Physical Chemistry Chapter 11 3 Atkins

Homogeneous Catalysis
A catalyst(, ) is a substance that accelerates a reaction

but undergoes no net chemical change.
- The catalyst lowers the activation energy of the reaction by
providing an alternative path that avoids the slow, rate-determining
step of the uncatalyzed reaction.
- The decomposition of H2O2 in
solution, Ea : 76 KJmol-1
I- added , Ea : 57 KJmol-1
The rate constant increases by
order of 2000.
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Homogeneous Catalysis
Enzymes (), which are biological catalysts, are very selective

and can have a dramatic effect on the reactions they control.
- H2O2 decomposition with enzyme catalyst, Ea = 8 KJmol-1 ;
acceleration of the reaction by a factor of 1015 at 298K.
A homogeneous catalyst() is a catalyst in the same
phase as the reaction mixture.
- H2O2 decomposition by Br- or catalase
A heterogeneous catalyst () is a catalyst in a
different phase from the reaction mixture.
- The hydrogenation of ethene to ethane, a gas phase reaction, a
solid catalyst (Pd, Pt, Ni)
- The metal provides a surface upon which the reactants bind; this
binding facilitates encounters between reactants and increasing the
2
rate of the reaction.
11.12 Acid and Base Catalysis

In acid catalysis the crucial step is the transfer of a proton to the
substrate.
X + HA HX+ + AHX+ products
- Keto-enol toutomerism
H+
CH3COCH2CH3 CH3C(OH)=CHCH3
In base catalysis a proton is transferred from the substrate to a base.
HX + B X- + HB+
X- products
- The hydrolysis of esters
OH-
CH3COOCH2CH3 + H2O CH3COOH (as CH3CO2-)

+ CH3CH2OH
11.13 Enzymes
The Michaelis-Menten mechanism
- The action of enzyme in an aqueous environment.
(1 )
E + S ES
Rate of formation of ES = ka[E][S]
(2 )
ES E + S
Rate of decomposition of ES = ka[ES]
(3)
ES P + E
Rate of formation of P = kb[ES]

Rate of consumption of ES = kb[ES]
Rate of formation of P = kb[ES]
- Net rate of formation of ES

ka[E][S] - ka[ES] - kb[ES] = 0
ka[E][S] (ka + kb) [ES] = 0
4
11.13 Enzymes
[E] : the molar concentration of the free enzyme

[S] : the molar concentration of the substrate
[E]0 : the total concentration of the enzyme
[E] + [ES] = [E]0
11.13 Enzymes
ka[ES] + kb[ES] = ka[E]0[S] - ka[ES][S]

(ka + kb + ka[S]) [ES] = ka[E]0[S]
(KM + [S]) [ES] = [E]0 [S]
11.13 Enzymes
- The Michaelis-Menten rate law

Rate of formation of P = kb[ES] = kb [E]0[S]/([S]+ KM)
- The Michaelis constant, KM
- [E]0 is the total concentration of enzyme (both bound and

unbound).
11.13 Enzymes
The rate of enzymolysis is first-order in the added enzyme

concentration, but the effective rate constant kr depends on the
concentration of substrate [S].
- When [S] << KM, , kr =kb[S]/KM, the rate constant increases
linearly with [S] at low concentration.
Rate of formation of P = kb[E]0[S]/KM
- When [S] >> KM, , kr ~ kb , Rate of formation of P = kr[E]0 = kb[E]0.
8
11.13 Enzymes
When [S] >> KM, , the rate is independent of the concentration of S

because there is so much substance present that it remains an
effectively the same concentration even though products are being
formed.
- The rate of formation of product is a maximum, and kb[E]0, is
called the maximum velocity, max, of the enzymolysis.
max = kb[E]0
- The rate-determining step is ES P + E, because there is ample
ES present, and the rate is determined by the rate at which ES
reacts to form the products.
11.13 Enzymes
The reaction rate at a general substrate composition is related to

the maximum velocity, max = kb[E]0
- The graph gives a clue to the

significance of KM, the rate of
enzymolysis reaches 1/2 max
when [S] = KM ; broadly
speaking, KM is a measure of
the substrate concentration at
an above which the enzyme is
effective.
10
11.13 Enzymes
A Lineweaver-Burk plot is a plot of 1/ against 1/[S].
Slope = KM/max
11
11.13 Enzymes
- 1/ vs. 1/[S] -- a straight line

- The slope of the straight line : KM/max.
- The extrapolated intercept at 1/[S] = 0 : 1/max.
- The intercept can be used to find max, and the value combined
with the slope to find the value of KM.
- The extrapolated intercept with the horizontal axis (where 1/ = 0)
occurs at 1/[S] = -1/KM.
12
11.13 Enzymes
The turnover frequency, or catalytic constant, of an enzyme, kcat , is

the number of catalytic cycles (turnovers) performed by the active
site in a given interval divided by the duration of the interval.
- The time constant for the first-order decomposition of ES is 1/kb.

