CYLIIO II Semester 2007 - 2008

MINORExamII
Date: Mar. 18, 2008 Time: 1 hour

1. The figure below summarizes the rate data for the oxidation of D-gluc:m;cby V O2+ .
12 !
i 15 r ' "'---"-' .--

C 101 j
12 12
8
-$. 9 ~ 81 9
//1
~ 61 "
-
A
~
",,' 6 "" 6.

/J
C. "§? 4
3 3
21
0 ' ""'-
0 . 0
0 30 60 90 120 0 2 3 4 5 0 2 3 4 5
10' (o-glucose] r (mol dm ') [HSOd (mol dm .-3) [W] (mol dm .3)
(a) Fig. Ia (b) Fig. Ib (c) Fig. Ie

(i) From the figure, what can you conclude about the rate law? Explain your reasoning. In Fig. 1a you
only need to consider one of the four curves labelled A, B, C, or D. [5]
(ii) With a justification decide whether the mechanism given below explains the rate law that you deduced
in part (i) of the question. [10]
- OH +

K HO OH
~
VO ++ H 0++ HSO ----1 1
"""""v/
I
'

2 3 4- <>H
~
- cf'A
"fS
0 J +

M
~
CH~H ~ CH~H
+A ==
~ l
.

H H OH .

OH f He-..! V /OH
HO""""-- "--OSO20H ~
Intermediate complex

CH2OH
~
Intermediate complex slow
- c::!:(.°+ VO'>+21<,0+H50.-
OH
Free. radical

fast
Free radical + V(V) r-X-rH
~O 0
+V(IV)+",
(iii) What is the predicted order with respect to the oxidant for this mechanism? 15]

(iv) With this mechanism illustrate the ideas of order and molecularity. [5]
I
::. 2. In a recent significant development, scientists have desi~ed and synthesized enzymes which catalyze tll('
I. retro-aldol reaction. The figure below gives the relevant-rate data for these synthetic enzymes.

(i) From the figure, estimate the approximate turnover number (k2) for the most efficient synthetic
enzyme. The enzyme concentration is 13.8 x 10-6 M. [5]

J
 --
(ii) Outline how one obtains the Michaelis constant from data such as this, [10]
(iii) H0Wwould you convert these graphs into a linear form and obtain the relevant rM(' parallletf'rs'l [1Oj
1410'S
B

12 10.5
--[)
RA22
RA34
I'>

---+--- RA45
,#im... lV'..;.(;

---b.- RA61 I'>

10 10-5
-.......
in
;:::: 81O-s
\U
E
>.
N
c: -
~
.....
610'"
>
410.5

2 1O,s.l.

0
0 0,0001 0,0002 0,0003 0.0004 00005 0.0006
Substrate concentration (M)

3. (i) The figure below shows the variation of the rate constant with temperature for the reaction of 0 H
with N2O. Explain its appearance and discuss the significance. [15]

10 ::J
~~.~
ID
.. (bl~=~~C.
:SB
::!
j

§
...
"0
.,..
.....
c
1
2 3 4 5
1000 KI T
(ii) Sketch the fraction present of each species versus the time elapsed for the following two cases: (a)
A in equilibrium with Band C simultaneously with first-order rate constants k1, L 1 and k2, L2,
respectively, and k1 = 1 X 10-2, k-l = 1 X 10-4, k2 = 1 X 10-3, and k-2 = 1 X 10-6 (with
appropriate units), (b) A decaying to Band B decaying to C with first-order rate constants of k1
and k2, respectively, and k2/k1 = 20 ([AJo =I0, [BJo = 0, and [GJo = 0), [5+5]
4. (i) Derive an expression for the relaxation time in terms of kj, k-l' and [Ah,eq (i.e.. [A]eq
- after the
.~.-----
temperature-jump) for the reaction described by
2A~D.
k-l

Assume the forward and reverse reactions to be second and first order, respectively, [15]
(ii) The first step in the assembly of the protein yeast phosphoglycerate mutase is a reversible dimerization
~ of a polypeptide according to the equilibrium mentioned above where A is the polypeptide and D is
the dimer. Suppose that a 1.43 x 10-5 mol dm=-3 solution of A is prepared and is allowed to COIn('
/' to equilibrium at 280 K. Once equilibrium is ac~ieved, the temperature of the solution is jumped to /'
293 K. The rate constants k1 and k-l for the dimerization reaction at 293 K are 6.25 x 103 dm3
mol-l S-1 and 6.00 x 10-3 S-I, respectively.l::alculate the value of the relaxation time observed in
the experiment. [10]