THE COLLISION THEORY OF REACTION

RATES
This page describes the collision theory of reaction rates. It
concentrates on the key things which decide whether a particular
collision will result in a reaction - in particular, the energy of the
collision, and whether or not the molecules hit each other the right
way around (the orientation of the collision).
The individual factors which affect the rate of a reaction
(temperature, concentration, and so on) are discussed on separate
pages. You can get at these via the rates of reaction menu - there
is a link at the bottom of the page.
We are going to look in detail at reactions which involve a collision
between two species.
Species: This is a useful term which covers any sort of particle you like molecule, ion, or free radical.

Reactions where a single species falls apart in some way are

slightly simpler because you won't be involved in worrying about
the orientation of collisions. Reactions involving collisions between
more than two species are going to be extremely uncommon (see
below).

Reactions involving collisions between two species

It is pretty obvious that if you have a situation involving two species
they can only react together if they come into contact with each
other. They first have to collide, and then they mayreact.

Why "may react"? It isn't enough for the two species to collide they have to collide the right way around, and they have to collide
with enough energy for bonds to break.
(The chances of all this happening if your reaction needed a
collision involving more than 2 particles are remote. All three (or
more) particles would have to arrive at exactly the same point in
space at the same time, with everything lined up exactly right, and
having enough energy to react. That's not likely to happen very
often!)
The orientation of collision
Consider a simple reaction involving a collision between two
molecules - ethene, CH2=CH2, and hydrogen chloride, HCl, for
example. These react to give chloroethane.

As a result of the collision between the two molecules, the double

bond between the two carbons is converted into a single bond. A
hydrogen atom gets attached to one of the carbons and a chlorine
atom to the other.
Note: The mechanism for this reaction is dealt with on a separate page.
This might help you to understand why the orientation of the two molecules is
so important.
If you want to read a bit more about this, follow this link and use the BACK
button on your browser to return to this page.

The reaction can only happen if the hydrogen end of the H-Cl bond
approaches the carbon-carbon double bond. Any other collision
between the two molecules doesn't work. The two simply bounce
off each other.

Of the collisions shown in the diagram, only collision 1 may

possibly lead on to a reaction.
If you haven't read the page about the mechanism of the reaction,
you may wonder why collision 2 won't work as well. The double
bond has a high concentration of negative charge around it due to
the electrons in the bonds. The approaching chlorine atom is also
slightly negative because it is more electronegative than hydrogen.
The repulsion simply causes the molecules to bounce off each
other.
Note: If you aren't sure about electronegativity , you might like to follow this
link.
Use the BACK button on your browser to return to this page.

In any collision involving unsymmetrical species, you would expect

that the way they hit each other will be important in deciding
whether or not a reaction happens.

The energy of the collision

Activation Energy
Even if the species are orientated properly, you still won't get a
reaction unless the particles collide with a certain minimum energy
called the activation energy of the reaction.
Activation energy is the minimum energy required before a reaction
can occur. You can show this on an energy profile for the reaction.
For a simple over-all exothermic reaction, the energy profile looks
like this:

Note: The only difference if the reaction was endothermic would be the
relative positions of the reactants and productslines. For an endothermic
change, the products would have a higher energy than the reactants, and so
the green arrow would be pointing upwards. It makes no difference to the
discussion about the activation energy.

If the particles collide with less energy than the activation energy,
nothing important happens. They bounce apart. You can think of
the activation energy as a barrier to the reaction. Only those
collisions which have energies equal to or greater than the
activation energy result in a reaction.
Any chemical reaction results in the breaking of some bonds
(needing energy) and the making of new ones (releasing energy).
Obviously some bonds have to be broken before new ones can be
made. Activation energy is involved in breaking some of the original
bonds.
Where collisions are relatively gentle, there isn't enough energy
available to start the bond-breaking process, and so the particles
don't react.

The Maxwell-Boltzmann Distribution

Because of the key role of activation energy in deciding whether a
collision will result in a reaction, it would obviously be useful to
know what sort of proportion of the particles present have high
enough energies to react when they collide.
In any system, the particles present will have a very wide range of
energies. For gases, this can be shown on a graph called the
Maxwell-Boltzmann Distribution which is a plot of the number of
particles having each particular energy.
Note: The graph only applies to gases, but the conclusions that we can
draw from it can also be applied to reactions involving liquids.

The area under the curve is a measure of the total number of

particles present.
Note: The reason for this lies in some maths beyond the scope of an A'level
chemistry course. It is important that you remember that the area under the
curve gives a count of the number of particles even if you don't understand
why!

