The oxygen dissociation curve is essential in understanding how oxygen binds to and is released from hemoglobin within red blood cells. This graph plots the partial pressure of oxygen (\(\mathrm{PO}_2\)) against the oxygen saturation of hemoglobin. The curve is sigmoidal, or S-shaped, indicating cooperative binding. As oxygen molecules bind to hemoglobin, it becomes easier for additional oxygen molecules to bind.
The sigmoidal shape means that at high \(\mathrm{PO}_2\) levels (like in the lungs), hemoglobin is quickly saturated with oxygen; whereas at lower \(\mathrm{PO}_2\) levels (like in tissues), oxygen is released. Several factors can shift this curve, including 2,3-Diphosphoglycerate (2,3-DPG), pH, and temperature.
- A rightward shift indicates a decrease in oxygen affinity, meaning hemoglobin releases oxygen more readily.
- A leftward shift means increased oxygen affinity, which makes it harder for hemoglobin to release oxygen.