Protein molecules w/ a quaternary structure evolved to make efficient loading of O2 under one set of conditions but unloading it under a different set of conditions
O2 not soluble in H2O but Hb are = efficient O2 transport if bound to Hb = Hb must readily associate with O2 at surface where gas exchange takes place & readily dissociate from O2 at those tissues requiring it
Shape of Hb molecules makes it difficult for first O2 molecule to bind to one of the sites on one of four polypeptide subunits because they are closely united
At low O2 conc = little O2 binds to haemoglobin = gradient of curve = shallow initially
In theory = easier for haemoglobin to bind the 4th O2 molecule
In practice = harder = due to probability with majority of binding sites occupied = less likely that a single O2 molecule will find an empty active site to bind to = gradient of curve reduces and graph flattens off