Catalysis

Facts and Figures about

Catalysts
Life cycle on the earth
Catalysts (enzyme) participates most part of life cycle
e.g. forming, growing, decaying
Catalysis contributes great part in the processes of converting sun
energy to various other forms of energies
e.g. photosynthesis by plant CO 2 + H2O=HC + O2
Catalysis plays a key role in maintaining our environment

Chemical Industry

ca. $2 bn annual sale of catalysts

ca. $200 bn annual sale of the chemicals that are related products
90% of chemical industry has catalysis-related processes
Catalysts contributes ca. 2% of total investment in a chemical
process

Catalysis
Catalysis
Catalysis is an action by catalyst which takes part in a chemical reaction
process and can alter the rate of reactions, and yet itself will return to its
original form without being consumed or destroyed at the end of the
reactions
(This is one of many definitions)

Three key aspects of catalyst action

taking part in the reaction
it will change itself during the process by interacting with other
reactant/product molecules

altering the rates of reactions

in most cases the rates of reactions are increased by the action of catalysts;
however, in some situations the rates of undesired reactions are selectively
suppressed

Returning to its original form

After reaction cycles a catalyst with exactly the same nature is reborn
In practice a catalyst has its lifespan - it deactivates gradually during use

Catalysis action - Reaction kinetics

and mechanism
Catalyst action leads to the rate of a reaction to change.
This is realised by changing the course of reaction (compared to noncatalytic reaction)
Forming complex with reactants/products, controlling the rate of
elementary steps in the process. This is evidenced by the facts
that
uncatalytic
The reaction activation energy is altered

catalytic

energy

The intermediates formed are different from

those formed in non-catalytic reaction
The rates of reactions are altered (both
desired and undesired ones)

reactant
product
reaction process

Reactions proceed under less demanding conditions

Allow reactions occur under a milder conditions, e.g. at lower
temperatures for those heat sensitive materials

Types of catalysts
Classification based on the its physical state, a catalyst can be
gas
liquid
solid

Classification based on the substances from which a catalyst is made

Inorganic (gases, metals, metal oxides, inorganic acids, bases etc.)
Organic (organic acids, enzymes etc.)

Classification based on the ways catalysts work

Homogeneous - both catalyst and all reactants/products are in the same
phase (gas or liq)
Heterogeneous - reaction system involves multi-phase (catalysts +
reactants/products)

Classification based on the catalysts action

Acid-base catalysts
Enzymatic
Photocatalysis
Electrocatalysis, etc.

Catalysis: General Mechanistic

Outlook

Alternate Case

Vant Hoff Intermediate

Comparative Activation Energy

Analysis

Acid Catalyzed Reactions

Mechanism for Acid-base

Catalysis

Acid Catalyzed Reaction

At low pH

At high pH

At an optimized condition

Acid-Base Catalysis Graphical

Representation

Acid Catalyzed Fast Preequilibria

fSH = fraction of protonated substrate

Base Catalyzed reaction under fast

pre-equilibrium

Alternate A-B Catalyzed Reaction

(Vant Hoff Intermediate)

Graphical Representation

Hydrolysis of Aspirin and its ester

Derivative

Enzyme Kinetics
measurement of velocity = reaction rate
compare enzymes under different conditions, or from
different tissues or organisms
understand how differences relate to physiology/function of organism
e.g., physiological reason for different Km values

compare activity of same enzyme with different substrates

(understand specificity)
measure amount or concentration of one enzyme in a mixture
by its activity
measure enzyme purity (specific activity = amount of
activity/amount of protein)
study/distinguish different types of inhibitors
info about enzyme active sites and reaction mechanism
development of specific drugs (enzyme inhibitors)

Enzyme Catalysis
Six major classes of reaction
catalyzed enzymes are Classified as
Oxidoreductase
Transferase
Hydrolase
Lyases
Isomerases
Ligases

Enzyme Catalysis
Lock and Key Theory

Induced Fit Theory

Enzymes are Exact Size fit

for substrates -conformational changes do
not occur when substrate
binds during the reaction.

