Catalysis

Catalyst and
catalysis:
Rate of the chemical reaction may be influenced considerably in the
presence of small amount of specific substance such substance are
called catalyst and the phenomena referred to as catalysis

 Catalyst
It is a substance which alter the rate of the chemical reaction without
being used up in the reaction and can be recovered chemically
unchanged at the end of the reaction

Positive catalyst Negative catalyst
Positive catalyst:
The catalyst which increases the rate of the reaction is called positive
catalyst and phenomena is known as positive catalysis
e.g.
Ni
Vegetable oil + H 2                                 Vegetable ghee

MnO2
2KClO3                              2KCl + 3O2

Negative catalyst:
The catalyst which decreases the rate of the reaction
The phenomena is negative catalysis
e.g. The oxidation of chloroform in the presence of air is retarded in
the presence of alcohol
Tetra ethyl lead decreases the knocking of petrol. Thus acts as
negative catalyst
 Characteristics of catalysts
1. A catalyst remains unchanged in mass and chemical composition at
the end of the reaction
e.g. Granular MnO 2 used as a catalyst during the decomposition of KClO3
is recovered as a fine powder after the reaction
2KClO3  + 2MnO 2                               2KMnO4  +  Cl 2  + O 2
2KMnO4                                           K 2MnO4   + MnO 2  + O 2
K2MnO4  +  Cl 2                          2KCl   + MnO 2 + O 2

2. A small amount of catalyst is sufficient to bring about an appreciable
change in the velocity of reaction
e.g. Presence of even 1mg of fine Pt powder is enough to catalyse the
combination of 2.5 lit of a mixture of H 2 and O2 to form H 2O
3. A catalyst can exert a selective action, like a key can open a particular lock
e.g. water gas       (CO + H 2)

ZnO + Cr 2O3 Ni/400o  C

400 O C

CH3OH CH4  +  H 2O

4. A catalyst does not alter the position of the equilibrium in a reversible
reaction
Since catalyst help in the equilibrium state being reached more quickly
through increasing rate of forward and reverse reaction in the same
proportions, the value of equilibrium constant is same whether a catalyst
is used or not.
5. A catalyst is most active at particular
temperature called optimum temperature
6. The activity of a catalyst substance can be changed by the presence
of small amount of foreign substances. These foreign substances can
be called promoters which increase the activity of a catalyst or
anticatalyst or catalytic poisons which inhibit or completely destroy
the activity
e.g. promoters
In the manufacture of NH 3 by Haber’s process, finely divided Fe acts
as a catalyst; while molybdenum (or a mixture of Al 2O3 + K 2O) acts as a
promoter.
In the manufacture of CH 3OH from CO and H 2 the activity of the
catalyst ZnO is greatly enhanced by the presence of Cr2O3, the
promoter.
e.g. Poisons
In the manufacture of H 2SO4 by the contact process, a trace of As 2O3
destroys the catalytic efficiency of spongy platinum.
Catalytic poisons like HCN, As 2O3, CO, H 2S, etc are remarkably
poisonous to organisms.
 Types of
catalysis

Auto-catalysis Homogenousca Heterogenousc Enzyme

talysis atalysis catalysis
 Auto-catalysis
When a product formed in the course of reaction enhances the velocity of the reaction
(or acts as a catalyst) the phenomenon, is called auto-catalysis
Example.
1. Hydrolysis of ester by water
RCOOR’ + H 2 O RCOOH + R’OH
The acid liberated as a result of hydrolysis catalyse the reaction
2. Titration of warm solution of oxalic acid by KMnO 4solution
First few drops take appreciable time before they are decolorised, since the reaction is
initially very slow, but after some time the decolorisation goes rapidly as the Mn 2+ ions
formed in the course of the reaction catalyse the reaction
5C 2 O42- + 2MnO 4- + 16H+ 2Mn 2+ + 10CO 2 + 8H 2 O
 Homogenous catalysis
In this, the catalyst is present in the same phase as the reacting substances
Examples
a) In gas phase:
(i) In the lead chamber process for the manufacture of H2 SO4 , nitric oxide (NO)
catalyse the oxidation of sulphur dioxide
2SO 2 (g) + O 2 (g) 2SO3 (g)
NO(g)
(ii) Decomposition of acetaldehyde is catalysed by iodine vapours
CH3 CHO (g) CH 4 (g) + CO(g)
I2 as a catalyst in the combination of carbon monoxide and
(iii) Nitric oxide acts
Vapour
oxygen
2CO(g) + O 2 (g) 2CO 2 (g)
b) In liquid phase NO(g)

