In hemoglobin Rainier, Tyr 145 is replaced by Cys, which forms a disulfide bond with another Cys

Question:

In hemoglobin Rainier, Tyr 145β is replaced by Cys, which forms a disulfide bond with another Cys residue in the same subunit. This prevents 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?