Carbon monoxide is a colorless, odorless gas that binds to hemoglobin at an oxygen-binding site. Indeed, it binds 200 times as tightly as oxygen, accounting for its toxic nature. Even if only one of the four oxygen-binding sites on hemoglobin is occupied by carbon monoxide and the remaining three are bound to oxygen, oxygen is not released. Explain.
Fetal hemoglobin (HbF) contains a Ser in place of a His at position 143 of the Ě chains of adult hemoglobin (HbA). Residue 143 faces the central cavity between the Ě chains.
a) What is the difference between the functional groups of the side chain Ser versus His?
b) Why does 2,3-BPG bind more tightly to deoxy HbA than to deoxy HbF?
c) How does the decreased affinity of HbF for 2,3-BPG affect the affinity of HbF for O2? (lower or higher)