Abstract
In hemoglobin (Hb) Roanne, the aspartate residue α 94(G1) is replaced by a glutamic acid. This residue plays a key role in the structural changes affecting the α1β2 contact area during the deoxy- to oxy-state transition in the hemoglobin molecule. Aspartate α94(G1) is involved in several contacts both in the deoxy- and oxy-structures. The most important of those is a hydrogen bond with asparagine β102 (G4), stabilizing the oxygenated structure. Alteration of this contact usually leads to a decrease in oxygen affinity. Hb Roanne is the first example in which an increased oxygen affinity was found as a result of a structural modification at this position. Functional data suggested that the mechanisms responsible for this altered property are a destabilisation of the T-structure and a modification of the allosteric equilibrium.
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