Chap.

7 Nonelementary Reaction Kinetics

& Bioreactions

1
 Nonelementary Reaction
to Iona stoj
Pseudo steady-state hypothesis (PSSH) is applied for the nonelementary reaction
rate constant
rA = g
kC nA

Example: Decomposition of acetaldehyde

CH 3 CHO CH 4 + CO

rCH 3CHO = kC CH 3CHO

3/2
Nonelementary reaction*
{ ateconstant
*Based on experimental data

2
Example: Production of hydrogen iodine from hydrogen and iodine

H 2 + I 2 2 HI
oeisrioo 3 oYwaow

ii
k 1k 3 C I 2 C H 2
rHI = Nonelementary reaction*
k 2 + k 3C H 2

MNJN 02 09

*Based on experimental data

3
Example: Decomposition of azomethane (AZO) to ethane and nitrogen
p overall rxn

(CH 3 ) 2 N 2 C2 H 6 + N 2 Gas phase

Case I P > 1 atm; rN 2 C AZO

*Based on experimental data

Case II P < 50 mmHg; rN2 C 2 AZO

-

Reaction occurs via each step.

Why ? An intermediate (*) is generated.
targeted
4
 Chain reaction & Intermediate
For decomposition of AZO

Step 1 k1
(CH 3 ) 2 N 2 + (CH 3 ) 2 N 2 (CH 3 ) 2 N 2 + [(CH 3 ) 2 N 2 ]* (1)

step bought rAZO*

elementary = k 1C 2 AZO Elementary Reaction
reaction
k2
Step 2 [(CH 3 ) 2 N 2 ] + (CH 3 ) 2 N 2 (CH 3 ) 2 N 2 + (CH 3 ) 2 N 2
*
(2)
now
p
rAZO* = k 2 C AZO C AZO* Elementary Reaction
decomposition
Step 3 k3
[(CH 3 ) 2 N 2 ] C 2 H 6 + N 2
*
(3)
Ydoio
overall Ag rAZO* = k 3 C AZO*
deteatoiogodsius
) on

go
Elementary Reaction rotators
non elementary reactionrN = k 3 C AZO* 2
Overall Rate
formation of Nz
* Intermediate [each step is elementary reaction based on the formation (+) or disappearance (-) of intermediate]
5
 n
r j = r ji
i =1

net rate rate of rate of rate of

of formation formation formation
= + +
formation of AZO * in of AZO * in of AZO * in
of AZO * (1) (2) (3)

rAZO* = rAZO* (1) + rAZO* (2) + rAZO* (3)

formed( + ) decomposed( ) decomposed( )

rAZO* = k 1C 2 AZO k 2 C AZO C AZO* k 3 C AZO*

6
 Pseudo Steady-State Hypothesis (PSSH)
n
rj = rji = 0, PSSH
i =1

rN 2 = k 3 C AZO* net rates

q
rAZO* = k 1C 2
AZO . k 2 C AZO C AZO* k 3 C AZO* = 0 (PSSH)

k1C 2 AZO k 2 C AZOC AZO* k 3C AZO* = 0

C AZO* (k 2 C AZO + k 3 ) = k1C 2 AZO

7
 Pseudo Steady-State Hypothesis (PSSH)

k 1C 2 AZO
C AZO* =
k 3 + k 2 C AZO

rN 2 = k 3 C AZO*
Substitute for CAZO*
2
k 1 k 3 C AZO
rN 2 =
k 3 + k 2 C AZO

8
 k 1 k 3 C 2 AZO
rN 2 =
k 3 + k 2 C AZO

At low CAZO , k2CAZO << k3 rN 2 = k 1C 2 AZO

At high CAZO , k2CAZO >> k3 k 1k 3

rN 2 = C AZO = kC AZO
k2

9
 PSSH Rule

I. Intermediate (*) is formed by activation . It

can be free radical, cation, and anion
intermediate.
p step doo
II. Each step involving the formation (+) or
decomposition (-) is elementary reaction.
III. Net rate of intermediate formation = 0
n
rj = rji = 0, PSSH
i =1

10
 Searching for a mechanism
milk rate 's
so
q
k 1C 2 AZO Numerator
If rate law is given; rN 2 =
1 + k ' C AZO Denominator
d
ng fun rate oo
In the real world, a rate law is first obtained by experimental data (i.e. collection of
batch data in Chap. 5). Then, the mechanism is proposed. The rule of thumb (Table
7-1) can be applied.
rate winter
q newly on intermediate
,
1) The appearance of CAZO in the numerator suggesting that AZO* is formed by
miles rate
collision of AZO (step 1) ran

intermediate
\ s
onion

2) AZO* collides with AZO resulting CAZO in the denominator. (step 2).
3) AZO* decomposes spontaneously (step 3) resulting a constant (k) in the
denominator. derive nsrtd check

Species generate intermediate being placed in the numerator

Species destroy intermediate being placed in the denominator.
11
 Rule of thumb for development of a mechanism (Table 1: p. 383)

1. Species having concentration (s) appearing in the denominator,

probably collide with the active intermediate;

A + A* Disappearance of A*

2. If a constant (k) appears in the denominator, the spontaneous

decomposition of active intermediate will occur;

A* Product

3 . Species having concentration (s) appearing in the numerator,

probably produce the active intermediate.

