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Hemoglobin Andrew has a mutation that stabilizes the R-state of hemoglobin. (A) Briefly explain Bohr effect....

Hemoglobin Andrew has a mutation that stabilizes the R-state of hemoglobin.

(A) Briefly explain Bohr effect.

(B) Would you expect the Bohr effect in Hemoglobin Andrew to be enhanced or reduced relative to normal hemoglobin?

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Answer #1

Ans ) A. Effect of pH on the oxygen affinity of hemoglobin is called Bohr effect. The oxygen binding affinity of Hb is lowered with low pH. pH decreases due to increase in PCO2. Bohr effect is caused due to binding of deoxyhemoglobin to hydrogen ions more readily than the
oxyhemoglobin. At low pH, H+ ion concentration is high, side chain of histidine present at beta chain of Hb gets protonated and deoxyhemoglobin is stabilized due to formation of salt bridge.
B ) Bohr effect is reduced in hemoglobin Andrew as Hb Andrew has increased oxygen affinity. It causes left shift in oxygen- Hb dissociation curve. The change in Hb is due to mutation of Lysine into asparagine at 144 position of beta chain.

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