Enzymes flexible -conformational changes

can occur when substrate
binds during the reaction, to
get maximal
complementarity to the
transition state.

Enzyme Kinetics
The initial velocity increases with [S] at low [S].

Initial velocity

Michealis-Menten Model
1. First step: The enzyme (E) and the substrate (S)
reversibly and quickly form a non-covalent ES complex.
2. Second step: The ES complex undergoes a chemical
transformation and dissociates to give product (P) and
enzyme (E).
3. v=k2[ES]
4. Many enzymatic reactions follow MichaelisMenten
kinetics, even though enzyme mechanisms are always
more complicated than the MichaelisMenten model.
5. For real enzymatic reactions use kcat instead of k2.

The Enzyme-Substrate Complex (ES)

The enzyme binds non-covalently to the substrate to form
a non-covalent ES complex
The ES complex is known as the Michaelis complex.
A Michaelis complex is stabilized by molecular
interactions (non-covalent interactions).
Michaelis complexes form quickly and dissociate
quickly.

Assumptions
1. k1,k-1>>k2 (i.e., the first step is fast and is always at equilibrium).
2. d[ES]/dt 0 (i.e., the system is at steady state.)

d[ES]
rate of formation of ES
dt
rate of breakdown of ES
0 (at steady state)
3. There is a single reaction/dissociation step (i.e., k 2=kcat).
4. STot = [S] + [ES] [S]
5. There is no back reaction of P to ES (i.e. [P] 0). This assumption
allows us to ignore k-2. We measure initial velocities, when [P] 0.

Michealis-Menten Equation

M-M Eqn
The final form of M-M equation in the case of a single
substrate is

kcat [ Etot ][ S ]
v
K m [S ]

kcat (turnover number): how many substrate molecules

can one enzyme molecule convert per second
Km (Michaelis constant): an approximate measure of
substrates affinity for enzyme

Linear representation of Enzyme

Kinetics
Lineweaver Burk Plot

Eadie Plot

Concentration of Various
Species

Zoomed outlook

Two Substrate Enzyme

Kinetics

Enzyme Inhibitors
Reversible versus Irreversible
Reversible inhibitors interact with an
enzyme via non-covalent
associations
Irreversible inhibitors interact with an
enzyme via covalent associations

Classes of Inhibition
Two real, one hypothetical
Competitive inhibition - inhibitor (I)
binds only to E, not to ES
Noncompetitive inhibition inhibitor (I) binds either to E and/or to
ES
Uncompetitive inhibition - inhibitor
(I) binds only to ES, not to E. This is a
hypothetical case that has never been
documented for a real enzyme, but
which makes a useful contrast to

Competitive Inhibition

Uncompetitive Inhibition

Non-Competitive Inhibition
E

ES

EI

ESI

E+P

Example of Irreversible Inhibition

Effect of pH on Enzyme
Kinetics

Low pH

High pH

Photochemical Processes and

Kinetics
Photochemical process The
initiation of a chemical reaction
through the absorption of a photon
by an atom or molecule.

Jablonski Diagram

Franck Condon
Principle

Photochemical Processes
After population of S1, the fate of the
excited species via photophysical
processes:
(1) Thermal equilibration of the
vibrational Energy = vibrational
relaxation (VR, ~100 fs)
(2) Fluorescence: A radiative
transition to lose the excess
electronic energy through emission of a
photon. (10-9 to 10-6 s)
(3) Intersystem crossing (ISC): A
change of spin state to T1, which is
forbidden by quantum mechanics.
Rate of S1 VR > fluorescence ~ ISC.

T1 VR

(4) Phosphorescence from T1 to S0, a

spin forbidden transition occurs in 10-6
to seconds timescales.

Fluorescence and Fluorescence

Quenching

Photochemical Process