27 Jan, 2019

Transistion State Theory

Submitted By : Amna Arshad
Instructor : Doc Sadia
Roll number : 44
Semester : 8 ( Physical)
Department : Chemistry
 TRANSISITION STATE THEORY

Introduction:

History:
Transition state theory was proposed in 1935 by Henry Erying, and further developed by Merrideth
G. Evans and Michael Polanyi (Laidler & King, 1983), as another means of accounting for chemical
reaction rates. It is based on the idea that a molecular collision that leads to reaction must pass
through an intermediate state known as the transition state. Based on their original assumption that
the reaction rates can be calculated absolutely, the theory is also called as the theory of absolute
reaction rates.

“Atoms and molecules can collide and combine to form an unstable, high energy complex.
When the molecules fall out of this high energy state, they may do so as new and different
molecules, or in their original states. The energy required to reach the activated state must be
available if the molecules are to change into something new.”

TST theory becomes the paradigm for interpretation of the rates of chemical processes as well as
their dependence on temperature, medium, structure, and other parameters. Since the kinetic energy
of colliding molecules, possessing sufficient energy and having proper orientation, is transformed
into potential energy the energetic state of activated complex is characterized by positive molar
Gibbs energy. The standard Gibbs energy of activation is the difference between the transition state
of a reaction and the ground state of reactants.

Activated state is then formed as highly energized and then unstable intermediate , which has
transient existence and decomposes to form the products of reaction. The rate of reaction is given by
the definite rate of decomposition of activated complex.

Assumption:
TST theory assumes that chemical reaction (or any other activated process proceeds as two-stage
process:
 Formation of activated complex;
 Decomposition of activated complex into the products of reaction;
Activated state is then less stable state than any other occurring during the reaction. Chemical
equilibrium is the state in which both, reactants and products are present in the concentrations which
have further tendency to change with time

Equation:

Consider the bimolecular reaction of A with B to form P, where k is the second order rate constant
describing this reaction:

Now, consider the same bimolecular reaction sequence, but in which A and B reversibly react to form
an intermediate complex (AB)‡ , which irreversibly decomposes to form final product P. The species
(AB)‡ is a so-called transition state (or activated complex) whose lifetime is less then 10-13 sec.
We can now write the rate of reaction of A and B to form P in two ways, as in equation

In this equation, k is the bimolecular rate constant for conversion of A and B to P and k' is the
unimolecular rate constant for decomposition of the activated complex (AB)‡ to form P.

Now, the Eyring approach assumes that we can

assume a thermodynamic quasi-equilibrium to exist
between A, B and (AB)‡ . If this is true, we can write
an equilibrium constant and an expression for ∆G0 ‡ ,
the free energy of reaction to form the transition state
(normally called the standard free energy of
activation); these quantities are expressed as
immediately below, we will leave off the subscripted
zero on ∆G0 ‡ , as well as for other thermodynamic
quantities; this simplifies formula construction).

This transition state is somewhat similar to a normal molecule with one important difference. It has
one degree of vibration that is special. The transition state moves along this special vibrational mode
to form product P (or to reform reactants A and B). From the above, we can obtain an expression for
[AB‡ ] in terms of K‡ , [A] and [B], and, thus, an expanded expression for the rate of reaction can be
written as equation

From this equality, we can write that the bimolecular rate constant k is given by the product k'K‡ eq.
Thus, if we can evaluate k' and K‡ eq, we can evaluate k.

In this equation, ∆H0 ‡ is the standard enthalpy of activation and ∆S0 ‡ is the corresponding
standard entropy of activation.From above equation, we can write an expression for K‡ as follows:

Then we can write the following expression for the rate constant k1.

Using statistical mechanical and quantum mechanical reasoning, Professor Henry Eyring calculated
that the value of k' was given by kRT/Nh, where R is the gas constant, T is the absolute temperature,
N is Avogadro's number and h is Planck's constant; k is a constant known as the transmission
coefficient and is often taken to have a value of unity. When the units of the rate constant are in
seconds, the value of k' is given fairly closely by 2x1010T

This equation is known as the transition state equation for bimolecular rate constants; it is often
termed the Eyring equation or the absolute rate equation.

Application of the Eyring Equation:

The linear form of the Eyring Equation is given below:

The values for ΔH‡ and ΔS‡ can be determined from kinetic data
obtained from a lnk/T vs. 1/T plot. The Equation is a straight line
with negative slope, −ΔH‡/R and a y-intercept, ΔS‡/R+ lnkB/h

Potential Energy Surfaces:

The potential-energy surface for a reaction has a reactant region and a product region that are
separated by a barrier. TST chooses a boundary surface located between the reactant and product
regions and assumes that all super molecules that cross this boundary surface become products.

In 1931, Henry Eyring and Michael Polanyi

constructed a potential energy surface for the reaction
below. This surface is a three-dimensional diagram
based on quantum-mechanical principles as well as
experimental data on vibrational frequencies and
energies of dissociation.
H + H2 → H2 + H
The importance of this work was that it was the first
time that the concept of col or saddle point in the
potential energy surface was discussed. They
concluded that the rate of a reaction is determined by
the motion of the system through that col.

Significance:
There are several significance of transistion state theory and some of them are mention here:
Biochemistry:
 Enzymes catalyze chemical reactions at rates that are astounding relative to uncatalyzed
chemistry at the same reaction conditions. Each catalytic event requires a minimum of three or
often more steps, all of which occur within the few milliseconds that characterize typical
enzymatic reactions. According to transition state theory, the smallest fraction of the catalytic
cycle is spent in the most important step, that of the transition state.
 The enzyme's ability to make the reaction faster depends on the fact that it stabilizes the
transition state. The transition state's energy or, in terms of a reaction, the activation energy is the
minimum energy that is needed to break certain bonds of the reactants so as to turn them into
products. Enzymes decreases activation energy by shaping its active site such that it fits the
transition state even better than the substrate. When the substrate binds, the enzyme may stretch
or distort a key bond and weaken it so that less activation energy is needed to break the bond at
 the start of the reaction.

In Chemical Kinetics:

Applications of TST is important in term of deriving an extendable form of rate equation, which can
be used to understand even most complicated or complex reaction in qualitative ways.

In Thermodynamics:

Transition state theory is used to calculate thermodynamic properties such as Gibbs free energy,
entropy and enthalpy etc. Values of the specific surface of the solid, the length of the molecular unit
involved in the decomposition and the solid density must be taken into account to calculate the
entropy of the activated complex.

Limitations of Transition State Theory (TST):

As was mentioned above, the universality of the transition state theory provides a conceptual
foundation for understanding the course and rate of elementary reaction on molecular scale. On the
other hand, the TST theory can fail in some cases, for example;
 If applied to each elementary step of multistep reactions.
 When the intermediates are very short-living, so that the Boltzmann distribution of energies is
not reached before the process continues to the next step.
 The transition state theory also fails for some reactions at high temperatures due to the more
complex motions of molecules or at very low temperatures due to the quantum tunneling.
 Transition state theory fails for some reactions at high temperature. The theory assumes the
reaction system will pass over the lowest energy saddle point on the potential energy surfaceat
high temperatures, molecules populate higher energy vibrational modes; their motion becomes
more complex and collisions may lead to transition states far away from the lowest energy
saddle point.

Conclusions:

Transition state theory assumes that an equilibrium exists between the reactants and the transition
state phase. However, in solution non-equilibrium situations can arise, upsetting the theory. Several
more complex theories have been presented to correct for these and other discrepancies. This theory
still remains largely useful in calculating the thermodynamic properties (Gibbs free energy, enthalpy,
entropy) of the transition state from the overall reaction rate. This presents immense usefulness in
medicinal chemistry, in which the study of transition state analogs is widely implemented.In
addition, transition state theory assumes that an equilibrium exists between the reactants and the
transition state phase. However, in solution non-equilibrium situations can arise, upsetting the theory.
Several more complex theories have been presented to correct for these and other discrepancies. This
theory still remains largely useful in calculating the thermodynamic properties of the transition state
from the overall reaction rate.
 References:
1.  Steinfeld J.I., Francisco J.S. and Hase W.L. Chemical Kinetics and Dynamics (2nd ed.,
Prentice-Hall 1998) p.263 ISBN 0-13-737123-3
2. ^ Atkins P. and de Paula J. Physical Chemistry (8th ed., W.H.Freeman 2006) p.886 ISBN 0-
7167-8759-8
3. ^ Here v is the vibratonal quantum number.
4. ^ Atkins P. and de Paula J. Physical Chemistry (8th ed., W.H.Freeman 2006) p.889-
890 ISBN 0-7167-8759-8
5. Laidler, K.; King, C., Development of transition-state theory. The Journal of Physical
Chemistry 1983, 87, (15), 2657
6. Laidler, K., A lifetime of transition-state theory. The Chemical Intelligencer 1998, 4, (3), 39
7. Schramm, VL., Enzymatic Transition States and Transition State Analog Design. Annual Review of
Biochemistry 1998, 67, 693-720

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