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Chemical Industry
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)
catalytic
energy
reactant
product
reaction process
Types of catalysts
Classification based on the its physical state, a catalyst can be
gas
liquid
solid
Acid-base catalysts
Enzymatic
Photocatalysis
Electrocatalysis, etc.
Alternate Case
At low pH
At high pH
At an optimized condition
Graphical Representation
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
Enzyme Catalysis
Six major classes of reaction
catalyzed enzymes are Classified as
Oxidoreductase
Transferase
Hydrolase
Lyases
Isomerases
Ligases
Enzyme Catalysis
Lock and Key Theory
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.
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 ]
Eadie Plot
Concentration of Various
Species
Zoomed outlook
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
Effect of pH on Enzyme
Kinetics
Low pH
High pH
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
Photochemical Process