The Maxwell-Boltzmann Distribution and activation energy

Remember that for a reaction to happen, particles must collide with
energies equal to or greater than the activation energy for the
reaction. We can mark the activation energy on the MaxwellBoltzmann distribution:

Notice that the large majority of the particles don't have enough
energy to react when they collide. To enable them to react we
either have to change the shape of the curve, or move the
activation energy further to the left. This is described on other
pages.
Note: You can change the shape of the curve by changing the
temperature of the reaction. You can change the position of the activation
energy by adding a catalyst to the reaction.
You could either go straight to these pages if you are interested, or access
them later via the rates of reaction menu (link at the bottom of the page).

Questions to test your understanding

If this is the first set of questions you have done, please read theintroductory
page before you start. You will need to use the BACK BUTTON on your
browser to come back here afterwards.

questions on the collision theory

answers

Where would you like to go now?

To the rates of reaction menu . . .
To the Physical Chemistry menu . . .
To Main Menu . . .

Jim Clark 2002 (modified October 2013)

Back to Table of Contents

[TOP]

A Theoretical approach to reaction rates:

The Collision theory and the Activated Complex Theory
In this section we will be deriving from first principles the rate law for the chemical equation A +
B -> P, given empirically by v = k[A][B]. This will be done through:

(1) Collision theory

(1-1) The reaction profile in the Collision theory:
(1-2) Derivation of the rate law through the Collision theory:

(2) Activated complex theory

(2-1) The reaction profile in the ACT
(2-2) Derivation of the rate law through the ACT (the thermodynamic derivation):

(2-3) The activated complex theory and reactions between ions.

[ TOP ]

(1) Collision theory

In this section we shall attempt to understand the origin of the Arrhenius parameters by studying
a class of gas-phase reactions in which reaction occurs when two molecules meet (collision
theory).
Under this theory, reaction occurs only if two molecules collide with a certain minimum kinetic
energy along their line of approach (Fig. 1). In fact, in the collision theory, a reaction resembles
the collision of two defective billiard balls: the balls bounce apart if they collide with only a
small energy, but might smash each other into fragments (products) if they collide with more
than a certain minimum kinetic energy. This model of a reaction is a reasonable first
approximation to the types of process that take place in planetary atmospheres and govern their
compositions and temperature profiles.
NOTE: The importance of the collision theory is that it provides a 'proof' from first principles
that reactions (or, strictly speaking, gas phase reactions!) can indeed display Arrhenius-like
behaviour.

Fig. 1: In the collision theory of gas-phase chemical reactions, reaction occurs when two
molecules collide, but only if the collision is sufficiently vigorous, (a) An insufficiently vigorous
collision: the reactant molecules collide but bounce apart unchanged, (b) A sufficiently vigorous
collision results in a reaction.
[ TOP ]

(1-1) The reaction profile in the Collision theory:

A reaction profile in collision theory is a graph showing the variation in potential energy as one
reactant molecule approaches another and the products then separate (Fig 2). (NOTE: Recall that
the potential energy of an object is the energy arising from its position (not speed), in this case
the separation of the two reactant molecules as they approach, react, and then separate as
products.)

Fig. 2: A reaction profile. The graph depicts schematically the changing potential energy of two
species that approach, collide, and then go on to form products. The activation energy is the
height of the barrier above the potential energy of the reactants.
This profile shows:

On the left, the horizontal line represents the potential energy of the two reactant
molecules that are far apart from one another.

The potential energy rises from this value only when the separation of the molecules is so
small that they are in contact, when it rises as bonds bend and start to break.

The potential energy reaches a peak when the two molecules are highly distorted.

Then it starts to decrease as new bonds are formed.

At separations to the right of the maximum, the potential energy rapidly falls to a low
value as the product molecules separate.

For the reaction to be successful, the reactant molecules must approach with sufficient kinetic
energy along their line of approach to carry them over the activation barrier, the peak in the

reaction profile. As we shall see, we can identify the height of the activation barrier with the
activation energy of the reaction.
[ TOP ]

(1-2) Derivation of the rate law through the Collision theory:

With the reaction profile in mind, the collision theory predics that the rate law for a reaction:

is proportional to:
(a) The encounter rate;
(b) The minimum energy requirement;
(c) The steric factor.
where:
(a) The encounter rate:
The rate of collisions between species A and B is proportional to both their concentrations: if the
concentration of B is doubled, then the rate at which A molecules collide with B molecules is
doubled, and, if the concentration of A is doubled, then the rate at which B molecules collide
with A molecules is also doubled. The kinetic theory of gasses goes even a step further and
allows us to write:

where NA is Avogadro's constant, kB is Boltzmann's constant, T is the temperature, is the

collision cross-section (see fig. 3), and is the reduced mass given by:

