cooperative binding process of oxygen
shape of haemoglobin makes it hard for first oxygen to bind to a site on a polypeptide chain as they are very close so at low pO2 little oxygen binds to haemoglobin so loan saturation of O2
after first of O2 binds the quaternary structure changes so haemoglobin changes shape making it easier for 2nd & 3rd Oxygens to bind so O2 binds at a smaller increase in pO2 - higher affinity
after 3rd O2 binds it becomes harder for last O2 to bind as majority of binding sites are occupied so probability of Oxygen binding to an empty site is lower