OXYGEN–HEMOGLOBIN DISSOCIATION CURVE
Encyclopedia of Respiratory Medicine, Vol: 1-4, Page: 290-296
2006
- 2Citations
- 39Captures
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Book Chapter Description
The oxygen equilibrium curve of red blood cells is the relationship between the concentration of oxygen in solution and the fractional saturation of hemoglobin. Hemoglobin is a complex protein, made up of four subunits, each one with an iron-containing pyrrole group, heme. At the center of each heme group is an iron atom, the site of ligation of one oxygen molecule. Thus each molecule of hemoglobin can reversibly bind four molecules of oxygen. The mechanism of oxygen binding and release by hemoglobin is a result of interaction of the peptide subunits. The simplest model of this interaction involves two fundamental conformations, corresponding to a low-affinity deoxyhemoglobin (T or tense) and a high-affinity oxyhemoglobin (R or relaxed). As hemoglobin binds oxygen molecules sequentially, the conformation shifts from T to R, thereby increasing the affinity, a process called ‘cooperativity’. The physiologic consequence of cooperativity is that oxygen is bound to hemoglobin until red blood cells reach tissue capillary beds where it is released and available to participate in oxidative phosphorylation.
Bibliographic Details
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