Antholine W E, Basosi R, Hyde J S, Taketa F
J Inorg Biochem. 1984 Jun;21(2):125-36. doi: 10.1016/0162-0134(84)85045-x.
Human hemoglobin has been shown to contain a high- as well as a low-affinity binding site for cupric ion on each of its constitutent beta chains. The copper that is bound to the low-affinity site has been implicated in the selective oxidation of the beta hemes. In the present work a low-affinity binding site for cupric ion has been located within 10 A of the heme iron in human hemoglobin. It is suggested that the proximal histidine is involved in the binding of copper at this site and that it participates in the oxidation of heme iron and reduction of cupric ion.
已表明，人血红蛋白的每条组成β链上都含有一个高亲和力和一个低亲和力的铜离子结合位点。与低亲和力位点结合的铜与β血红素的选择性氧化有关。在本研究中，已在人血红蛋白中血红素铁的10埃范围内定位了一个铜离子低亲和力结合位点。有人提出，近端组氨酸参与该位点铜的结合，并参与血红素铁的氧化和铜离子的还原。
