Editor-In-Chief: C. Michael Gibson, M. It binds with greater affinity to deoxygenated hemoglobin e. In bonding to partially deoxygenated hemoglobin it allosterically upregulates the release of the remaining oxygen molecules bound to the hemoglobin, thus enhancing the ability of RBCs to release oxygen near tissues that need it most. Its function was discovered in by Reinhold Benesch and Ruth Benesch.
It is broken down by a phosphatase to form 3-phosphoglycerate. Its synthesis and breakdown are therefore a way around a step of glycolysis. When 2,3-BPG binds deoxyhemoglobin, it acts to stabilize the low oxygen affinity state T state of the oxygen carrier. It fits neatly into the cavity of the deoxy- conformation, exploiting the molecular symmetry and positive polarity by forming salt bridges with lysine and histidine residues in the four subunits of hemoglobin.
The R state, with oxygen bound to a heme group, has a different conformation and does not allow this interaction. By selectively binding to deoxyhemoglobin, 2,3-BPG stabilizes the T state conformation, making it harder for oxygen to bind hemoglobin and more likely to be released to adjacent tissues. Conditions of low tissue oxygen concentration such as high altitude 2,3-BPG levels are higher in those acclimated to high altitudes , airway obstruction , or congestive heart failure will tend to cause RBCs to generate more 2,3-BPG in their effort to generate energy by allowing more oxygen to be released in tissues deprived of oxygen.
Ultimately, this mechanism increases oxygen release from RBCs under circumstances where it is needed most. This release is potentiated by the Bohr effect in tissues with high energetic demands.
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This review article describes the synthesis and breakdown of 2,3-DPG in the Embden-Meyerof pathway in red cells and briefly explains the molecular basis for its effect on oxygen affinity.
Interaction of the effects of pH, Pco2, temperature and 2,3-DPG on the oxyhaemoglobin dissociation curve are discussed. The role of 2,3-DPG in the intraerythrocytic adaptation to various types of hypoxaemia is described. The increased oxygen affinity of blood stored in acid-citrate-dextrose ACD solution has been shown to be due to the decrease in the concentration of 2,3-DPG which occurs during storage.
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