Medical Allosteric effect on hemeglobin

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Hydrogen ions and 2,3-bisphosphoglycerate (2,3-BPG) interact primarily with the globin chains of hemoglobin rather than the porphyrin structure. Specifically, 2,3-BPG binds to deoxygenated hemoglobin (deoxy-Hb), promoting the release of oxygen by occupying a unique binding site between the beta chains, allowing only one molecule of BPG per hemoglobin tetramer. The binding of hydrogen ions, associated with the Bohr effect, occurs at multiple sites on the globin chains, influencing hemoglobin's oxygen affinity. The discussion emphasizes the complexity of these interactions and encourages exploration of conceptual challenges rather than basic textbook knowledge.
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where do hydrogen ion(Bohr effect) and 2,3 BPG bind to? porphyrin or just the globin chains?
 
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The protein chains. BPG binds to deoxy-Hb so favours deoxygenation. A bit unusual in that it binds just one molecule BPG per Hb tetramer (in the cavity between the beta chains).

I believe the Bohr protons bind in lots of places but I am not up to date.

This site is not for getting basic textbook information, more for conceptual difficulties and puzzles when you read the books or try to answer the problems. There is lots on the web e.g. http://www.biochem.arizona.edu/classes/bioc460/spring/460web/lectures/LEC8-9_MbHb_08-ppt.pdf

and lots of others.
 
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