e.g. Inversion of cane sugar

C12H22 O11 + H 2 O C 6H12O6 + C6H12O6
H+
 Assignment
1. What is catalysis and catalyst? Mention
different type of catalyst.
2. Give example of positive and negative
catalysis.
 Mechanism of catalytic action
Unstable intermediate compound formation theory
Forwarded by Clement and Desormes in 1806
According to this the catalyst forms a very reactive and unstable
intermediate compound with reactants, which immediately reacts with other
reactants yielding the products of the reaction and liberating the catalyst in
its original chemical composition
In a reaction type A + B AB
A+ K AK (Intermediate compound)
AK + B AB + K (catalyst)
Many reactions can be explained by this mechanism
Example: Catalytic action of NO in the manufacture of H 2 SO4 by Chamber’s
process:
2NO + O 2 2NO 2
2SO2 + 2NO 2 2SO 3 + NO
2NO + 2SO2 + O 2 2SO3 + 2NO
 Limitations of Unstable intermediate compound
formation theory
1. The action of promoters and catalytic poisons
2. The function of catalyst in heterogenous reactions, where
intermediate compound formation is not possible,
e.g. Combination of SO 2 and O2 in presence of platinised asbestos, where
catalyst is solid and the reactants are gases
 Heterogenous
substances.
Catalysis
In such reactions, the catalyst is present in a different phase from the reacting

Examples
(i) In contact process for the manufacture of H 2 SO4, sulphur dioxide is directly
oxidized to sulphur trioxide by atmospheric oxygen in the presence of platinum or
vanadium pentoxide as catalyst
2SO + O Pt or
2SO
2 2 3
V 2 O5

(ii) In Haber’s process for the manufacture of NH 3, nitrogen and hydrogen in the
volume ratio of 1:3 are passed over heated iron catalyst, which contains a
promoter (molybdenum)
Fe, Mo
N 2 + 3H 2 2NH 3
 Adsorption or contact theory
1) The surface of the solid catalyst possesses some isolated active spots (or centres)
having residual affinity or free unsatisfied valency forces
2) Due to these free unsatisfied valency forces on the catalyst surface, the
molecules of the gaseous reactants get adsorbed in unimolecular thickness layer.
3) The adsorbed molecules react due to their close proximity, forming products. The
latter then fly off; leaving the surface for fresh action
4) The chemical action is accelerated on account of increased concentration of the
reacting substances on the surface of the solid catalyst, and no definite
intermediate compound formation takes place
5) The forces which keep the molecules of reactants intact with catalyst also attract
the reacting molecules. The distorted molecules of a catalyst, being under more
strain are more active
 Advantages of adsorption
theory
a) The catalyst is more efficient in finely divided state: Increases in disintegration increases
surface area thereby increasing the number of free valencies or active centres, which are
responsible for the adsorption of reactant molecules and consequently , the activity of
the catalyst is also enhanced
b) Enhanced activity of a rough surfaced catalyst: Rough surface possesses cracks, peaks,
corners, etc. and consequently, have larger number of active spots, which in turn must be
catalytically more active
c) Action of promoters is explained by assuming that a loose compound is formed between
the catalyst and the promoter, which possesses an increased adsorption capacity than
the pure catalyst only
d) Action of catalytic poisons: The catalytic poison preferentially adsorb on the active sites
of the catalyst, thereby reducing the number of active sites available for the promotion
of the molecules of reactants
e.g In contact process for the manufacture of sulphuric acid, catalytic poison As 2 S3 adsorb
on the active site of Pt forming platinum sulphide on the surface of Pt, thereby reducing
the catalytic activity
 Assignment
▶ What are enzymes? Give two examples of
enzyme catalyzed reactions.
1. Explain the terms: Prosthetic group, cofactor,
coenzyme in connection with enzyme
catalysis
2. Explain homogeneous catalysis and its
mechanism. What are the limitations of this
theory?
Enzymes: The Catalysts of
Life
Enzymes are highly complicated non-living nitrogenous organic substances
produced by living organisms . They are proteins with high relative molar
mass of the order of 10,000 or even more units. They possess incredible
capacity in bringing about many complex chemical reactions like hydrolysis,
oxidation, reduction etc.
Enzyme Catalysis: Catalytic activity brought about by enzymes

Brought inside the Brought outside the body

body e,.g manufacture of ethyl
e,.g digestion of food alcohol from molasses

Examples
Diastase
2(C6H10 O5 )n + n H 2 O nC 12H22 O11 (Maltose)
Maltase
C12H22 O11 + H 2 O 2C 6H12O6 (glucose)
NH2 CONH2 + 2H 2 O Urease
(NH ) CO
4 2 3
 Characteristics of enzymes
1. Enzymes are proteins that can act as effective catalyst and speed up the reaction by high
20
factor upto 10
Carbonic
anhydrase
e.g. H2 CO3 H2 O + CO 2
Under ideal conditions even a single molecule of catalysts is capable of catalysing as many
as 36 million molecules of carbonic acid in just one minute
2. Enzymes are highly specific and their specificity is of three types

a. Reaction type-specific
b. Substrate specific
c. Stereochemistry specific (stereospecific)

