Question

In hemoglobin Rainier, Tyr 145β is replaced by Cys, which forms a disulfide bond with another Cys residue in the same subunit. This pre- vents the formation of ion pairs that normally stabilize the T state. How does hemoglobin Rainier differ from normal hemoglobin with respect to (a) oxygen affinity, (b) the Bohr effect, and (c) the Hill constant? .

Answer 1

Hemoglobin rainier differ from normal hemoglobin with respect to oxygen affinity.

Step-by-step explanation:

Hemoglobin is one of the most significant protein of Red Blood Cell containing heme(that contain Fe2+ which is coordinated with four porphyrine rings) and globin protein.

Hemoglobin exist in two state one is tensed state or deoxy hemoglobin that have less affinity for oxygen, the other state is relaxed state or oxy hemoglobin that has high affinity for oxygen.

In hemoglobin rainer the formation of new di sulfide bond prevent the formation of ion pairs that normally stabilize the T state as a result T state get unstable and this unstable T state is converted to R state to achieve the stability of hemoglobin structure.

The R or relaxed state of hemoglobin has high oxygen affinity for oxygen.