structure of [ co(edta) ] -
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Structure of [Co(EDTA)]-
Co
N N
O O
CH2 CH2
CH2
C
H2C
C
O
O
CH2O
O
H2CO
O
Q. 1.
O
O
O
OO
O
N
O O
N
O O
O O
O
O
CH2 CH2 O
CH2 CH2 O4
4
N
O O
N
O O
O OM
n+
+ M
n+
Macrocyclic ligands
Q. 4.
[18]crown-6
dibenzo[30]crown-10
cryptand[2.2.2.] cryptate (complex)
O
CH3 O
CH3
H3C
O
CH3
O
CH3
O CH3
O
H3C
O
CH3
O O
O O
K
The nonactin-potassium complex
Q. 4.
The valinomycin-potassium complex
Q. 4.
H D-Val
L
L-Val
H
D-Val
LL-Val
H
D-Val
L
L-Val
O
O
O
O
O
OK+
Mg
NH3C
CHCH2
N
R
CH2 CH3
CH3
N
OH3COOC
N
H3C
O
O
Q. 6.
Chlorophyl
without Mg: porphyrin
skeleton
methyne group
pyrrole ring
vinyl group
ester bond phytol
Q. 6.
O
P
OO
OOP
O
O
O
OH OH
OO
O
R R
M2+
OH
M2+ M2+
O
R
The mechanism of the phosphate hydrolysis
Q. 8.
Outlined structure of apoferritin
Iron(II)-protoporfirin IX-complex (HEME)
N
NHC
N
CH
NHC CH
H3C CH
CH2
CH3
CH
CH2
CH3H2C
H2C
H2C
CH2
OOC
COO
H3C
Fe
Q. 9.
Q. 9.
myoglobin hemoglobin
Catalytic cycle of P-450 enzymes
Q. 10.S
Fe
H2O
III
S
FeIII
RH
RH
Fe
S
II
S
Fe
O
ORH
III
S
Fe
O
ORH
III
S
Fe
O
R H
IV
RHH2O
e-
3O2e-
H2O
2 H+
H2OROH
+ AO
+ A
Zink(II) in the active centre of carboxipeptidase-A
Q. 11.
O
Zn
O
NHN N
NH
CH2
H2C
CNC
HH H
C
O
H2C
CH2
His-69
Glu-72
His-196
O Zn
S
S
N
C
CH3
H
H
(Cys)
(His)
(Cys)
The active centre of the alcohol dehydrogenase
Q. 11.
Coordination environment of the copper centre in azurin
Q. 12.
Path of electrons through cytocrhome c oxidase
Q. 12.
Cyt c(Fe2+)
Cyt c(Fe3+)
CuA
CuB
Cyt a
Cyt a3
O2 + 4H+
H2O
H+
Matrix
Intermembranespace
Cu
His
His O
L
HisO
Cu
His
His
His
Cu
His
His
His
Cu
His
His
His
I I II II
+ 3O2
- 3O2
deoxyhemocyanin oxyhemocyanin
Reversible oxygenation of hemocyanin
Q. 13.
Structure of dimetal centre in Cu-Zn superoxide dismutase
Q. 13.
Fe S
S Fe
SFe
S Fe
S Fe
Fe S
FeS
Fe SS
S
S
MoS
Supposed structure of Fe-S-Mo cofactor of nitrogenase
Q. 14.
3 NADH + 3H+
3 NAD+
3 Ferredoxin(oxidized)
3 Ferredoxin(reduced)
Fe protein(reduced)
Fe protein(oxidized)
Fe protein(oxidized)
Fe protein(reduced)
12 ATP
12 ATP
12 ADP + 12 Pi
Fe-Mo protein(oxidized)
Fe-Mo protein(reduced)
Fe-Mo protein(oxidized)
N2
2 NH3
6 H+
12 ATPN2
Q. 14.
The supposed reaction mechanism of dinitrogenase
Q. 14.
The reaction mechanism of dinitrogenase
Fe
S
Mo(V)
HN NH
Fe
S
Mo(V)
H2N NH2
Fe
S
Mo(V)
NH3 NH3
Fe
S
Mo(V)
OH
Fe
S
Mo(V)
P
Fe
S
Mo(III)
Fe
S
Mo(III)
:N N:
:N N:
+ 2H+ + 2e-
+ 2H+ + 2e-
2 NH4+
+ 2H+
- ADP
+ 2e-
- Pi
+ 2H+
N2 + 8 H+ + 6 e- 2 NH4+
Coordination environment of the Cr3+ centre in the glucose tolerance factor
Q. 15.
N
Cr
N
L
L L
L
COOH
HOOC
Cross-linking between collagen chains in lung tissue
Q. 19.
(CH2)2
CH2
CH2
NH2
CH2
HC
(CH2)2
OH
NH2
(CH2)2
CH2
CH2
NH2
CH
HC
(CH2)2
OH
O
(CH2)2
CH2
CH2
N
CH
HC
(CH2)2
OH
(CH2)2
CH2
CH2
NH
CH2
C
(CH2)2
O
Hydroxylysine Hydroxyallysine Schiff’s base Stable cross-link
Hypothetical model of silification
Q. 20.
The catalytic cycle of GSH peroxidase
Q. 21.
E – Se- E – SeOH
E – Se – S – G
ROOH, H+ ROH
G – SH
H2OG – SH
H+, G – S – S – G
O. 22.
Thyroid hormones
O CH2 C
H
NH3+
COO-HO
I I
I
O CH2 C
H
NH3+
COO-HO
I I
II
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