A A* +

12
 Steps to deduce a rate law (Table 7-2: p. 384)

1. Assume an active intermediate (s).

2. Postulate a mechanism, utilizing the rate law obtained from experimental
data.
3. Model each reaction as an elementary reaction.
4. After write raw law for the desired product (in terms of intermediate). Then,
write the rate laws for each of intermediates.
5. Use PSSH.
6. Eliminate concentration of intermediates using steps 4 & 5.
7. If the derived rate law does not agree with the experimental observation ,
assume a new mechanism and/or intermediates and go to step 3. (Trial and
error).

13
Example 7-1 The Stern-Volmer Equation

Example 7-2 PSSH Applied to Thermal Cracking of Ethane

 Reaction pathway ethane cracking
a

3,2889
fox k2
C2H6 k1 2CH3o0 CH4 + C2H5o
C2H6
k3
Ho k4
C2H4 + Ho
C2H5o + H2

C2H5o k5
o
r3C 2 H 4 = k 3 [C 2 H 5 ]
C4H10

15
 Enzymatic Reaction Fundamental

Enzyme (E) is a high MW protein,

used to transform a substrate (S)
into a product (P) without being a
part of product at all (without being
consumed).

The reaction pathway proceeds to

an active intermediate complex
(E.S).

Enzyme chymotrypsin containing

various amino acids
16
 Enzymatic Reaction

rail E + S E.S
.
k1

E = Urease
k2
S = Urea
6
E.S E + S
k3
W = Water
E.S + W P + E E.S = Enzyme-substrate
complex (Intermediate)
P = 2NH 3 + CO 2 P = Product
elementary
s
non

PSSH rs = k 1 (E)(S) k 2 (E.S) Overall Reaction

(
net rates ) unfnow 7
rE.S = k 1 (E)(S) k 2 (E.S) k 3 (W)(E.S)

17
Reaction Mechanism p
Armoires

(E t ) = (E) + (E.S) Et = Total enzyme concentration

one :
enzyme
mifrnfd
(E) = (E t ) (E.S)

rE.S = 0 = k 1 [(E t ) (E.S)](S) k 2 (E.S) k 3 (E.S)(W) PSSH

k1(E t )(S)
(E.S) =
k 1 (S) + k 2 + k 3 (W)

18
 rS = rP

k1(E t )(S)
rS = k 3 (W)(E.S) = rP (E.S) =
k 1 (S) + k 2 + k 3 (W)

Substitute for (E.S); rS =

8
k 1 k 3 (W)(E t )(S)
k 1 (S) + k 2 + k 3 (W)

19
Michaelis-Menten Equation

'
k 3 = k 3 (W)

: KM =
k 3 '+ k 2
k1
Km= Michaelis Constant

k 3 ' (S)(E t )
rS =
(S) + K M Fenzy mean Vmax
snafu
3 Vmax = k 3 ' (E t ) Vmax = Maximum rate at any Et
Cs
0
Vmax (S)
Then, rS =
K M + (S)
main conc
20
 A plot of rate VS urea concentration

Vmax = f(Et)
KM f(Et)
Vmax

Saad
Body
-rS
Vmax/2

KM
CS
21
 Vmax (S)
rS = Michaelis-Menten Equation
K M + (S)

Vmax (S)
At low (S); rS
KM

At high (S); (S) >> K M and rS Vmax

22
 ?!:dm
Vmax
rS = At (S1/2)
2

Vmax V (S )
Substitute for rS ; = max 1/2
2 K M + (S1/2 )

Then ; K M = (S1/2 )

KM is the substrate concentration that gives the rate = Vmax/2

23
Batch data for enzymatic reaction;
dN A
Fin Fout + rA V =
dt
dN A
rA V =
dt
dN urea
= rurea V
dt
For liquid (constant V)
dC urea
= rurea
dt integrate
M
The rate law for urea decomposition is :
V C
rurea = max urea , combine and integrate for t
K M + C urea

24
 dC urea
= rurea
dt
1
dt = dC urea
rurea
t C urea C urea0
1 1
dt =
o

C urea0
rurea
dC urea =
C urea
- rurea
dC urea

C urea0 C urea0 C
K M + C urea KM urea0
C urea
t=
C urea
Vmax C urea
dC urea =
C urea
Vmax C urea
dC urea +
Vmax C urea
dC urea
C urea

KM C urea0 C urea0 C urea

t= ln +
Vmax C urea Vmax
For conversion,
C urea = C urea0 (1 X)

25
Curea = Curea0 (1-X)
Bath system only
KM 1 C urea0 X Word
t= ln +
Vmax 1 X Vmax cstn
,
...
.

i
integrates aed

1 1 Vmax C urea0 X
ln =
t 1 X KM
conversion
On .*ap
KMt
=sgs

1 S0 Vmax S0 S
.

ln =
t S KM KMt
Where; S0 = initial concentration of substrate
S = concentration of substrate at time (t)

26
 A plot of substrate concentration VS time

Intercept = Vmax/KM
1 S0 Vmax S0 S
ln =
t S KM KMt
(1/t) ln(S0/S)
Slope = -1/KM

(S0-S)/t

27
Example 7-3 Evaluation of Michaelis-Menten Parameters Vmax and KM

Example 7-4 Batch Enzymatic Reactors

 Inhibition of Enzyme Reaction

Inhibitors are species that interact with enzymes and

render the enzyme ineffective to catalyze its specific
reaction.

