Arnone A, Williams D
Prog Clin Biol Res. 1977;14:317-28.
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.
我们在脱氧血红蛋白A晶体中仅发现一个主要的锌结合位点。它位于相邻四聚体之间的界面处，其中一个四聚体β1链上的组氨酸116、组氨酸117和谷氨酸26与相邻四聚体α2链上的赖氨酸16和谷氨酸116紧密相邻。如果在聚合的脱氧血红蛋白S的刚性纤维中不存在这种四聚体间接触，那么低水平的锌可能会促进其在纤维上的随机点形成，从而抑制长纤维的形成。
