In: Biology
Ans-
Each myoglobin can bind one oxygen molecule because it contains one heme per molecule.
This number is different from that of hemoglobin because myoglobin is monomer, so quaternary structure is absent in myoglobin. On the other hand, hemoglobin is a tetramer that consists of closely related subunits such as alpha and beta.
Myoglobin binds oxygen more tightly than does hemoglobin. In a deoxygenated state, hemoglobin has a low affinity for oxygen as compared to myoglobin. When oxygen binds the first subunit of hemoglobin, then it changes into the quaternary structure of the protein. Therefore, this makes to easier for an oxygen molecule to bind to the next subunit.