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(iii)
(iv)
2-
(ii)
(1)
A physiological deficiency appears when the
element is removed from the diet
-1
-1
Specificity
Active site provides specificity for its particular substrate
(2)
(3)
(4)
Active sites of
Enzymes
Cys(S)
Zn
His(N)
OH
Zn
OH2 Cys(S)
Glu(O)
His(N)
His(N)
Carboxy
peptidase
His(N)
Zn OH
His (N)
H O + CO
2
His(N)
Carboxy
anhydrase
CH CH OH
peptide
hydrolysis
(removes
terminal
amino acids
from
proteins)
NAD+
NADH
H2CO3
+ HCO
3-
H3
C
H
O
Porphyrins
Porphyrins are tetrapyrrole macrocycles with conjugated double
bonds and various groups attached to the perimeter
R
N
R
R
NH
HN
R
Variation of substituents facilitates the tuning of electrondonating and electron-withdrawing ability of the ligand
The porphyrins can accept two hydrogen ions to form+2 diacids or donate
two protons to form -2 dianions
Function
Fe-porphyrin
Cytochrome
electron transfer
Fe-porphyrin
Hemoglobin
Myoglobin
dioxygen carrier
Mg-porphyrin
Chlorophyll
photosynthesis
Cytochromes
Cytochromes are electron transfer proteins
There are three types of cytochromes depending upon the porphyrin types
s-cys protein
s-cys protein
HO
HO
N
Fe
Fe
Fe
N
O
H
HO
OH
O
OH
HO
O
HO
OH
O
O2
th
III
p
ar
a
m
a
g
n
et
ic
4
t 2g
2
eg
w
S
p
i
n
d
t
2
g
6
e
g
0
The size of Fe
2+
2+
Cooperativit
y
W
h
e
n
O
2
b
i
n
d
s
t
o
o
n
e
s
u
b
u
n
i
t
trigg
ers
confor
mation
al
change
s in the
globin
chain
t
r
a
n
s
l
a
t
e
d
t
h
r
o
u
g
h
H
b
o
n
d
n
e
t
w
o
r
k
Fe
2+
moves
co
nt
ra
ct
s,
m
ov
es
in
to
pl
an
e
of
po
rp
hy
ri
n
ri
ng
the
histidin
e
attache
d to it
En
ha
nce
s
the
abi
lity
of
oth
er
thr
ee
uni
ts
to
bind
O2
This
phenomenon is
called
cooperative
effect
In a similar way
when the blood
reaches the muscle,
only one O2 is
released, the others
are released even
more easily due to
the cooperative effect
in reverse