Fig. 3: The collision cross-section for two molecules can be regarded to be the area within which
the centre of the projectile molecule (A) must enter around the target molecule (B) in order for a
collision to occur. If the diameters of the two molecules are dA and dB, the radius of the target
area is d = 1/2 (dA + dB) and the cross-section is d2.
(b) The minimum energy requirement:
Next, we need to multiply the collision rate by a factor f that represents the fraction of collisions
that occur with at least a kinetic energy Ea along the line of approach (Fig 4), for only these
collisions will lead to the formation of products. Molecules that approach with less than a kinetic
energy Ea will behave like a ball that rolls toward the activation barrier, fails to surmount it, and
rolls back.

Fig. 4: The criterion for a successful collision is that the two reactant species should collide with
a kinetic energy along their line of approach that exceeds a certain minimum value Ea that is
characteristic of the reaction. The two molecules might also have components of velocity (and an
associated kinetic energy) in other directions (for example, the two molecules depicted here
might be moving up the page as well as towards each other): but only the energy associated with
their mutual approach can be used to overcome the activation energy.
It follows from very general arguments concerning the probability that a molecule has a specified
energy that the fraction of collisions that occur with at least a kinetic energy Ea is (from the
kinetic theory of gasses):

i.e. at this stage we can conclude that the rate of reaction, which is proportional to the rate of
collision multiplied by the fraction of successful collisions, is:

Note that this equation now has the Arrehenius form, i.e.:

This means that at this stage we can already conclude that The activation energy, Ea, is the

minimum kinetic energy required for a collision to result in reaction.

(c) The steric factor
However, it is often found that the experimental value of A is smaller than that calculated from
the kinetic theory so far, i.e.:

One possible explanation is that, not only must the molecules collide with sufficient kinetic
energy, but they must also come together in a specific relative orientation (Fig 5).
It follows that the reaction rate is proportional to the probability that the encounter occurs in the
correct relative orientation. The pre-exponential factor A should therefore include a steric
factor,P, which usually lies between 0 (no relative orientations lead to reaction) and 1 (all
relative orientations lead to reaction).
E.g. 1: The reactive collision in which two NOCl molecules collide and break apart into two NO
molecules and a Cl2 molecule:

E.g. 2: For the hydrogen addition reaction in which a hydrogen molecule attaches directly to an
ethene molecule to form an ethane molecule:
This very low value of P which suggests that the reaction has very stringent orientational
requirements.
Some reactions have P > 1. Such a value may seem absurd, because it appears to suggest that the
reaction occurs more often than the molecules meet! An example of a reaction of this kind is the
reaction in which a K atom plucks a Br atom out of a Br2 molecule:

In this reaction, the distance of approach at which reaction can occur seems to be considerably
larger than the distance needed for deflection of the path of the approaching molecules in a nonreactive collision! To explain this surprising conclusion, it has been proposed that the reaction
proceeds by a 'harpoon mechanism'.
ASIDE: The harpoon mechanism is based on a model of the reaction that pictures the K atom as approaching the
Br2 molecules, and when the two are close enough an electron (the harpoon) flips across to the Br 2 molecule. In
place of two neutral particles there are now two ions, and so there is a Coulombic attraction between them: this
attraction is the line on the harpoon. Under its influence the ions move together (the line is wound in), the reaction
takes place, and KBr and Br emerge. The harpoon extends the cross-section for the reactive encounter and we would

greatly underestimate the reaction rate if we used for the collision cross-section the value for simple mechanical
contact between K and Br2.

Fig. 5: Energy is not the only criterion of a successful reactive encounter, for relative orientation
may also play a role. (a) In this collision, the reactants approach in an inappropriate relative
orientation, and no reaction occurs even though their energy is sufficient, (b) In this encounter,
both the energy and the orientation are suitable for reaction.

[ TOP ]

(2) Activated complex theory

The activated complex theory (ACT), formerly known as the transition state theory, is a more
sophisticated theory of reaction rates that offers the following advantages over the collision
theory:
1. It can be applied to reactions taking place in solution as well as in the gas phase;
2. The advantage that a quantity corresponding to the steric factor appears automatically, in

contrast to the collision theory where P had to be grafted on as an afterthought.

