No more than 3 sentences, but be very specific: why is myoglobin's hyperbolic O2 binding better...

No more than 3 sentences, but be very specific: why is myoglobin's hyperbolic O2 binding better suited for muscle and hemoglobin's allosteric binding better for blood?

Expert Solution

A very simple answer is relative affinity and efficiency.

Hemoglobin can release oxygen more easily than can myoglobin, which allows myoglobin to have a higher overall efficiency in binding and then releasing oxygen species. For this reason, the body tends to use hemoglobin more often for oxygen-distributing purposes, although myoglobin is used as well, particularly for carrying oxygen to muscle cells. Binding of carbon monoxide to heme is much stronger than that of oxygen. Once hemoglobin is fully saturated with oxygen,the oxyhemoglobin circulates to deoxygenated blood, oxygen is incrementally unloaded and the affinity of hemoglobin for oxygen is reduced. Thus at the lowest oxygen binding affinity of hemoglobin for oxygen is very low allowing maximal delivery of oxygen to the blood. In contrast the oxygen binding curve for myoglobin is hyperbolic in character indicating the absence of allosteric interactions in this process.

3 sentence answer:

myoglobin can be fully oxygen saturated in the tissues, hemoglobin requires much higher oxygen tension to become fully saturated which only occurs in the lungs. The position of HbF (fetal hemoglobin) saturation to the left of HbA (adult hemoglobin i.e. at lower oxygen tension) reflects the fact that fetal hemoglobin binds oxygen with higher affinity than adult hemoglobin and this is so that the fetus can acquire oxygen from the maternal circulation.

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queen_honey_blossom answered 2 years ago

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