- The number of catalytic events in an interval t is
t /(1/kb) = kb t
- The frequency of such event is this number divided by the interval
t , which is kb itself.
kcat = kb
13
11.13 Enzymes
- An alternative interpretation of kcat is a measure of the

effectiveness of an active site, as it is the maximum rate of
enzymolysis that can be achieved divided by the concentrations of
active sites.
14
11.13 Enzymes
The catalytic efficiency, , of an enzyme is the ratio.
- kcat is a number of the effectiveness of an enzyme and KM is a

measure of the concentration at which the enzyme becomes
effective.
- The higher the value of , the more efficient is the enzyme.
- We can think of the catalytic efficiency as the effective rate
constant of the enzymatic reaction.
KM = (ka + kb)/ka
15
11.13 Enzymes
- The efficiency reaches its maximum value of ka when kb >> ka.

- Because ka is the rate constant for the formation of a complex
from two species that are diffusing freely in solution, the
maximum efficiency is related to the maximum rate of diffusion of
E and S in solution.
- In this limit, rate constants are about 108 ~ 109 dm3mol-1 s-1 for
molecules as large as enzyme at room temperature.
- The enzyme catalase has = 4.0x108 dm3mol-1s-1 and as said to
have attained catalytic perfection.
- The rate of the reaction it catalyzes is controlled only by diffusion :
it acts as soon as a substrate makes contact.
16
11.13 Enzymes
17
11.13 Enzymes
18
11.13 Enzymes
(Self-test 11.6)
19
11.13 Enzymes
Slope = 40.0
= KM/max
Intercept = 4.0
= 1/max
20
11.13 Enzymes
The action of an enzyme may be partially suppressed by the present

of a foreign substance, which is called an inhibitor.
- An inhibitor may be a poison that has been administered to the
organism, or it may be a substance that is naturally present in a
cell and involved in its regulatory mechanism.
In competitive inhibition, the inhibitor competes for the active site
and reduces the ability of enzyme to bind the substance.
21
11.13 Enzymes
In non-competitive inhibition, the inhibitor attaches to another part

of the enzyme molecule, thereby distorting it and reducing its ability
to bind the substrate.
22
Chain Reactions
()
In chain reaction, an intermediate produced in one step generates
a reactive intermediate in a subsequent step, then that intermediate
generates another reactive intermediate and so on.
23
11.14 The Structure of Chain Reactions

The intermediates responsible for the propagation of a chain
reaction are called chain carriers.
- radicals, ions, neutrons
- Radicals are marked with a dot to signify the unpaired electron.
A radical chain reaction typically involves some but not necessarily
all of the following steps.
- Initiation, in which radicals are formed from non-radical
molecules.
- Propagation, in which a radical attacks a molecule and forms a
new radical.
- Branching, in which the attack by a radical produces two radicals.
24
- Retardation, in which a product molecule is destroyed by a radical.

- Inhibition, in which radicals are removed other than by
termination; perhaps by reaction with the walls of the reaction
vessel or an added agent.
- Termination, in which two radicals combine to form a molecule
and so end the chain.
25
(Self-test 11.7)
26
Initiation :
CH3CH3 2 CH3
Propagation : CH3 + CH3CH3 CH4 + CH2CH3

Termination : CH2CH3 + CH2CH3 CH3CH2CH2CH3
Inhibition : CH2CH3 to react with the wall of the reaction vessel.
Retardation : CH3CH2CH2CH3 + CH2CH3 CH2CH2CH2CH3
+ CH3CH3
27
The NO molecule has an unpaired electron and is a very efficient

chain inhibitor.
- The observation that a gas-phase reaction is quenched when NO is
introduced is a good indication that a radical chain mechanism is
in operation.
28
11.15 The Rate Laws of Chain Reactions

