Oxygen in myoglobin

Ribbon views of proteins with varying amounts of helices and pleated sheets. Immunoglobulin, an antibody, is made up almost entirely of pleated sheets (magenta). Myoglobin, which stores oxygen in muscle tissue, is composed of about 70% helix (blue). G-Actin, a component of muscle protein fibers, is a complex mixture of helices and pleated sheets. Regions with no specific secondaiy stmcture are shown in orange. 

Each heme unit in myoglobin and hemoglobin contains one ion bound to four nitrogen donor atoms in a square planar arrangement. This leaves the metal with two axial coordination sites to bind other ligands. One of these sites is bound to a histidine side chain that holds the heme in the pocket of the protein. The other axial position is where reversible binding of molecular oxygen takes place. 

The 4 g of iron in the human body is normally com-partmented into its functional locations in the haem- and non-haem-containing, and iron-binding proteins and enzymes (Fig. 3.5). The majority (65%) of the iron is in the divalent state in haemoglobin and myoglobin, which are involved in the transport and storage of oxygen in erythrocytes and myocytes, respectively. The remainder is distributed between storage sites, predominantly in the... 

Iron plays a special role as a key constituent of hemoglobin and myoglobin. These proteins carry, hemoglobin, or store, myoglobin, oxygen in the hnman body and in those of other mammals. It is the iron atom, as Fe +, to which molecnlar oxygen binds in these proteins. 

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