Conformational changes in oxyhemoglobin C (Gluβ6 → Lys) detected by spectroscopic probing

Abstract

Hemoglobin C (Glu β6 → Lys) shares with hemoglobin S (Gluβ6 → Val) the site of mutation, but with different consequences: deoxyHbS forms polymers, whereas oxyHbC readily forms crystals. The molecular mechanism for this property of oxyHbC is unknown. Since no detailed oxyHbC crystal structural information exists, spectroscopic probing is used in this study to investigate possible solution-phase conformational changes in HbC compared with HbA. Intrinsic fluorescence combined with UV resonance Raman data demonstrate a weakening of the Trpβ15-Serβ72 hydrogen bond that most likely leads to a displacement of the A helix away from the E helix.