The thermal reaction of H2 with Br2.
- The overall reaction and the observed rate law
H2 (g) + Br2 (g) 2 HBr
- The complexity of the rate law suggests that a complicated

mechanism is involved.
29
- The radical chain mechanism

Initiation :
ka
Br2 Br + Br
Rate of consumption of Br2 = ka[Br2]
k
= kb[Br][H2]
kc
H + Br2 HBr + Br
= kc[H][Br2]
kd
= kd[H][HBr]
b
Propagation : Br + H2
HBr + H
Retardation :
H + HBr H2 + Br
ke
Termination : Br + Br + M Br2 + M = ke[Br]2
30
- The third body, M, a molecule of an inert gas removes the

energy of recombination.
- The constant concentration of M has been absorbed into the rate
constant ke .
- Other possible termination steps include the recombination of H
atoms to form H2 and the combination of H and Br atoms; however,
it turns out that only Br atom recombination is important.
31
The rate law of a chain reaction

- The experimental rate law is expressed in terms of the rate of
formation of products, HBr.
Net rate of formation of HBr
= kb[Br][H2] + kc[H][Br2] kd[H][HBr]
(1)
- Set up the expressions for the net rates of formation of [H] and [Br]
and apply the steady-state assumption to both.
Net rate of formation of H
= kb[Br][H2] - kc[H][Br2] kd[H][HBr] = 0
(2)
Net rate of formation of Br

= 2ka[Br2] - kb[Br][H2] + kc[H][Br2] + kd[H][HBr] 2ke[Br]2 = 0
32
(3)
(2) + (3)
(4)
1/2
(4) (2)
(5)
(1) (2) and (5)
33
e
34
- The proposed mechanism is at least consistent with the observed

rate law.
- Additional support for the mechanism would come from the
detection of the proposed intermediate (by spectroscopy), and the
measurement of individual rate constants for the elementary steps
and confirming that they correctly reproduced the observed
composite rate constants.
35
Road map of key equations
36
Homework
(Chapter 11)
11.2
11.12 11.26
11.4
11.20 11.27
11.5
11.21 11.29
11.8
11.23 11.30
11.9
11.24 11.31
37

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Homogeneous Catalysis

A catalyst(, ) is a substance that accelerates a reaction

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Enzymes (), which are biological catalysts, are very selective

11.12 Acid and Base Catalysis

CH3COOCH2CH3 + H2O CH3COOH (as CH3CO2-)

Rate of formation of ES = ka[E][S]

Rate of decomposition of ES = ka[ES]

Rate of formation of P = kb[ES]

Rate of formation of P = kb[ES]

- Net rate of formation of ES

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[E] : the molar concentration of the free enzyme

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ka[ES] + kb[ES] = ka[E]0[S] - ka[ES][S]

(KM + [S]) [ES] = [E]0 [S]

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- The Michaelis-Menten rate law

- The Michaelis constant, KM

- [E]0 is the total concentration of enzyme (both bound and

The rate of enzymolysis is first-order in the added enzyme

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When [S] >> KM, , the rate is independent of the concentration of S

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The reaction rate at a general substrate composition is related to

- The graph gives a clue to the

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A Lineweaver-Burk plot is a plot of 1/ against 1/[S].

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- 1/ vs. 1/[S] -- a straight line

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The turnover frequency, or catalytic constant, of an enzyme, kcat , is

- The time constant for the first-order decomposition of ES is 1/kb.

- An alternative interpretation of kcat is a measure of the

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The catalytic efficiency, , of an enzyme is the ratio.

- kcat is a number of the effectiveness of an enzyme and KM is a

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- The efficiency reaches its maximum value of ka when kb >> ka.

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The action of an enzyme may be partially suppressed by the present

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In non-competitive inhibition, the inhibitor attaches to another part

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11.14 The Structure of Chain Reactions

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11.14 The Structure of Chain Reactions

- Retardation, in which a product molecule is destroyed by a radical.

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11.14 The Structure of Chain Reactions

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11.14 The Structure of Chain Reactions

Propagation : CH3 + CH3CH3 CH4 + CH2CH3

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11.14 The Structure of Chain Reactions

The NO molecule has an unpaired electron and is a very efficient

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11.15 The Rate Laws of Chain Reactions

- The complexity of the rate law suggests that a complicated