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Structure of Haemoglobin

Haemoglobin is an iron-containing protein in red blood cells that transports oxygen and carbon dioxide throughout the body. It is made up of four polypeptide chains and a heme group containing iron. Each heme group binds one oxygen molecule, allowing haemoglobin to carry four oxygen molecules in total. The structure changes slightly between the deoxygenated (tense) state and oxygenated (relaxed) state, allowing it to efficiently deliver oxygen to tissues and pick up more from the lungs.

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627 views12 pages

Structure of Haemoglobin

Haemoglobin is an iron-containing protein in red blood cells that transports oxygen and carbon dioxide throughout the body. It is made up of four polypeptide chains and a heme group containing iron. Each heme group binds one oxygen molecule, allowing haemoglobin to carry four oxygen molecules in total. The structure changes slightly between the deoxygenated (tense) state and oxygenated (relaxed) state, allowing it to efficiently deliver oxygen to tissues and pick up more from the lungs.

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lotd6002
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STRUCTURE OF

HAEMOGLOBIN
1 RBC consists of
approximately 250
million Hb molecules
STRUCTURE OF HB- GENERAL
Haemoglobin is a hemoprotein only found in the cytoplasm of RBC
transports O
2
and CO
2
between lungs and various tissues
normal concentration of Hb in the blood:
adult males 135 175 g/L
adult females 120 168 g/L



STRUCTURE
Made up of heme +
Globin
4 polypeptide Subunits
Heme group
Porphyrin ring
Ferrous iron
Globin chain
2 Alpha Chains
2 Beta chains
HEME STRUCTURE
HEME IS A METALOPORPHYRINE
(CYCLIC TETRAPYRROLE)
Heme contains:
conjugated system of
double bonds red colour
4 nitrogen (N) atoms
1 iron cation (Fe
2+
)
bound in the middle of
tetrapyrrole skeletal by
coordination covalent
bonds

methine bridge pyrrole ring
PROPERTIES OF IRON IN HEME
Coordination number of
iron in heme = 6

6 bonds:
4x pyrrole ring (A,B,C,D)
1x link to a protein
1x link to an oxygen

STRUCURE OF GLOBIN
Globin:
Four polypeptide chains in one
molecule of Hb
Adult Hb(Hb A) has four
polypeptide chains
2 variety & 2 variety
consists of 141 AA and 146
AA
HbA is symbolised 2 2
Other types of normal Hb:
o Hb F (22)
o Hb A2(22) (2.5% of HbA)

STRUCURE OF HAEMOGLOBIN
With each of 4 polypeptide chains one haem
molecule is attached
Each haem part contains one iron molecule
With each iron molecule, one molecule O2 can
combine
With each molecule of Hb, 4 molecules of O2
can combine
Structure changes slightly during binding &
release of O2

BOND OF HAEMOGLOBIN
Bonds between 1 & 2 chains are
weaker than 1, 1.
1 & 2 are able to move and get
twisted, allowing change between tense
and relaxed form.
Tense form is present in deoxygenated
Hb
chains move away from each other
2,3 DPG binds here.
Presence of 2 3 DPG increases O2
delivery to tissues
Relaxed form is present in Oxygenated
Hb.
2 3 DPG expelled allowing further O2
binding.

Quaternary structure of deoxy- and
oxyhemoglobin
T-state (deoxy-state)
R-state (oxy-state)
THANK YOU

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