Catalysis
catalyst: a substance that increases the rate of reaction, but is not part of the
overall reaction
A catalyst lowers the Ea ⇒ usually a catalyst helps weaken or break reactant bonds
A catalyst alters the reaction mechanism, but does not change the overall reaction
A catalyst may appear in the experimental rate law ⇒ a reaction may have more than one
rate law.
Catalyzed reaction: Ea is lower, but ∆H = ∆H (products) - ∆H (reactants) is the
same:
Features of catalyst
Catalyst remain unchanged in mass and chemical composition at the end of
reaction
Small amount of catalyst is generally needed to produce unlimited reaction
Catalyst is mor effective when finely divided
Catalyst is specific in action.
Catalyst cannon in general initiate a reaction
Catalyst does not affect final position of equilibrium, although it shorten time
required to establish equilibrium
Types of catalyst
Heterogeneous – The catalyst is in a different phase than the reactants. Typically,
a metal is used to provide a surface upon which reactants can adsorb and react.
E.g.
Homogeneous – The catalyst is in the same phase as the reactants. The
catalyst is consumed, then regenerated in a subsequent step. Homogeneous
catalyst may appear in rate law.
Example. Homogeneous catalyzed decomposition of hydrogen peroxide:
2H2O2 → 2H2O + O2
Step 1: H2O2 + I- → H2O + IO- Slow
Step 2: H2O2 + IO- → O2 + H2O + I- Fast
Acid-catalyzed reaction
• Consider equation below
Where are rate constant for the reversible reaction and k3 is equilibrium constant
for formation of product.
…………………………………………….1
But SH+ is intermediate, using SSA
Substituting in eqn. 1 above
Here ,there are two cases
Case I: If
Then,
The reaction is second-order and the acid is strong
Case II: if
The reaction is first-order and acid is weak
Enzyme
Large protein molecules with one or more active sites that serve as biological
catalysts in living organisms. The enzymes are compatible with specific substrate
molecules
Example of enzyme catalytic reaction
(C6H10O6)n diartac C12H22O11 maltase C6H12O6 zymase invertase C2H5OH
Michaelis-Menten Kinetics
Enzyme inhibitor Type of enzyme inhibitor
Molecule which reduce the enzyme Competitive inhibitor; substrate and
activity is called inhibitor e.g. drugs,
inhibitor compete to bind in enzyme
food preservative, poison etc.
active site
Metabolic pathway are regulated by Noncompetitive inhibitor; inhibitor
enzyme inhibition
attack at allosteric site and substrate
Inhibition occur when any compound bind to the active site of enzyme
compete with substrate for active site
of enzyme
Kinetics of competitive inhibitor
Competitive inhibitor bind reversibly to the free
enzyme, not to ES complex to form EI complex
EI
ES readily dissociate
Increase KM value
Free enzyme is readily available but enzyme
activity decline, no product form
This can be reversibly by increasing substrate
concentration
Kinetics of Noncompetitive inhibitor
Inhibitor binds to EI complex only and
not to free enzyme
Adding more substrate increase velocity
only
It is found in reaction where E binds to
more than one substrate
Kinetics of Noncompetitive inhibitor
Factors affecting the rate of enzyme
kinetics
Temperature
enzymes are ineffective at extremely low & high temperature
Enzyme has maximum activity at optimal temperature
pH
Most enzymatic are maximum at neutral
At other pH value the rate is extremely low
Activators
Usually, enzymatic reaction are maximum in presence of activators