NOTES:
(1) The concepts used in the derivation of the rate constants in terms of the ACT are based on
statistical thermodynamics.
(2) The reason why P appears automatically in the ACT framework is that the orientation
requirements are carried in the entropy of activation. Thus, if there are strict orientation
requirements (for example, in the approach of a substrate molecule to an enzyme), then the
entropy of activation will be strongly negative (representing a decrease in disorder when the
activated complex forms), and the pre-exponential factor will be small. In practice, it is
occasionally possible to estimate the sign and magnitude of the entropy of activation and hence
to estimate the rate constant.
(3) The general importance of activated complex theory is that it shows that even a complex
series of events (not only a collisional encounter in the gas phase) displays Arrhenius-like
behaviour, and that the concept of activation energy is applicable.

[ TOP ]
(2-1) The reaction profile in the ACT:
Activated complex theory is an attempt to identify the principal features governing the
magnitude of a rate constant in terms of a model of the events that take place during the reaction.
Let us have a look at a typical the reaction profile (i.e.a plot of the 'potential energy' vs. 'reaction
coordinate'), for a bimolecular reaction between A and B forming products P (fig. 6). This plot
illustartes the following features:

Initially, only reactants A and B are present.

As the reaction event proceeds, A and B come into contact, distort, and begin to exchange
or discard atoms.

The potential energy rises to a maximum and the cluster of atoms that corresponds to the
region close to the maximum are referred to the activated complex, (AB) or C. The
configuration at the actual peak of the potential energy curve is called the transition
state.

After the maximum, the potential energy falls as the atoms rearrange in the cluster, and it
reaches a value that is characteristic of the products, P.

NOTE: At the transition state, the two reactant molecules have come to such a degree of
closeness and distortion that a small further distortion will send them in the direction of products.

(Although some molecules entering the transition state revert to reactants, if they pass through
this configuration then it is inevitable that products will emerge from the encounter.)

Fig. 6: A reaction profile. The horizontal axis is the reaction coordinate, and the vertical axis is
potential energy. The activated complex is the region near the potential maximum, and the
transition state corresponds to the maximum itself.
In other words we have:

which in terms for the ACT, we have:

or:
i.e. the reaction between A and B proceeding through the formation of an activated complex, C,
that falls apart by unimolecular decay into products, P. Note that we not all (AB) will proceed to
products, and in fact, some will decay back to A and B, i.e.
The scope now becomes to derive an expression for k2 from first principles, which as we have
said before, is done through concepts from statistical thermodynamics. This formulation is
known as the Eyring equation.
[ TOP ]
(2-2) Derivation of the rate law through the ACT (the thermodynamic derivation):

In a simple form of activated complex theory, we suppose that the activated complex is in
equilibrium with the reactants (pre-equilibrium), and that we can express its abundance in the
reaction mixture in terms of an equilibrium constant, K.

Then, if we suppose that the rate at which products are formed is proportional to the
concentration of the activated complex, we can write:
The full activated complex theory gives an estimate of the constant of proportionality to give:

Thus, if we compare this expression with the form of the rate law, i.e.:
we would find:

But since we may think of K as an equilibrium constant, then it may be expressed in terms of the
standard reaction Gibbs energy, or in this context, the activation Gibbs energy, and written G.
It follows that:
i.e.:

But:
i.e.:

This expression has the form of the Arrhenius expression, i.e.:

if we identify the enthalpy of activation, H, with the activation energy and the term in square
brackets, which depends on the entropy of activation, S, with the pre-exponential factor.

[ TOP ]

(2-3) The activated complex theory and reactions between ions.

The simplified (thromodynamic) approach to the activated complex theory simplifies the
discussion of reactions in solution. We can combine the rate law:

with the thermodynamic equilibrium constant:

i.e.:

Let us now define ko2 as the rate constant with the activity coefficients equal to 1, i.e.:

At low concentrations the activity coefficients can be expressed in terms of the ionic strength, I,
of the solution by using the Debye-Huckel limiting law (see P.W. Atkins, Physical Chemistry,
6th Ed. Section 10.2c, particularly eqn 10.19) in the form:

where A = 0.509 in aqueous solution at 298 K and zJ is the charge numbers on particle J.
Thus,

(Eqn. K.Salt.Effect)
This equation expresses the kinetic salt effect, the variation of the rate constant of a reaction
between ions with the ionic strength of the solution (see fig. 6):

If the reactant ions have the same sign (as in a reaction between cations, or, between
anions), then increasing the ionic strength by the addition of inert ions increases the
rate constant.

Conversely, ions of opposite charge react more slowly in solutions of high ionic
strength.

