The Bohr effect is a crucial physiological phenomenon that describes how hemoglobin's affinity for oxygen is influenced by the concentration of carbon dioxide (CO2) and hydrogen ions (H+). In tissues where CO2 and H+ concentrations are high, hemoglobin binds to these molecules, forming carbaminohemoglobin (HbCO2) and protonated hemoglobin (HHb+). This binding stabilizes the T state of hemoglobin, leading to a decreased affinity for oxygen and promoting its release to the tissues. Consequently, the oxygen binding curve shifts to the right, indicating a higher dissociation of oxygen under these conditions.
Conversely, in the lungs, where CO2 and H+ concentrations are low, hemoglobin releases CO2 and is deprotonated, resulting in a higher pH (approximately 7.6). This transition causes hemoglobin to adopt a more favorable R state for oxygen binding, increasing its affinity for oxygen and shifting the oxygen binding curve to the left. The left shift signifies that hemoglobin can bind more oxygen in the lungs, optimizing oxygen uptake.
The oxygen binding curves illustrate these shifts: the blue curve represents hemoglobin in the lungs with high oxygen affinity, while the green curve represents hemoglobin in the tissues with lower affinity. The transition from the blue curve to the green curve exemplifies the Bohr effect, allowing hemoglobin to maximize oxygen binding in the lungs and optimize oxygen release in the tissues. This dynamic adjustment is essential for efficient gas exchange and oxygen delivery throughout the body.