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Part a shows disc-shaped red blood cells. An arrow points from a red blood cell to the hemoglobin in part b. Hemoglobin is made up of coiled helices. The left, right, bottom, and top parts of the molecule are symmetrical. Four small heme groups are associated with hemoglobin. Oxygen is bound to the heme.
The protein inside (a) red blood cells that carries oxygen to cells and carbon dioxide to the lungs is (b) hemoglobin. Hemoglobin is made up of four symmetrical subunits and four heme groups. Iron associated with the heme binds oxygen. It is the iron in hemoglobin that gives blood its red color. Source: OpenStax Biology 2e

OpenStax Biology 2e

Hemoglobin, or Hb, is a protein molecule found in red blood cells (erythrocytes) made of four subunits: two alpha subunits and two beta subunits. Each subunit surrounds a central heme group that contains iron and binds one oxygen molecule, allowing each hemoglobin molecule to bind four oxygen molecules. Molecules with more oxygen bound to the heme groups are brighter red. As a result, oxygenated arterial blood where the Hb is carrying four oxygen molecules is bright red, while venous blood that is deoxygenated is darker red.

It is easier to bind a second and third oxygen molecule to Hb than the first molecule. This is because the hemoglobin molecule changes its shape, or conformation, as oxygen binds. The fourth oxygen is then more difficult to bind. The binding of oxygen to hemoglobin can be plotted as a function of the partial pressure of oxygen in the blood (x-axis) versus the relative Hb-oxygen saturation (y-axis). The resulting graph—an oxygen dissociation curve—is sigmoidal, or S-shaped. As the partial pressure of oxygen increases, the hemoglobin becomes increasingly saturated with oxygen.

The graph plots percent oxygen saturation of hemoglobin as a function of oxygen partial pressure. Oxygen saturation increases in an S shaped curve, from 0 to 100 percent. The curve shifts to the left under conditions of low carbon dioxide, high p H, and low temperature, and to the right in conditions of high carbon dioxide, low p H, or high temperature.
The oxygen dissociation curve demonstrates that, as the partial pressure of oxygen increases, more oxygen binds hemoglobin. However, the affinity of hemoglobin for oxygen may shift to the left or the right depending on environmental conditions. Source: OpenStax Biology 2e


Clark, M., Douglas, M., Choi, J. Biology 2e. Houston, Texas: OpenStax. Access for free at: https://openstax.org/details/books/biology-2e

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