

 A restricted region of an enzyme molecule

which binds to the substrate.
substrate
47
48
Models of How Enzymes Work
1. Lock and Key model
2. Induced Fit model

49
 Lock and Key Model
 Substrate (key) fits to the active
site (lock) which provides a
microenvironment for the specific
reaction.

50
 Induced Fit
 A change in
the shape of
an enzyme’s
active site
 Induced by
the substrate

51
Induced Fit Model
 Substrate “almost” fits into the
active site, causing a strain on the
chemical bonds, allowing the reaction.

52
Enzymes
 Usually specific to one substrate.

 Each chemical reaction in a cell

requires its own enzyme.

53
Factors that Affect Enzymes
 Environment (Temperature & pH)
 Cofactors
 Coenzymes
 Inhibitors
 Allosteric Sites

54
Environment
 Factors that change protein
structure will affect an enzyme.
 Examples:
 pH shifts
 temperature
 salt concentrations

55
 Temperature & pH
 High temperatures denature enzymes
(Most enzymes like normal body
temperatures)
temperatures
 Most enzymes function near neutral
pH (6 to 8)
 Denatured (unfolded) by ionic salts

56
57
 Cofactors
 Inorganic substances (zinc, iron, copper)
are sometimes need for proper enzymatic
activity.
activity
 Non-protein helpers can bond to the active
site of enzymes to help in reactions

 Example:
Iron must be present in the quaternary
structure of hemoglobin in order for it
to pick up oxygen.
oxygen
58
 Coenzymes
 Organic molecules that act as
cofactors which help enzymes.
 Examples:
 vitamins

59
Two examples of Enzyme
Inhibitors
a. Competitive inhibitors: are
chemicals that resemble an enzyme’s
normal substrate and compete with
it for the active site.
site

Substrate
Enzyme
Competitive inhibitor

60
 Inhibitors
b. Noncompetitive inhibitors:
Inhibitors that do not enter the active site,
site
but bind to another part of the enzyme causing
the enzyme to change its shape,
shape which in turn
alters the active site.
site

Substrate Noncompetitive
Inhibitor
Enzyme
active site
altered
61
62
 Control of Metabolism
 Is necessary if life is to function.
 Controlled by switching enzyme activity
"off" or "on” or separating the enzymes in
time or space.
Types of Control
1. Switching on or off the genes that
encode for specific enzyme
production
2. Allosteric sites
3. Feedback inhibition
4. cooperativity
63
 Allosteric Regulation
 The control of an enzyme complex by the binding
of a regulatory molecule.
 Regulatory molecule may stimulate or inhibit the
enzyme complex.

 Allosteric site is a specific receptor site on some

part of the enzyme molecule away from the active
site
 When activated, this site changes the shape of
the enzyme to inhibit it or to stimulate it

64
Allosteric Regulation

65
 Feedback Inhibition
 When a metabolic pathway is
switched off by its end-product.
 End-product usually inhibits an
enzyme earlier in the pathway.
 Prevents the cell from wasting
chemical resources

66
67
 Cooperativity
 One substrate molecule can trigger
the same favorable shape-change in
all the other subunits of the enzyme

 Amplifies the response of the

enzymes to substrate

68
Review

69
How many high energy phosphate
bonds does ATP have?

70
Which is true of photosyntheis?

Anabolic or Catabolic

Exergonic Or Endergonic

71
 The breakdown of ATP is
due to:
Dehydration or Hydrolysis

H2O added or H2O removed

72
 Which Reactions are often
Coupled in Organisms
Hydrolysis BOTH
or Dehydration

Anabolism or
BOTH Catabolism

Endergonic or
BOTH Exergonic

73