Perspective Chapter: Iron Chelation Inhibits Reduced Glutathione (GSH) as a Prooxidant in Iron-Mediated Hemoglobin Oxidation in Purified Hemoglobin

As a trace element, iron is required by all living. Although this crucial metal is required, maintaining its biological equilibrium in an organism is far more important than any other trace element. Excess iron plays a vital role in the generation of harmful oxygen radicals due to its catalysis of one electron redox chemistry. In disorders such as thalassemia and sickle cell anemia, this is clearly visible. In vitro experiments were carried out using pure hemoglobin (HbA) exposed to ferric (Fe3+) iron. The addition of Fe3+ (0–250 µM) caused spectrophotometric alterations in the absorption spectra (500–700 nm) of (40 µM HbA; pH 7.4). There was no HbA oxidation in the absence of Fe3+. Similarly, unlike hemolysates, the mere addition of Fe3+ to HbA exhibited negligible oxidative consequences. However, the addition of glutathione (GSH) and Fe3+ caused significant oxidation. The iron chelators (DFO desferrioxamine or Deferiprone L1) suppressed Fe3+-mediated HbA oxidation in a dose-dependent manner. The findings of this study have important significance for damage mechanisms in disorders like as thalassemia and sickle cell anemia. In addition, our findings suggest that chelating bioreactive iron within aberrant erythrocytes might be a potential therapy strategy.