In hemoglobin, the transition from t state to r state (low to high affinity) is triggered by Bisphosphoglycerate (BPG)
Bisphosphoglycerate (BPG), also known as 2,3-Disphosphoglycerate (2,3-DPG), aids in the transition of hemoglobin from a high-oxygen-affinity to a low-oxygen-affinity state.
2,3-BPG binds to hemoglobin, causing oxygen to be unloaded. Furthermore, 2,3-BPG reduces hemoglobin's affinity for oxygen. As hemoglobin is unloaded in our tissues, 2,3-BPG binds to it, promoting oxygen unloading.
When we increase the concentration of 2,3-BPG in our blood, the oxygen binding curve shifts to the right. This means hemoglobin will have a lower affinity for oxygen and will be able to deliver more oxygen to our body's tissues and cells.
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