Why myoglobin has higher affinity for oxygen than hemoglobin
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Myoglobin has higher affinity for oxygen than haemoglobin as it has a proximal histidine group which helps it to bind to oxygen, which is absent in haemoglobin.
Haemoglobin is present in RBCs while myoglobin in muscles.
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Myoglobin owes its high affinity for oxygen due to its has a proximal histidine group that helps it bind oxygen. Once the oxygen has been successfully bound, the structure of myoglobin becomes apparent. It prevents the reactive oxygen from escaping by modifying the natural reactivity of the heme group. By retarding the release of the oxygen with its structure, myoglobin can bind and hold on to oxygen atoms.
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