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Myoglobin has a very high affinity for oxygen, meaning it binds it very strongly. At very low oxygen concentrations in the cell, myoglobin releases its oxygen, despite the high affinity, simply because there are too few oxygen molecules around to rebind to the myoglobin when they are released naturally from the myoglobin (which usually occurs anyway).

Once the oxygen concentration increases again, returning to normal, oxygen molecules will collide with myoglobin. The myoglobin, with its high oxygen affinity, will strongly bind any oxygen that meets it, replenishing myoglobin's oxygen storage very quickly.

As myoglobin's affinity for oxygen is stronger the haemoglobin's, it will 'steal' oxygen from haemoglobin in the blood very easily, replacing its bound oxygen.

This binding system serves to release oxygen when it is needed if blood oxygen levels are reduced (due to high levels of exercise), but replenishes the supply when oxygen levels begin to rise again.

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