HISTIDINE & FERROUS IONS NEW TYPE OF OXYGEN CARRIER FOR THALASSEMIA PATIENTS

In thalassemia, a genetic mutation disrupts the production of hemoglobin, the vital protein in redblood cells responsible for carrying oxygen. This defect leads to the creation of abnormalhemoglobin molecules that are unstable and prone to breaking down. Consequently, the redblood cells are fragile, short-lived, and cannot effectively pick up or transport oxygen throughoutthe body. This fundamental failure in oxygen delivery results in the symptoms of anemia, such asfatigue and shortness of breath. Histidine, an amino acid commonly found in the active sites ofproteins like hemoglobin, plays a crucial role in binding an iron ion (Fe²⁺). This histidine-ironcomplex is then able to bind molecular oxygen (O₂). The process typically involves the Fe²⁺ ion,which is coordinative unsaturated, meaning it has an open binding site. The O₂ molecule thenbinds directly to this available site on the iron, forming a coordinate covalent bond. In manybiological systems, the oxygen binding event triggers a subtle change in the geometry of the ironatom, pulling the histidine residue and the surrounding protein structure, a key step in facilitatingoxygen transport.