Oxygen (O2) competitively and reversibly binds to hemoglobin, with certain changes within the environment altering the affinity in which this relationship occurs. The sigmoidal shape of the oxygen dissociation curve illustrates hemoglobin’s propensity for positive cooperativity, as hemoglobin undergoes conformational changes to increase its affinity for oxygen as molecules progressively bind to each of its four available binding sites. The Bohr effect describes hemoglobin’s lower affinity for oxygen secondary to increases in the partial pressure of carbon dioxide and/or decreased blood pH. This lower affinity, in turn, enhances the unloading of oxygen into tissues to meet the oxygen demand of the tissue.
Copyright © 2023, StatPearls Publishing LLC.