Elucidation of cooperative binding of oxygen to hemoglobin from the standpoint of the electronic theory of the heme cofactor

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Hemoglobin is the heme-containing oxygen-transport protein in the red blood cell. Highly efficient oxygen-transport of hemoglobin is achieved by cooperative oxygen binding properties of the protein. In this study, molecular mechanism responsible for the cooperative oxygen binding of the protein has been investigated from the standpoint of a novel theory, i.e., the electron theory of the heme cofactor. The study revealed that electronic interaction among the heme π-system, the heme iron, and the F-bound histidine plays a crucial role in control of the cooperative oxygen binding of the protein.