Allosteric Effects
The conformational changes from the T to the R state is initiated by

binding of oxygen to the heme
movement of the proximal histidine towards the heme
reorganization of protein-protein contacts between the individual subunits
movement of the F-helix, which contains the proximal His

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Allosteric Effects
Bisphosphoglycerate (BPG) cannot bind to the oxygenated R state of hemoglobin because

it is displaced from the heme by movement of the proximal histidine
its binding pocket becomes too small to accommodate BPG
it is displaced from the heme by oxygen
BPG binds to the R state with the same affinity as the T state

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Allosteric Effects
O2 binding to hemoglobin results in

both (a) and (b)
100-fold lower affinity for the last O2 bound than for the first
100-fold higher affinity for the last O2 bound than for the first
extensive protein conformational change

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