The binding of zinc to human deoxyhemoglobin and its possible relevance to the anti-sickling effect of zinc.
We find only one major zinc binding site in crystals of deoxyhemoglobin A. It is located at an interface between adjacent tetramers where residues histidine 116, histidine 117, and glutamate 26 on the beta 1 chain of one tetramer are in close proximity to lysine 16 and glutamate 116 on the alpha 2 chain of a neighboring tetramer. If this intertetramer contact does not exist in the rigid fibers of polymerized deoxyhemoglobin S, then low levels of zinc may promote its formation at random points along the fiber and thereby inhibit the formation of long fibers.
D000755:Anemia, Sickle Cell / Q000209:etiology; D001665:Binding Sites; D006451:Hemoglobin, Sickle; D006454:Hemoglobins; D006801:Humans; D011485:Protein Binding; D015032:Zinc / Q000172:deficiency / Q000378:metabolism*
D006451:Hemoglobin, Sickle; D006454:Hemoglobins; D015032:Zinc