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Oxygen Myoglobin Dissociation Curve

  • As shown in the animation, an isolated muscle fiber has been placed in a vial of deoxygenated blood. Inside the muscle fiber, each molecule of myoglobin can bind one O2. The O2-Mb bond is reversible, and the direction of the reaction is dependent on the concentration of O2 (partial pressure or pO2) in the surrounding fluids.

pO2

Mb + O2 <———–>MbO2

  • Therefore, as more image descriptionO2 is forced into the vial of blood, the myoglobin becomes increasingly saturated.
An animation that demonstrates how myoglobin becomes increasingly saturated.
An animation that demonstrates how myoglobin becomes increasingly saturated.
An animation that demonstrates how myoglobin becomes increasingly saturated.
An animation that demonstrates how myoglobin becomes increasingly saturated.
An animation that demonstrates how myoglobin becomes increasingly saturated.
An animation that demonstrates how myoglobin becomes increasingly saturated.
An animation that demonstrates how myoglobin becomes increasingly saturated.
An animation that demonstrates how myoglobin becomes increasingly saturated.
An animation that demonstrates how myoglobin becomes increasingly saturated.
An animation that demonstrates how myoglobin becomes increasingly saturated.
An animation that demonstrates how myoglobin becomes increasingly saturated.
An animation that demonstrates how myoglobin becomes increasingly saturated.
Myoglobin becomes saturated as o2 is forced into the blood.
  • Therefore, as more O2 is forced into the vial of blood, the myoglobin becomes increasingly saturated.
  • The steep (= hyperbolic) dissociation curve indicates that much lower concentrations of O2 are needed to saturate myoglobin molecules compared with hemoglobin molecules, which have four heme groups.The myoglobin and hemoglobin molecules