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At onset of muscle contraction, myoglobin (Mb) immediately releases its bound O 2 to the mitochondria. Accordingly, intracellular O 2 tension (P mb O 2) markedly declines in order to increase muscle O 2 uptake (m O 2).t onset of muscle contraction, myoglobin (Mb) immediately releases its bound O 2 to the mitochondria. Accordingly, intracellular O 2 tension (P mb O 2) markedly declines in order to increase muscle O 2 uptake (m O 2).
For one the protein has only one binding site for oxygen on the one heme group on the protein. While myoglobin can only hold one oxygen, the affinity for that oxygen is very high compared to hemoglobin.This is likely due to the fact that hemoglobin, transporting 4 oxygens to the tissues and muscles where myoglobin is mostly present.hile myoglobin can only hold one oxygen, the affinity for that oxygen is very high compared to hemoglobin. This is likely due to the fact that hemoglobin, transporting 4 oxygens to the tissues and muscles where myoglobin is mostly present.