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Keny Keny
wrote...
6 years ago
When hemoglobin experiences the Bohr effect, the protonation of residues at the N-terminus of the alpha subunits is responsible for ~30% of the 0.6 mol of protons bound to hemoglobin upon release of 1 mol of O2 at physiological pH. If this residue has a pKa of 7.0 in oxyhemoglobin, what is its pKa in deoxyhemoglobin.
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wrote...
6 years ago
Let's start by defining the bohr-effect:

- Enhances O₂ transport.
- The conformational changes in Hb that occur in O binding decreases pKs of several groups
- An increase in pH (remove protons), it stimulates Hb to bind more O₂ at lower oxygen pressure

Lower pH = easier release.
(lower [H+], basic) promotes tighter binding of oxygen to hemoglobin

Higher pH = difficult to release.
(higher [H+], acidic) permits the easier release of oxygen from hemoglobin

Someone else can take it from here
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