Hemoglobin: Difference between revisions
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Each individual <scene name='Hemoglobin/Deoxyheme/8'>heme</scene> molecule contains one | Each individual <scene name='Hemoglobin/Deoxyheme/8'>heme</scene> molecule contains one | ||
<scene name='Hemoglobin/Deoxyheme_fe/9'>Fe2+</scene> atom. In the lungs, where oxygen is abundant, an <scene name='Hemoglobin/Oxyheme_fe/7'> | <scene name='Hemoglobin/Deoxyheme_fe/9'>Fe2+</scene> atom. In the lungs, where oxygen is abundant, an <scene name='Hemoglobin/Oxyheme_fe/7'>oxygen molecule</scene> binds to the ferrous iron atom of the heme molecule and is later released in tissues needing oxygen. The heme group binds oxygen while still attached to the <scene name='Hemoglobin/Oxysubunit/8'>hemoglobin monomer</scene>. The spacefill view of the hemoglobin polypeptide subunit with an oxygenated heme group shows how the <scene name='Hemoglobin/Oxysubunitsf/4'>oxygenated heme group is held</scene> within the polypeptide. | ||
<scene name='Hemoglobin/Anchortrace/4'>Anchoring of the heme</scene> is facilitated by a histidine nitrogen that binds to the iron. A second histidine is near the bound oxygen. The "arms" (propanoate groups) of the heme are hydrophilic and face the surface of the protein while the hydrophobic portions of the heme are buried among the hydrophobic amino acids of the protein. | <scene name='Hemoglobin/Anchortrace/4'>Anchoring of the heme</scene> is facilitated by a histidine nitrogen that binds to the iron. A second histidine is near the bound oxygen. The "arms" (propanoate groups) of the heme are hydrophilic and face the surface of the protein while the hydrophobic portions of the heme are buried among the hydrophobic amino acids of the protein. | ||
