Explain how cooperativity enhances hemoglobin O₂ loading at high O₂ concentration and O₂ unloading at low O₂ concentration and interpret a graph of hemoglobin oxygen binding
a. Hemoglobin binds O₂ reversibly, loading O₂ on the lungs and unloading it into other parts of the body
b. When O₂ binds to one subunit, the other change shape slightly, increasing their affinity for O₂
c. A slight change in PO₂ causes hemoglobin to load or unload a substantial amount of O₂
d. Low pH decreases the affinity of hemoglobin for O₂ (Bohr effect)