The dissociation and binding of oxygen by hemoglobin is not directly proportional to the pO₂ of its environment but instead exhibits a sigmoid-curve relationship termed:

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The hemoglobin oxygen dissociation curve describes the sigmoid-curve relationship between the pO2 of the environment and the binding of oxygen by hemoglobin. This curve reflects the cooperative binding of oxygen by hemoglobin, where the binding of the first oxygen molecule enhances the affinity of hemoglobin for subsequent oxygen molecules. As a result, the curve shows a steep increase in oxygen uptake by hemoglobin at low pO2 levels and a plateau at high pO2 levels, indicating near-saturation of hemoglobin with oxygen. The Embden-Meyerhof and phosphogluconate pathways are metabolic pathways involved in glucose metabolism, while the Luebering-Rapaport pathway is related to the production of 2,3-bisphosphoglycerate, a molecule that modulates the oxygen-binding properties of hemoglobin.

The Dissociation and Binding of Oxygen by Hemoglobin Is Not