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REVERSIBLE BINDING OF
OXYGEN

BY,
KRISHNAJA K J
IMSc
35218043
NEED FOR TRANSPORT OF OXYGEN
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 Every cell in our body is in constant requirement of energy

 It is the oxidation of metabolic fuel that releases energy.
 Hence efficient transport and storage of O2 is very important.
Specialised protein is present in RBC of blood for transport of
O2 : Hemoglobin
HOW IS O2 TRASPORTED
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• O2 move from high pO2 to low

pO2
• Partial pressure of oxygen is the
order
lungs > capillaries >tissue
STRUCTURE OF HEMOGLOBIN
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The heme part of Hb is responsible
for O2 binding

• Each Hb molecule binds with four molecules O2,

corresponding to 1 ml O2 per 1 g Hb.
• Hb that contain O2 - Oxyhemoglobin
• Hb that do not contain O2 – Deoxyhemoglobin
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T State R State

In deoxy hemoglobin, Fe atom is too big to fit into the center of protoporphyrin due to large electron density.
Hence it will be found slightly below the protoporphyrin chain.
Binding of O2 on to the Fe atom pulls away the electron density of atom, reducing its atomic radii, enabling Fe atom can
easily fit in the cavity.
COOPERATIVE BINDING
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
Cooperative binding:
Binding of O2 onto heme site of one subunit increases the affinity of
other subunits towards O2.
It is caused due to conformational changes caused by indirect
interaction between heme group when T form changes to R form

The sigmoid(S) shape of curve is due to cooperative binding.

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REFERENCES

Wolfgang Kaim, Brigitte Schwederski, Axel Klein - Bioinorganic Chemistry -

Inorganic Elements in the Chemistry of Life_ An Introduction and Guide-Wiley
(2013)

Ivano Bertini, Harry B. Gray, Stephen J. Lippard - Bioinorganic Chemistry-

University Science Books (1994)
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