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The effect of pH on the rate of dissociation of the oxygenated beta chain tetramer of Hb A

Biochemical and Biophysical Research Communications, ISSN: 0006-291X, Vol: 111, Issue: 1, Page: 55-60
1983
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The effect of pH on the overall assembly of oxyhemoglobin A following mixing of equivalent concentrations of α and β heme subunits has been studied in 0.1 M potassium phosphate buffers at 20°C. The resultant kinetic profiles monitored at 582.5 nm (the maximum of the oxyhemoglobin — oxy chain difference spectrum) were homogeneous and appeared to be first order. The rate of these exponential time courses, reflecting the rate of dissociation of the β chain tetramer, increased from 0.013 min −1 at pH 6.4 to 0.30 min −1 at pH 8.0 and 1.0 min −1 at pH 8.5. Concurrent with this increased rate was a decrease in the overall color yield from the reaction. The absorbance changes, which involve a significant contribution from the β chain tetramer to monomer dissociation step, changed three fold over the pH range studied. The findings indicate that protons enhance the stability of the β chain tetramer.

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