why myoglobin have high high efficiency for oxygen then hemoglobin?
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Haemoglobin has less affinity for binding oxygen and its concentration is higher in RBC (red blood cells). So when oxygen binds to the first subunit of haemoglobin, it changes into the quaternary structure of the protein and thus making easier for other molecules to bind.
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And unlike hemoglobin which is found in the red blood cells, myoglobin is found in muscle tissues. Myoglobin owes its high affinity for oxygen to several factors. ... Although it has a much higher affinity for oxygen than its structural analog hemoglobin, myoglobin is a less efficient oxygen carrier for the cell.
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