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Haemoglobin
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haemoglobinHAEMOGLOBIN
9. what is
haemoglobin ?
oxygen carrying protein
•
It is the main -
in the human
body .
•
Found in RBC 's .
Binds in it
oxygen lungs and releases in tissues
•
.
Binds coz release in
in tissues
for lungs
• .
•
Tetrameric protein with 2 identical
.
a -
subunits and 2 identical B subunits .
structure has an
P configuration
◦
✗ .
, ,
Each subunit contains
globin a naan
•
1 theme ) which binds 0214 Oz in total)
group
The Maan
cofactor is
Tetrapyrrale ring
a
•
molecule in association with Fett ion an .
U
4 pyrrole rings
^
.
4 carbons +
1
nitrogen
, what is
myoglobinmuscles
?
A
protein located in that
facilitates the
diffusion
of oxygen through the cell
for
the
generation of cellular
available
energy and
provides
need
a reserve
supply of oxygen
in times
of
.
The molecular mechanism for O2 binding to
haem was elucidated using myoglobin.
Mechanism for myoglobin is the same as
occurs in a single Haemoglobin subunit.
Q How was the structure
determined ?
of myoglobin
using way ✗
crystallography
-
helices linked to
Myoglobin contains a
form
-
structure
a
globular
.
, Yumi
group
The ability of myoglobin, and hemoglobin as well, to bind oxygen
depends on the presence of a bound prosthetic group called heme.
It gives muscle and blood their distinctive red color. It con-
sists of an organic component and a central iron atom.
The organic component, called protoporphyrin, is made up of four
pyrrole rings linked by methine bridges to form a tetrapyrrole ring.
Four methyl groups, two vinyl groups, and two propionate side
chains are attached.
The iron atom lies in the center of the protoporphyrin, bonded to
the four pyrrole nitrogen atoms.
Under normal conditions, the iron is in the ferrous (Fe2+) oxidation
state. The iron ion can form two additional bonds, one on each side
of the heme plane.
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