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Adult human hemoglobin (HbA) is the primary oxygen-transport metalloprotein found in red blood cells, characterized by a heterotetrameric structure consisting of two alpha (α) and two beta (β) globin chains (StatPearls, 2023). Each subunit contains a prosthetic heme group with a central iron atom capable of reversibly binding one molecule of oxygen (UniProt, 2024). Beyond oxygen delivery, HbA plays a vital role in transporting carbon dioxide and buffering blood pH through the Bohr effect. In clinical medicine, HbA is a major therapeutic target for hemoglobinopathies like sickle cell disease, where drugs like voxelotor stabilize the oxygenated state to inhibit the polymerization of mutant hemoglobin (FDA, 2019). It also serves as a critical diagnostic tool, with glycated hemoglobin (HbA1c) levels reflecting average blood glucose over several months (PubMed, 2021).
Allosteric modulation to increase oxygen affinity and stabilize the relaxed (R) state, or competitive binding at the heme iron site.
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