In the text, we learned that BPG is abundantly present in erythrocytes to greatly reduce the affinity of hemoglobin for oxygen. When 2,3-BPG binds to deoxyhemoglobin, it acts to stabilize the low oxygen affinity state (T state) of the oxygen carrier. What would happen to hemoglobin if the BPG were removed? Would our body still be able to efficiently deliver oxygen to the tissues?
In the text, we learned that BPG is abundantly present in erythrocytes to greatly reduce the affinity of hemoglobin for oxygen. When 2,3-BPG binds to deoxyhemoglobin, it acts to stabilize the low oxygen affinity state (T state) of the oxygen carrier. What would happen to hemoglobin if the BPG were removed? Would our body still be able to efficiently deliver oxygen to the tissues?
The α and β subunits of hemoglobin are homologous and have similar three-dimensional structures. The capacity of hemoglobin to bind oxygen depends on the presence of a bound prosthetic group called heme. The heme group is responsible for the distinctive red color of blood. The heme group consists of an organic component and a central iron atom.
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