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What does hemoglobin have that myoglobin does not which makes positive cooperatively in binding oxygen possible?

What does hemoglobin have that myoglobin does not which makes positive cooperatively in binding oxygen possible?

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Answer #1

The reason behind this is mainly because of the structural difference between hemoglobin and myoglobin.

Hemoglobin is the oxygen carrying molecule that we can find in human blood. Myoglobin is the oxygen carrying molecule in the muscle tissues. Hemoglobin is a tetramer which means it consists of 4 haem groups. Myoglobin is monomeric and it contains only one haem group. Because of this having only one group it could not show cooperativity in oxygen binding. As said above hemoglobin has four subunits. If one subunit binds to oxygen it increases the other three will do the same.

Usually myoglobins have more affinity towards oxygen rather than hemoglobin. The cooperative behaviour allows hemoglobin to be more efficient in transporting oxygen.

Oxygen binding curve is a plot of fractional saturation (binding sites for oxygen ) verses partial pressure of oxygen.

For myoglobin a hyperbolic curve is obtained it shows the non-cooperativity of myoglobin and a sigmoidal curve is obtained for hemoglobin which shows the positve cooperativity of hemoglobin.

Haemoglobin Hb - Hb (O2) : positive co-operative - binding Myoglobin Mb - MbO2 : Non-cooperatie bindingT + fractional 0.8 sahrahon 0.67 tuto ०.०: 5 50 + bo - pO₂ (Toos) A - oxygen binding by myoglobin B- onugen binding by hemogl

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