This because if reactant ions have the same sign, the formation of a single, highly charged ionic
complex from two less highly charged ions is favoured by a high ionic strength because the new
ion has a denser ionic atmosphere and interacts with that atmosphere more strongly.
Conversely, if reactant ions have opposite same signs, the charges in the activated complex
cancel out and the complex has a less favourable interaction with its atmosphere than the
separated ions with a solution of a high ionic strength.
>> TECHNICAL NOTE: A plot of log(k/k0) vs. l1/2 should be linear wheer the gradient gtives
infomation about the charge type of the activated complex for the rate determining step. (see Fig
5 below).

Fig. 6: Experimental tests of the kinetic salt effect for reactions in water at 298 K. The ion types
are shown as spheres, and the slopes of the lines are those given by the Debye-Hckel limiting
law and the Kinetic salt effect equation above (Eqn. K.Salt.Effect).

Collision Theory and Transition

State Theory
It has been recognized for a long time that the rate of reaction is markedly
affected by temperature. In fact, it is generally found that by increasing the
reaction temperature by 10K approximately doubles the rate of reaction. Two

theories - the collision theory and the transition state theory have been
developed to explain this temperature effect. The collision theory is based on
the kinetic theory and assumes a collision between reactants before a reaction
can take place. The transition state theory suggests that as reactant molecules
approach each other closely they are momentarily in a less stable state than
either the reactants or the products. Both of these classical theories provide
upper limits of enzyme catalysis.
Like all catalysts, enzymes decrease the energy required to a reaction started. It
does this by decreasing the activation energy needed to form the transition
state.

The key points for these theories are:

1. All reactions involving two reactants require collisions between particles
to proceed.
2. Not all collisions taking place between particles results in a reaction.
3. In the middle of a reaction, there is a configuration of the particles,
which is difficult to achieve - this is the Transition State.
4. The total kinetic energy of reactant molecules must be at least as high as
the activation energy in order to achieve the Transition State so the
reaction can proceed.
5. The Transition State does not always proceed to the products of the
reaction - it can also return to reactant molecules.
Collision Theory
Transition State Theory

Collision Theory

Enzymes are biological catalysts that enhance the rate of a reaction by several
mechanisms. Making a clear determination of the predominant mechanism is
difficult. One may wonder if there is a physical limit to the rate of a chemical
reaction? There is indeed such an upper limit; and two theories provide an
estimate of the rate constant.
Collision Theory
Collision theory basically states for a bimolecular reaction to occur, molecules
must:
1. Collide with one another to initiate a reaction.
2. Collide with a sufficient amount of energy.
3. Collide in a specific orientation.

Click to view a reaction:

4. For a bimolecular reaction in the gas of liquid state the rate
constant can be expressed by:

5. Where:
Z: The frequency of collisions between two molecules A
and B that posses enough energy to overcome the energy
barrier for a reaction to occur. .
p: The fraction of molecules that have the correct
orientation for a reaction. (To get the upper limit of the rate
coefficient we assume that p = 1)

 Ea: The minimum activation energy for reaction.

Frequency of collisions Z:
The frequency Z can be correlated a number of ways:
Maxwell-Boltzman distribution curve is a plot of
the fraction of particles with a particular kinetic
energy against kinetic energy values. Z can be calculated
by taking the area under the curve that is greater than the
minimum activation energy. Increasing the temperature of a
reaction increases this area under the curve, which results
in a greater Z.
Z can also be calculated by:

Where:
N: Avogadros number
DA: Diffusion coefficient of molecule A
DB: Diffusion coefficient of molecule B
rA: Radii of molecule A
rB: Radii of molecule B
Z can also be expressed in terms of fluid viscosity, temperature, and radii of reacting species
by the Stokes-Einstein equation:

Where:

kb: Boltzmann constant

: Fluid viscosity

Substitution yields a new equation for Z:

Where R is the universal gas constant.

Transition State Theory

Theory
In the transition state theory, the mechanism of interaction of reactants is not
considered; the important criterion is that colliding molecules must have sufficient
energy to overcome a potential energy barrier (the activation energy) to react.
For a bimolecular reaction, a transition state is formed when the two molecules old
bonds are weakened and new bonds begin to form or the old bonds break first to form
the transition state and then the new bonds form after. The theory suggests that as
reactant molecules approach each other closely they are momentarily in a less stable
state than either the reactants or the products. In the example below, the first scenario
occurs to form the transition state:

It takes a lot of energy to achieve the transition state, so the state is a high-energy
substance. The potential energy of the system increases at this point because:
The approaching reactant molecules must overcome the mutual repulsive forces
between the outer shell electrons of their constituent atoms
Atoms must be separated from each other as bonds are broken

