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The oxygen–hemoglobin dissociation curve, also called the oxyhemoglobin dissociation curve or oxygen dissociation curve (ODC), is a curve that plots the proportion of hemoglobin in its saturated (oxygen-laden) form on the vertical axis against the prevailing oxygen tension on the horizontal axis. This curve is an important tool for ...
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Hemoglobin's oxygen binding affinity (see oxygen–haemoglobin dissociation curve) is inversely related both to acidity and to the concentration of carbon dioxide. [1] That is, the Bohr effect refers to the shift in the oxygen dissociation curve caused by changes in the concentration of carbon dioxide or the pH of the environment.
Dissociation curve may refer to: Ligand (biochemistry)#Receptor/ligand binding affinity represented in a graph; Oxygen-haemoglobin dissociation curve, a graphical representation of oxygen release from haemoglobin; Melting curve analysis, a biochemical technique relying on heat-dependent dissociation between two DNA strands
The sigmoidal shape of hemoglobin's oxygen-dissociation curve results from cooperative binding of oxygen to hemoglobin. An example of positive cooperativity is the binding of oxygen to hemoglobin. One oxygen molecule can bind to the ferrous iron of a heme molecule in each of the four chains of a hemoglobin molecule.
Histidine residues in hemoglobin can accept protons and act as buffers.Deoxygenated hemoglobin is a better proton acceptor than the oxygenated form. [1]In red blood cells, the enzyme carbonic anhydrase catalyzes the conversion of dissolved carbon dioxide to carbonic acid, which rapidly dissociates to bicarbonate and a free proton:
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This results in the Hb-O 2 dissociation curve being shifted downward and not just to the right. At low pH, hemoglobins showing the Root effect don't become fully oxygenated even at oxygen tensions up to 20kPa. [2] This effect allows hemoglobin in fish with swim bladders to unload oxygen into the swim bladder against a high oxygen gradient. [3]