The binding saturation of this protein is defined by Hüfner’s constant. Ligand saturation was incorporated in an equation to explain rates of successive binding to this protein (15[1])by Gilbert (15[1])Smithson (15[2])Adair after observing its unusual Hill coefficient. (15[4])The larger (15[1])binding pocket of this (15[1])protein when unbound allows 2,3-BPG (15[3])to function (15[1])as an (15[1])allosteric (15[1])effector. (15[1])Upon binding, the conformation of this protein changes from its T, (15[1])or (*) tense, (10[1])state (10[1])to its R, or relaxed, (10[1])state. The “fetal” form of this protein (10[3])replaces the two beta subunits of its tetrameric structure with two gamma subunits. Perpendicular bond formation with the porphyrin ring in this protein’s binding site leads (10[1])carbon monoxide (10[1])to bind (10[2])to it (10[2])with 250 times (10[1])more (10[1])affinity (10[1])than oxygen. (10[2])For 10 points, (10[1])name this iron-containing protein found in blood. ■END■