Bond Transition
This increase in potential energy corresponds to an energy barrier over which the
reactant molecules must pass if the reaction is to proceed. The transition state occurs
at the maximum of this energy barrier.
The transition state is an unstable transitory combination of reactant molecules
that occurs at a potential energy maximum
The combination can either go on to form products or fall apart to return to the
unchanged reactants.
The energy difference between the reactants and the potential energy maximum
is referred to as the activation energy

The equation for an enzymatic reaction is:

is the concentration equilibrium constant, defined as:

Use the following equation to find the rate constant (k):

, where kB is Boltzmanns constant, h is Plancks constant and T is the

temperature

Thermodynamics
resembles the equilibrium constant used to describe Gibbs free energy, defined
as:

where co is the standard state concentration. Gt can be defined as the Gibbs energy of
activation. The Gibbs energy difference between the ground and transition state can be
used to predict the rate of reaction. The binding energy associated with the specific
substrate-enzyme interaction is a significant factor in lowering the Gibbs free energy
change required for reaction. The large binding energies of substrates are due in part
to the complementary shape of the active site of the enzyme. The Gibbs energy can be
considered to be composed of two terms, Gt, the binding energy and Gs, the
activation energy involved in the making and breaking of bonds leading to the
transition state
from enzyme-substrate intermediate (ES). They are related as
follows:
Gt = Gt + Gs
This can be seen on the energy diagram below:

The above equation can be substituted into the equation for the rate constant k, and k
is defined as a second order constant (kcat/KM).

Entropy is composed of translational, rotational, and internal entropies. When

two molecules react without a catalyst there is a loss of rotational and
translational entropies. An enzyme brings together the reactants as an effective
intramolecular adduct that will not suffer the previous losses. There will only
be a small loss of internal entropy. Therefore this reaction will be entropically
favored.
A sample calculation can be done below to find the entropic contribution to a
reaction for the following equation:
Entropy Difference Between Ground and Activated States
Enter in values with appropriate units
Temperature

Rate Constant

s-1

Enthalpy Difference

J/mol

Entropy Difference:

Transition State Theory

Theory
In the transition state theory, the mechanism of interaction of reactants is not
considered; the important criterion is that colliding molecules must have sufficient
energy to overcome a potential energy barrier (the activation energy) to react.
For a bimolecular reaction, a transition state is formed when the two molecules old
bonds are weakened and new bonds begin to form or the old bonds break first to form
the transition state and then the new bonds form after. The theory suggests that as
reactant molecules approach each other closely they are momentarily in a less stable
state than either the reactants or the products. In the example below, the first scenario
occurs to form the transition state:

It takes a lot of energy to achieve the transition state, so the state is a high-energy
substance. The potential energy of the system increases at this point because:

 The approaching reactant molecules must overcome the mutual repulsive forces
between the outer shell electrons of their constituent atoms
Atoms must be separated from each other as bonds are broken

Bond Transition
This increase in potential energy corresponds to an energy barrier over which the
reactant molecules must pass if the reaction is to proceed. The transition state occurs
at the maximum of this energy barrier.
The transition state is an unstable transitory combination of reactant molecules
that occurs at a potential energy maximum
The combination can either go on to form products or fall apart to return to the
unchanged reactants.
The energy difference between the reactants and the potential energy maximum
is referred to as the activation energy

The equation for an enzymatic reaction is:

is the concentration equilibrium constant, defined as:

Use the following equation to find the rate constant (k):

, where kB is Boltzmanns constant, h is Plancks constant and T is the

temperature

Thermodynamics
resembles the equilibrium constant used to describe Gibbs free energy, defined
as:

where co is the standard state concentration. Gt can be defined as the Gibbs energy of
activation. The Gibbs energy difference between the ground and transition state can be
used to predict the rate of reaction. The binding energy associated with the specific
substrate-enzyme interaction is a significant factor in lowering the Gibbs free energy
change required for reaction. The large binding energies of substrates are due in part
to the complementary shape of the active site of the enzyme. The Gibbs energy can be
considered to be composed of two terms, Gt, the binding energy and Gs, the
activation energy involved in the making and breaking of bonds leading to the
transition state
from enzyme-substrate intermediate (ES). They are related as
follows:
Gt = Gt + Gs
This can be seen on the energy diagram below:

The above equation can be substituted into the equation for the rate constant k, and k
is defined as a second order constant (kcat/KM).

