Define positive cooperativity and negative cooperativity. How are these related to oxygen binding/release, and how is this...

Define positive cooperativity and negative cooperativity. How are these related to oxygen binding/release, and how is this impacting the T or R states?

Expert Solution

Cooperativity is a usual phenomenon in biochemistry and it is the concept of asscoiation and dissociation reaction that is occurred in order to form a reaction. For example:- when oxygen binds to one of the heamoglobin subunits then it is called as positive cooperativity and negative cooperativity happens when the affinity of ligand for binding to the protein decreases. Example of negative coopeartivity is occurred between glyceraldehyde-3-phosphate and glyceraldehyde-3-phosphate dehydrogenase enzyme.

When the 4 subunits of haemoglobin do not bind to oxygen then they are 0.4A below in the plane of the ring. In this state it is called as T state or tetramer state. But when the haemoglobin has bound to oxygen then they make oxyhaemoglobin state which is more relaxed and in 3-haemoglobin, oxygen has 300 times more oxygen binding affinity than the deoxyhaemoglobin state. The oxyhaemoglobin state is known as relaxed or R state.

gladiator answered 7 months ago

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