The Hill equation was first used to describe the cooperative binding of this protein. The fetal form of this protein has a higher affinity than its adult form because it does not interact with 2,3-BPG ["two three b-p-g"]. This protein shows a lower binding affinity under acidic conditions and in higher carbon dioxide concentrations, a phenomenon known as the Bohr shift. This protein consists of two alpha and two beta subunits, and like catalase it contains four porphyrin rings with iron centers. This protein has a higher affinity to carbon monoxide than its typical substrate, oxygen. For 10 points, name this protein found in red blood cells.
The Hill equation was first used to describe the cooperative binding of this protein. The fetal form of this protein has a higher affinity than its adult form because it does not interact with 2,3-BPG ["two three b-p-g"]. This protein shows a lower binding affinity under acidic conditions and in higher carbon dioxide concentrations, a phenomenon known as the Bohr shift. This protein consists of two alpha and two beta subunits, and like catalase it contains four porphyrin rings with iron centers. This protein has a higher affinity to carbon monoxide than its typical substrate, oxygen. For 10 points, name this protein found in red blood cells.