Entropy is composed of translational, rotational, and internal entropies. When

two molecules react without a catalyst there is a loss of rotational and
translational entropies. An enzyme brings together the reactants as an effective
intramolecular adduct that will not suffer the previous losses. There will only
be a small loss of internal entropy. Therefore this reaction will be entropically
favored.
A sample calculation can be done below to find the entropic contribution to a
reaction for the following equation:
Entropy Difference Between Ground and Activated States
Enter in values with appropriate units
Temperature

Rate Constant

s-1

Enthalpy Difference

J/mol

Entropy Difference:

Transition State Theory

Theory
In the transition state theory, the mechanism of interaction of reactants is not
considered; the important criterion is that colliding molecules must have sufficient
energy to overcome a potential energy barrier (the activation energy) to react.
For a bimolecular reaction, a transition state is formed when the two molecules old
bonds are weakened and new bonds begin to form or the old bonds break first to form
the transition state and then the new bonds form after. The theory suggests that as
reactant molecules approach each other closely they are momentarily in a less stable
state than either the reactants or the products. In the example below, the first scenario
occurs to form the transition state:

It takes a lot of energy to achieve the transition state, so the state is a high-energy
substance. The potential energy of the system increases at this point because:
The approaching reactant molecules must overcome the mutual repulsive forces
between the outer shell electrons of their constituent atoms
Atoms must be separated from each other as bonds are broken

Bond Transition
This increase in potential energy corresponds to an energy barrier over which the
reactant molecules must pass if the reaction is to proceed. The transition state occurs
at the maximum of this energy barrier.
The transition state is an unstable transitory combination of reactant molecules
that occurs at a potential energy maximum
The combination can either go on to form products or fall apart to return to the
unchanged reactants.
The energy difference between the reactants and the potential energy maximum
is referred to as the activation energy

The equation for an enzymatic reaction is:

is the concentration equilibrium constant, defined as:

Use the following equation to find the rate constant (k):

, where kB is Boltzmanns constant, h is Plancks constant and T is the

temperature

Thermodynamics
resembles the equilibrium constant used to describe Gibbs free energy, defined
as:

where co is the standard state concentration. Gt can be defined as the Gibbs energy of
activation. The Gibbs energy difference between the ground and transition state can be
used to predict the rate of reaction. The binding energy associated with the specific
substrate-enzyme interaction is a significant factor in lowering the Gibbs free energy
change required for reaction. The large binding energies of substrates are due in part
to the complementary shape of the active site of the enzyme. The Gibbs energy can be
considered to be composed of two terms, Gt, the binding energy and Gs, the
activation energy involved in the making and breaking of bonds leading to the
transition state
from enzyme-substrate intermediate (ES). They are related as
follows:
Gt = Gt + Gs
This can be seen on the energy diagram below:

The above equation can be substituted into the equation for the rate constant k, and k
is defined as a second order constant (kcat/KM).

Entropy is composed of translational, rotational, and internal entropies. When

two molecules react without a catalyst there is a loss of rotational and
translational entropies. An enzyme brings together the reactants as an effective
intramolecular adduct that will not suffer the previous losses. There will only
be a small loss of internal entropy. Therefore this reaction will be entropically
favored.
A sample calculation can be done below to find the entropic contribution to a
reaction for the following equation:
Entropy Difference Between Ground and Activated States
Enter in values with appropriate units
Temperature

Rate Constant

s-1

Enthalpy Difference

J/mol

Entropy Difference:

Transition State Theory

Theory
In the transition state theory, the mechanism of interaction of reactants is not
considered; the important criterion is that colliding molecules must have sufficient
energy to overcome a potential energy barrier (the activation energy) to react.
For a bimolecular reaction, a transition state is formed when the two molecules old
bonds are weakened and new bonds begin to form or the old bonds break first to form
the transition state and then the new bonds form after. The theory suggests that as
reactant molecules approach each other closely they are momentarily in a less stable
state than either the reactants or the products. In the example below, the first scenario
occurs to form the transition state:

It takes a lot of energy to achieve the transition state, so the state is a high-energy
substance. The potential energy of the system increases at this point because:
The approaching reactant molecules must overcome the mutual repulsive forces
between the outer shell electrons of their constituent atoms
Atoms must be separated from each other as bonds are broken

Bond Transition
This increase in potential energy corresponds to an energy barrier over which the
reactant molecules must pass if the reaction is to proceed. The transition state occurs
at the maximum of this energy barrier.
The transition state is an unstable transitory combination of reactant molecules
that occurs at a potential energy maximum
The combination can either go on to form products or fall apart to return to the
unchanged reactants.
The energy difference between the reactants and the potential energy maximum
is referred to as the activation energy

