Energy

Energy – capacity to do work

Forms of Energy
Enthalpy
Potential – energy which (H or E)
is stored; energy at rest;
due to object’s position H or E
or material composition
e.g. chemical

Kinetic – energy
accomplishing work;
energy in motion; due to
motion of an object
e.g. heat, light
1st Law of Thermodynamics
 total energy in the universe is constant
 Energy can be changed from one form to
another but cannot be created nor
destroyed.
 In all energy exchanges and conversions,
the total energy of the system and its
surroundings after the conversion is equal to
the total energy before the conversion
 Example: total energy absorbed by the leaf
= energy emitted from leaf + energy stored
by leaf
The First Law of Thermodynamics
http://biology200.gsu.edu/houghton/2107%20'11/Figures/Chapter6/figure6.3a.jpg
2nd Law of Thermodynamics
 states that the natural tendency of the
universe is towards increasing disorder.
 The total entropy (degree of randomness)
naturally tends to increase and energy
naturally converts to less organized form
 Example: constituent amino acids
dissociated or hydrolyzed from a larger
protein molecule will exhibit higher entropy
(greater freedom of movement) than the
protein molecule itself (constraint
movement of individually bonded amino
acid)
 2nd Law of Thermodynamics
 In all energy exchanges and conversions, if no
energy leaves or enters the system under study,
the potential energy of the final state will always
be less than the potential energy of the initial
state.
 if potential energy of final state is less than
initial:
releases energy (exergonic)
 If potential energy of final state is greater than
initial:
requires energy (endergonic)
 Entropy – measurement of disorder or
randomness of a system
 2nd Law of Thermodynamics

 The second law of thermodynamics: events in the

universe tend to proceed from a state of higher
energy to a state of lower energy.
Such events are called spontaneous, they can
occur without the input of external energy.
Loss of available energy during a process is the
result of a tendency for randomness to increase
whenever there is a transfer of energy.
Free Energy

Measure of energy for the performance of

work; Gibbs free energy (G)
Free energy change, G, is a function of
the displacement of the reaction from or
towards equilibrium

Enthalpy – total energy content of the

system.
Free energy / Gibbs free energy (G)
- combines enthalpy (H) and entropy (S)
- ultimately decides the spontaneity of a process

G = H  T S

 Negative G ( G)

Spontaneous process – Exergonic

 Positive G ( G)

Non-spontaneous process – Endergonic

 An Overview of Metabolism

 Catabolic pathways  Anabolic pathways

break down complex synthesize complex
substrates into simple end products from
end products. simple substrates.
Provide raw Require energy.
materials for the cell.
Use ATP and NADPH
Provide chemical from catabolic
energy for the cell. pathways.
Exergonic – net release of energy
e.g. Respiration
C6H12O6 + 6O2  6CO2 + 6H2O + ATP
G =  686 kcal/mole or  2880 kJ/mole

Endergonic – absorbs energy

e.g. Photosynthesis
light

6CO2 + 6H2O  (CH2O)n + 6O2

G =  686 kcal/mole or  2880 kJ/mole
Energy coupling

Catabolic processes
degradative, usually oxidative
energy yielding (exergonic)

Anabolic processes
synthetic, usually reductive
energy utilizing (endergonic)
Enzymes
 Enzymes
- biological catalysts ; “agents of life”

Properties of Enzymes
Specificity
– usually acts on single substrate

Catalytic efficiency
– 108–1020 times over uncatalyzed reaction

Mostly reversible
– exceptions are decarboxylases and
hydrolases
 Enzyme Composition
(protein + non-protein component)
 Non-protein component
 Prosthetic group – tightly bound; organic molecule
(e.g. flavin, sugar)
 Cofactor – not tightly bound
Metal activator – metal ion (e.g. Zn, Fe, Cu)
Coenzyme – organic molecule (e.g. NAD, FAD, FMN,
vitamins)
 Enzyme
Structure
Four successive levels
1. Primary
- amino acid sequence

2. Secondary
- local structural units held by
H-bond

3. Tertiary
- three-dimensional shape of
polypeptide (subunit)

4. Quaternary
- association of two or more
subunits
Mechanism
of Enzyme
Action

Enzymes lower the

barrier of
activation energy!
Purves et al., Life: The Science of Biology, 4th Edition, by Sinauer Associates
(www.sinauer.com) and WH Freeman (www.whfreeman.com),
Catalytic Cycle of Enzyme
Model of Enzyme-Substrate Interaction
Kinetics of Enzyme-Catalyzed
Reaction

Michaelis-Menten Equation

Km = Michaelis-Menten constant
= substrate concentration
when Vi is one-half Vmax
Km Values of Some Enzymes

Enzyme Substrate Km (M)

Carbonic anhydrase CO2 800

-Galactosidase Lactose 4,000

PEP Carboxylase CO2 2

Pyruvate carboxylase HCO3- 1,000

RuBisCO CO2 12

RuBisCO O2 250
Enzyme Inhibitor

Allosteric site
 Enzymes and inhibitors

 Inhibitors are molecules that prevent

enzymes reaching their maximum
turnover numbers
 Some inhibitors compete with the
Active site directed inhibition
substrate for the active site
 Some inhibitors affect the active site
shape by binding
Non-active to theinhibition
site directed enzyme
elsewhere on the enzyme
Environmental Factors
Affecting Enzyme Activity
 Temperature
 pH
 Salt concentration
 Enzymes and temperature

Increasing kinetic
energy increases
successful
collision rate
Reaction rate / arbitrary units

Temperature / oC
 Enzymes and temperature
Permanent disruption
of tertiary structure
leads to loss of active
site shape, loss of
Reaction rate / arbitrary units

binding efficiency and

activity

Temperature / oC
 Enzymes and temperature
Optimum
temperature
Reaction rate / arbitrary units

Temperature / oC
Enzymes and pH

 Changing pH can cause these side

chains to ionise resulting in the loss of
H-bonding…
 Denaturation state…
 Presence of charged or uncharged
amino or carboxyl group...
 Neutral carboxyl requires low pH optimum
 Uncharged amino group needs high pH
optimum
 Enzymes and pH

Optimum pH Either side of the optimum

pH, the gradual ionising of
the side-chains (R-groups)
Reaction rate / arbitrary units

results in loss of H-
bonding, 3o structure,
active site shape loss of
binding efficiency and
eventually enzyme activity

pH
 Enzymes and pH

Optimum pH This loss of activity is only

truly denaturation at
extreme pH since
Reaction rate / arbitrary units

between optimum and

these extremes, the loss
of activity is reversible

pH
Enzymes and pH
 Enzymes and [S]

As soon as a reaction begins, [S]

Initial reaction rate / arbitrary

begins to fall and so it is important

that initial reaction rates are
measured
units

[S]
 Initial reaction rate / arbitrary
units
Enzymes and [S]

[S]
 Enzymes and [S]

Increasing [S]
increases collision
Initial reaction rate / arbitrary

rate and increases

reaction rate
units

[S]
 Enzymes and [S]
All active sites are
occupied. Enzymes
are working at
maximum rate.
Initial reaction rate / arbitrary
units

All active sites

are not occupied

[S]
 Enzymes and [S]
Maximum
turnover number
or Vmax has been
reached
Initial reaction rate / arbitrary
units

[S]
 Enzyme activity is often
regulated

Cells can control the flux of

metabolites through:
Gene expression
Compartmentation
Covalent modification
Feedback inhibition
 Gene expression
 regulates enzyme activity through the amount or
concentration of enzymes present in the cell ---
determined by relative rates of enzyme synthesis and
degradation

 Compartmentation
 localizes enzymes with different catalytic properties
in the different parts of the cell
enzymes involved in PS are found in chloroplast
hydrolases are found in vacuoles
 Covalent modification
 regulates enzyme activity through phosphorylation ---
phosphorylated form is active while non-
phosphorylated form is inactive

 Feedback inhibition
 enzyme activity is regulated by the end products of
the metabolic pathways which inhibit the enzymes
involved in earlier steps
End of Chapter 1