Does myoglobin show cooperativity in O2 binding? If not, what structural differences account for this?
Myoglobin does not show cooperativity because it is monomeric
Myoglobin does not show cooperativity in O2 binding. The structural differences between myoglobin and hemoglobin account for this.
Myoglobin is a monomeric protein with a single heme binding site, whereas hemoglobin is a tetrameric protein with four heme binding sites. In hemoglobin, the binding of O2 to one subunit affects the affinity of the other subunits for O2. This is known as cooperativity and results in sigmoidal O2 dissociation curve.
On the other hand, myoglobin does not show cooperativity because it only has one heme binding site. Therefore, the binding of O2 to one heme site does not affect the affinity of other heme sites as it only has one binding site.
In summary, myoglobin does not show cooperativity in O2 binding due to its monomeric structure and single heme binding site.
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