There are 3 types of reversible inhibition for

inhibitors; (i) competitive, (ii) uncompetitive and (iii)

noncompetitive.
FD now 1,2

29
 (I) Competitive Inhibition

I competes with S to form E I (inactive)

Reaction step Competitive inhibition pathway
k1
(1) E + S E S E + S E S E + P
k2
(2) E S E + S +
antireform aroeobdoiooidaspndd
I inhibitor

k3
,
(3) E S P + E

(4) I + E E0 I (inactive) 'atf

Is I
k4
KI
k5 unknow EI
(5) E I E + I

30
 (I) Competitive Inhibition
intermediate net rate

y
rp = k 3 (E S) (7 34)
Unknow

@ k 2 (E S) k 3 (E S) (7 35)
rES = 0 = k1 (E)(S)

/ dado broom
rEI = 0 = k 4 (E)(I) k 5 (E I) (7 36)
Et = E + (E S) + (E#

I) (7 37)
,

oonnrnaoos

combining equation (7 35), (7 36), and (7 37), then solving

for (E S), and substituting for (7 34)
Vmax (S)
rp = rs = Rate law for competitive

a
(I) inhibitor
(S) + K M 1 +
KI
smooth
ompetitie km 31
 (I) Competitive Inhibition
HB

@
Vmax = k 3 E t and K M =
k2 + k3
k1
K I is inhibition constant (mol/dm3 )
k5
KI =
k4
letting K ' M = K M (1 + I/K I )
Effect of competitive inhibitor is to increase the apparent Michaelis constant, KM is that
a larger (S) is needed for rs, to reach half its maximum rate (KM)

1 1 KM (I) 1 Rearrange to obtain a Lineweaver-

= + 1+
- rs Vmax Vmax KI (S) Burk plot (eq. 7-39 p. 411 is wrong.)
New slope

wfagguboenoaw
Vmax unchanged, KM changed
32
(I) Competitive Inhibition

a
sand
aioeag
ng
:
-

D) Morna @ 03

33
 (II) Uncompetitive Inhibition
I ties up with ES to form IES (inactive)
Reaction step Uncompetitive inhibition pathway
k1

!
(1) E + S E S E + S E S E + P
k2 +
(2) E S E + S tone E. S
I

k3
(3) E S P + E ES KI
k4
inactive form )
(4) I + E S I E S (inactive)
(
I E S
k5
(5) I E S I + E S

34
 (II) Uncompetitive Inhibition
Find ES using PSSH

Vmax (S) k5
rp = rs = , where KI = Rate law for uncompetitive
(I) k4 inhibitor
K M + (S) 1 +
KI

Rearranging;
pkmtaidogiog
Rearrange to obtain a Lineweaver-
+ OM
1 1 (I) K 1
= 1+ Burk plot
- rs Vmax KI Vmax (S)
New intercept

Vmax changed, KM unchanged

35
 (II) Uncompetitive Inhibition

Slope (KM/Vmax) remains the same as (I) increases, while

intercept increases (-rs decreases).
36
 (III) Noncompetitive Inhibition (Mixed Inhibition)

Reaction step Mixed inhibition

(1) E + S E S gcsmpetitne
(2) E + I E I (inactive)
s uncompetitive
(3) I + E S I E S(inactive)
(4) S + I E I E S(inactive)

*
(5) E S P + E
ooroiwvuadn roars :D !
product

37
.
 (III) Noncompetitive Inhibition (Mixed Inhibition)

PSSH

Vmax (S) k5
rp = rs = , where KI = Rate law for noncompetitive
k4
[((S) + K M )] 1 + (I)
inhibitor
KI

Rearranging;

1 1 (I) KM (I) 1 Rearrange to obtain a

= 1+ + 1+
- rs Vmax KI Vmax K I (S) Lineweaver-Burk plot

Vmax changed, KM changed

38
(III) Noncompetitive Inhibition (Mixed
Inhibition)

Both slope and intercept increase

with increasing inhibitor
concentration.

39
Summary of types of inhibitor

40
 Summary of inhibitor effect
(I)
1+ Inhibitor term
KI

1 1 K 1
= + M
fads
Michaelis-Menten equation
- rs Vmax Vmax (S) (inverse) without inhibitor
)NoN8V
1 1 KM (I) 1
= + 1+
- rs Vmax Vmax KI (S) Competitive inhibitor
New slope

1 1 (I) KM 1
= 1+ +
- rs Vmax KI Vmax (S) Uncompetitive inhibitor
New intercept

1 1 (I) K (I) 1
= 1+ + M 1+ Noncompetitive inhibitor
- rs Vmax KI Vmax K I (S)

41