Studies on the reactions of hydrogen peroxide with Sickle cell haemoglobin

The reaction between hydrogen peroxide and myoglobin (or haemoglobin) ferric haem is a two -electron redox process, yet the stable final product is ferrylhaem, retaining only one oxidizing equivalent. The ferrylhaem produced from the reaction enhances oxidation-related toxicity associated with inflammation, ischemia and hemolytic disorders. The aim of this study was to compare sickle cell and normal adult haemoglobin reactions with H2O2 to elucidate the possible role of such reactions in the pathology of sickle cell anaemia. This studied was carried out using UV-visible spectroscopy and HPLC. The UV-visible spectroscopy investigations show that the reactivity of ferric HbS with hydrogen peroxide show s identical and almost indistinguishable pattern to that of normal adult ferric HbA. The HPLC chromatographic pattern of hydrogen peroxide induced haem-protein cross link in sickle cell haemoglobin (HbS) is identical to that of normal adult haemoglobin (HbA). This probably underlines the fact no significant instability exist in the relationship between the sickle cell Hb haem pocket and its globin as a result of the mutation.