The enzyme invertase can break up sucrose in to glucose and fructose but fails to break
up very similar disaccharide maltose which require another enzyme maltase
 3. Effect of Temperature

All enzymatic reactions exhibit maximum efficiency

at optimum temperature
Above this temperature enzyme gets denatured.
Thereby losing its activity.
Below optimum temperature the rate of the reaction
is slow due to the temperature effect
For most enzymes the reaction rate increase up to
45o C and above 45 o C thermal denaturation takes
place. Above 55 o C rapid thermal denaturation
destroy completely the catalytic activity of enzyme
protein
4. Enzyme catalysed reactions are much more sensitive to catalytic
poisons such as HCN, H 2S, CS 2 etc. The inhibitors interact with the
active functional groups present on the enzyme surface and often
reduce or completely destroy the catalytic activity of the enzymes

5. The activity of certain enzymes depend upon certain non-protein

substances called Co-enzymes. For each enzyme, there is only one co-
enzyme

6. Enzymes lose their activity when exposed to ultravoilet radiations

or in presence of electrolytes

7. Even a small amounts of an enzyme can be highly efficient in

bringing about a particular biological reaction, because a typical
enzyme molecule may be regenerated million times in a minute

8. Like ordinary catalysts, enzymes cannot disturb the final state of

equilibrium of a reversible reaction
 9. Effect of pH
Effect of pH on the rate of enzyme catalysed
reaction is of complex nature but the
favourable pH range for most of the
reactions is 5-7
• Binding of substrate to enzyme
• Ionization state of “catalytic” amino acid
residue side chains
• Ionization of substrate
• Variation in protein structure

Multistage equilibria exists in these reactions

E EH EH 2
And
ES EHS EH 2 S

EH + Product
Prosthetic group: Enzymes are associated with non-protein components called
prosthetic groups

Co-factor: The prosthetic groups could be metal ions such as Zn 2+, Mg2+, Co2+, K+ ,
Na+ etc. called as co-factor

Co-enzyme: If the prosthetic group is a small organic molecule, it is referred to

as a co-enzyme

Apo-enzyme: Many of the coenzymes for biological processes are derived from
vitamins like thiamine, riboflavin, niacin, etc. In such enzymes the protein part of
the enzyme is called apoenzyme

Neither apoenzyme nor coenzyme is able to catalyse the reaction alone. The two
must combine together before acting as a catalyst
 Mechanism of enzyme action
The substrate is bound to a particular active site in the enzyme,
where the necessary functional groups are gathered

These functional groups are poised in just the right position for the
attack on the substrate

The enzymes can increase the rate of biochemical reactions by

factors ranging from 106 to 10 12
The high turnover number suggest that the substrate molecule
cannot be very tightly bound to the enzymes; if they were, they
might block the active sites.
Reaction would then be slow, because the active site is not quickly
cleared out
There is an equilibrium between the substrate (S) and the active site
of enzyme (E)
E + S ES (enzyme-substrate complex)
ES E + P(product)
The second step is the rate determining step
The rate of enzyme catalysed reaction increases because enzyme
catalyst decreases the activation energy of a reaction to a sufficient
amount
The reaction rate of an enzyme-catalysed reaction changes from
first order to zero order as the concentration of substrate, [S] is
increased
Each molecule has 1 or more active
sites at which the substrate must be
bound in order that the catalytic
action may occur

At low [S], most of these active sites

remain unoccupied at any time.

As the [S] increased, the number of

active sites which are occupied
increases and hence the reaction
rate also increases

At very high [S], all the active sites

are occupied at any time so that
further increase in substrate
concentration cannot further
increase the formation of enzyme-
substrate complex, because all
 Lock and key model
Developed by Fischer (1894) to explain the specificity of enzymes

An enzyme is ordinarily a very large protein molecule that contains one

or more active sites, where the reactions with the substrate takes place;
the rest of the molecule maintains the three-dimensional integrity of the
network

The active site has a rigid structure, similar to a lock. A substrate

molecule has a complementary structure that causes it to fit and function
like a key

Geometry of an active site only fit one type of substrate in most cases.

That’s why enzymes are highly specific in action
 Role of a
promoter
Promoter first attaches itself
on the appropriate binding
site on the surface of enzyme,
thereby changing the shape of
active sites

Now substrates can easily fit

in leading to the formation of
enzyme substrate complex .
Subsequently one or more
products will form and
separate from the enzyme
Role of a poison
Competitive inhibitors Noncompetitive inhibitors
 Assignment
▶ Explain the following terms:
(i) Apo enzyme
(ii) Coenzyme
(iii) Co- factor
 NPTEL LINKS

▶ http://nptel.ac.in/courses/103102012/