The equation for an enzymatic reaction is:

is the concentration equilibrium constant, defined as:

Use the following equation to find the rate constant (k):

, where kB is Boltzmanns constant, h is Plancks constant and T is the

temperature

Thermodynamics
resembles the equilibrium constant used to describe Gibbs free energy, defined
as:

where co is the standard state concentration. Gt can be defined as the Gibbs energy of
activation. The Gibbs energy difference between the ground and transition state can be
used to predict the rate of reaction. The binding energy associated with the specific
substrate-enzyme interaction is a significant factor in lowering the Gibbs free energy
change required for reaction. The large binding energies of substrates are due in part
to the complementary shape of the active site of the enzyme. The Gibbs energy can be
considered to be composed of two terms, Gt, the binding energy and Gs, the
activation energy involved in the making and breaking of bonds leading to the
transition state
from enzyme-substrate intermediate (ES). They are related as
follows:
Gt = Gt + Gs
This can be seen on the energy diagram below:

The above equation can be substituted into the equation for the rate constant k, and k
is defined as a second order constant (kcat/KM).

Entropy is composed of translational, rotational, and internal entropies. When

two molecules react without a catalyst there is a loss of rotational and
translational entropies. An enzyme brings together the reactants as an effective
intramolecular adduct that will not suffer the previous losses. There will only
be a small loss of internal entropy. Therefore this reaction will be entropically
favored.
A sample calculation can be done below to find the entropic contribution to a
reaction for the following equation:
Entropy Difference Between Ground and Activated States
Enter in values with appropriate units
Temperature

Rate Constant

s-1

Enthalpy Difference

J/mol

Entropy Difference:

Transition State Theory

Theory
In the transition state theory, the mechanism of interaction of reactants is not
considered; the important criterion is that colliding molecules must have sufficient
energy to overcome a potential energy barrier (the activation energy) to react.
For a bimolecular reaction, a transition state is formed when the two molecules old
bonds are weakened and new bonds begin to form or the old bonds break first to form
the transition state and then the new bonds form after. The theory suggests that as
reactant molecules approach each other closely they are momentarily in a less stable
state than either the reactants or the products. In the example below, the first scenario
occurs to form the transition state:

It takes a lot of energy to achieve the transition state, so the state is a high-energy
substance. The potential energy of the system increases at this point because:
The approaching reactant molecules must overcome the mutual repulsive forces
between the outer shell electrons of their constituent atoms
Atoms must be separated from each other as bonds are broken

Bond Transition
This increase in potential energy corresponds to an energy barrier over which the
reactant molecules must pass if the reaction is to proceed. The transition state occurs
at the maximum of this energy barrier.
The transition state is an unstable transitory combination of reactant molecules
that occurs at a potential energy maximum
The combination can either go on to form products or fall apart to return to the
unchanged reactants.
The energy difference between the reactants and the potential energy maximum
is referred to as the activation energy

The equation for an enzymatic reaction is:

is the concentration equilibrium constant, defined as:

Use the following equation to find the rate constant (k):

, where kB is Boltzmanns constant, h is Plancks constant and T is the

temperature

Thermodynamics
resembles the equilibrium constant used to describe Gibbs free energy, defined
as:

where co is the standard state concentration. Gt can be defined as the Gibbs energy of
activation. The Gibbs energy difference between the ground and transition state can be
used to predict the rate of reaction. The binding energy associated with the specific
substrate-enzyme interaction is a significant factor in lowering the Gibbs free energy
change required for reaction. The large binding energies of substrates are due in part
to the complementary shape of the active site of the enzyme. The Gibbs energy can be
considered to be composed of two terms, Gt, the binding energy and Gs, the
activation energy involved in the making and breaking of bonds leading to the
transition state
from enzyme-substrate intermediate (ES). They are related as
follows:
Gt = Gt + Gs
This can be seen on the energy diagram below:

The above equation can be substituted into the equation for the rate constant k, and k
is defined as a second order constant (kcat/KM).

Entropy is composed of translational, rotational, and internal entropies. When

two molecules react without a catalyst there is a loss of rotational and
translational entropies. An enzyme brings together the reactants as an effective
intramolecular adduct that will not suffer the previous losses. There will only
be a small loss of internal entropy. Therefore this reaction will be entropically
favored.
A sample calculation can be done below to find the entropic contribution to a
reaction for the following equation:
Entropy Difference Between Ground and Activated States
Enter in values with appropriate units
Temperature

Rate Constant

s-1

Enthalpy Difference

J/mol

Entropy Difference: