CH2210 – Kinetics; From Polymers to Enzymes

The Basic Principle

In a reaction between A and B an increase in the concentration of either will increase the number of
collisions and so increase the rate at which the reaction occurs. Doubling [A] will double the rate,
doubling both would quadruple the rate.

With respect to A, the rate law can therefore be written as;

k is the rate constant and n the reaction order. The minus sign indicates a decrease in the
concentration of A with time, it is a reagent and not a product.

For a reaction of the form aA+bB→cC+dD rate can be equal to one of four things;

For first order rate laws the differential and integrated forms can give special information;

ln[A]=ln[A]0-kt will give a straight line with a slope equal to –k.

[A]=[A]0exp(-kt) can be used to give the half-life (t1/2), the time taken for half of A to be consumed.

In principle any method of measuring concentration can be used to measure rate.

Rate is temperature dependent, according to a Boltzmann distribution at higher temperatures more

molecules will have the required kinetic energy to react. This relationship is defined by;

A is the Arrhenius constant, Ea the activation energy, R the gas constant and t the temperature.
A catalyst reduces Ea by offering an alternate low energy reaction pathway, thus it also increases the
rate.

Consecutive Unimolecular Reactions

A→B

This reaction is described by a rate constant k 1, as such the concentration of A and the rate can be
related by;

The relation between the concentration of B can then be related to rate by;
This time it is a positive k1 since B is being formed.

From these equations;

For the reaction; A→B→C, the reaction A→B can be defined by the rate k1 and B→C can be defined
by the rate k2.
For the concentrations of A and C the link to rate constants is simple and the same as before;

Since B takes part in two mechanistic steps it becomes harder to define;

If [A]=[A0] and [B]=[C]=0 then;

[A]=[A0]exp(-kt)

This can be substituted into the equation for B to give;

Since [A]+[B]+[C]=[A0];

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Reversible Unimolecular Reactions

Here;

At equilibrium;
Parallel Unimolecular Reactions

Here A→B is given the rate constant k2 and A→C the rate constant k1.

If k2>>>k1 product B will form the majority of the product.

By inspection;

To solve these rate equations approximations are required. The simplest and most common is the
steady-state approximation which assumes that during the major part of the reactions the rates of
changes of the concentrations of the intermediates are negligibly small.

An Example; N2O5 Decomposition

2N2O5(g)→4NO2(g)+O2(g)

This reaction occurs by the following mechanism;

In the above mechanism NO3 and NO are both intermediates, they are formed in one step then
consumed in the subsequent step. When considering the change in [NO] over change in time the
following equation is formed;

Similarly for d[NO3]/dt;

Substituting these equations into the rate equation for N 2O5 gives;

The following values cancel;

To give;

To make the denominator ‘universal’, present in all terms, the first term can be multiplied by the
denominator divided by itself.

This is consistent with the experimentally observed rate law.

Enzyme Kinetic
For a basic enzyme reaction;

From this;

To then find [ES] the steady-state equilibrium can be applied as before;

k2 is often called the ‘turnover number’ of an enzyme that acts in this manner.
For reactions of this type the Michaelis constant (K m) is equal to;

And so;

When [S]>>>Km the fraction will become so small it becomes insignificant and so;
In other words the reaction will be 0th order with respect to [S].

When Km>>>[S] the equation becomes;

In this scenario the reaction is 1st order with respect to [S].

A Lineweaver-Burke plot provides further information about a reaction when only the rate at various
original concentrations of [S] is known, the inverse of the rate equation is used to plot a straight-line
graph on which the gradient of the slope is equal to K m/vmax, the y-intercept equal to 1/vmax and the
x-intercept equal to -1/Km.

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It is possible for an inhibiting species to block the action of an enzyme by entering the active
site and preventing the entry of a substrate molecule. It is also possible for the inhibitor to
bind to the enzyme-substrate complex, the reaction is now shown as;
Based on these two equations a small value of K I and KI’ will suggest an efficient inhibitor.

With no inhibitor;

( )

Depending on KI and KI’, [ES] will be lower in the presence of an inhibitor and so this
becomes;

( )

The α terms are derived by considering the mass balance for the enzyme in the inhibitor
scenario.

[Etotal]=[E]+[ES]+[EI]+[ESI]

Rearranging the equations for KI and KI’ gives;

This gives;

( ) ( )

By plotting a Lineweaver-Burke plot, which is 1/reaction rate against 1/[S] the type of
inhibition present can be determined, since νmax=k[Etotal] if the inhibitor is competitive then a
plot with varying amounts of inhibitor will show a set of crossing lines that meet at the y-
intercept. A non-competitive inhibitor will give lines that cross at the x-intercept.
The Lindemann-Hinshelwood Mechanism for Unimolecular Reactions
Simple reactions such as molecular decompositions can sometimes involve some sort of
complex, the Lindemann-Hinshelwood mechanism proposes such a process.

Here;

Since A* is an intermediate (and so the steady-state approximation may be used);

This expression does now show a simple reaction order, if the rate of deactivation (k -1) is
much greater than the rate of decay then k-1[A]>>k2 and so the reaction is first order
following;

If k-1[A]<<k2 then the reaction will follow a second-order reaction rate;

Chain Reactions
Many reactions, particularly those involving radicals, can be considered chain reactions,
here several reactive species are formed and there are often various pathways for the
reaction to take, making it difficult to track each mechanism accurately and perform kinetic
analysis of the reactions. An example could be the reaction between H2 and Br2 to give
2HBr.

Here;

The proposed mechanism is;

Since H here acts as an intermediate it can be approximated using the Steady-State

approximation that;
Br also acts as an intermediate however and so;

Given that;

√( )√

Putting this equation into the original equation for d[H]/dt ;

√( )√

√( )√

Now placing this into the equation for dBr2/dt;

√( )√

Dividing by [Br2] and consolidating the rate constants gives;

( ) ( )

Polymerisation Kinetics
There are three distinct steps during polymerization;

1. Initiation
an active centre is created to serve as the chain carrier
Initiation may be a free radical or ionic process, initiation will produce two radicals (a
 radical is an atomic or molecular species whose normal bonding system has been
modified and an unpaired electron remains). Examples of initiation include the
heating of benzoyl peroxide (giving two phenyl radicals and 2CO2 molecules) or the
light-induced radicalization of azobisisobutyronitrile (AIBN);

2. Propagation
the chain grows through numerous additions of a monomer to the growing chain
Propagation can be summarized as;
RMn.+M1→RMn+1.
3. Termination
active centre is neutralized and polymerization stops
Termination can occur through several mechanisms;
i) the interaction of two active chain ends
ii) the interaction of an active centre and a free radical
iii) the transfer of the active centre to a separate molecule, a solvent, monomer or
impurity such as O2.

Initiation is a two-stage reaction involving decomposition and radical attack on a monomer

to form the active centre;

The decomposition step is much slower than the rate of attack of a free radical on the
monomer and so is the rate determining step, therefore;

During propagation it is assumed that each radical shows a comparable reactivity and so;
The termination is a bimolecular process related to [M .];

A steady-state is often achieved when the rate of radical formation is equal to the rate of
radical destruction, when νi=νt, here;

This can be substituted into the equation for νp to give;

In other words νp is related to [M1] and √[I].

The average chain length (xn) is proportional to νp/νt and so;

( )
And so xn is related to [M1] and √(1/[I]).

Frequently polymers consist of more than one monomer type, these are defined as
copolymers and the different monomers are often used to provide beneficial properties to
the polymer. Staudinger (1930) realized that the tendency of each monomer to enter the
chain differs markedly when two polymers copolymerize, this effect is known as
composition drift.

It is important to understand how the composition of a polymer evolves over time, and this
can be predicted using knowledge of the monomers involved.

Considering two monomers, M1 and M2, the rate at which these monomers add to a chain
that presents M1* and M2* at the end can be given the constants k11, k22, k12 and k21 where
the first subscript relates to the active centre and the second subscript the approaching
monomer. The first two are self-propagating rates, the second are cross-propagating rates.
By applying the steady-state approximation and assuming that the monomer reactivity is
independent of the chain length, depending only on the nature of the end group then;

Assume then that;

Then;

{ }{ }

Where r1=k11/k12 and r2=k22/k21, the relative reactivity ratios, defined more generally as the
ratio of the reactivity of the propagating species with its own monomer to the reactivity of
the propagating species to the other monomer.

If the monomer mole fractions present within the feed mixture are then defined as f1 and
f2,;

F1 and F2 are the mole fractions of monomer being added to the growing chain at any given
time;

The above equation may also be written as;

The Q-e scheme can be used to estimate r1 and r2, introducing three new terms, Q - the
measure of resonance stabilization of the double bond, and P - a characteristic of the radical
active centre and e – the measure of the electrostatic character of the monomer, each k
term can be rewritten as;
And so;

( )

( )
{ }

Q and e are literature values and so can often be placed directly into the necessary equation
to calculate r1 and r2 values.

Diffusion Controlled Reactions

Reactions in solution occur very differently to reactions in the gas phase. In solution the
molecules must diffuse through the solvent before reacting, hence the collision frequency is
vastly reduced when compared to gaseous reactions. Due to this diffusion process,
however, a given arrangement of particles has a much longer lifetime, and so even if
molecules originally colliding are without the required energy to react there is a longer time-
period over which to acquire that energy. For reactions in a solution the activation energy is
therefore a much more complex parameter to consider.

For the reaction A+B→AB, νd=kd[A][B] where ‘d’ denotes diffusion. The pair of atoms may
then break up without reaction or continue to form products, AB→A+B for which ν=k’d[A][B]
or AB→Products for which ν=ka[AB].
By applying the steady-state approximation;

Also;

There are now two limiting scenarios that may be applied, if the rate of separation of the
unreacted molecules is much slower than the rate at which products are formed, i.e.
k’d<<<ka then;

And the process has a diffusion controlled limit.

If the opposite is true and k’d>>>ka;

And the process has an activation controlled limit.

To calculate the rate of a diffusion controlled reaction the rates of diffusion of the reactants
must be considered;

Where R* is the separation of the species and D is the sum of the diffusion coefficients;

( )

( )

There is no dependence of the rate constant on the size of the species, it is only the
temperature and the viscosity, ƞ, that are important.