Hempstead P D, Hudson A J, Artymiuk P J, Andrews S C, Banfield M J, Guest J R, Harrison P M
Krebs Institute, Department of Molecular Biology and Biotechnology, University of Sheffield, UK.
FEBS Lett. 1994 Aug 22;350(2-3):258-62. doi: 10.1016/0014-5793(94)00781-0.
X-Ray analysis of the ferritin of Escherichia coli (Ec-FTN) and of Ec-FTN crystals soaked in (NH4)2Fe(SO4)2 has revealed the presence of three iron-binding sites per subunit. Two of these form a di-iron site in the centre of the subunit as has been proposed for the 'ferroxidase centres' of human ferritin H chains. This di-iron site, lying within the 4-alpha-helix bundle, resemble those of ribonucleotide reductase, methane monoxygenase and haemerythrin. The third iron is bound by ligands unique to Ec-FTN on the inner surface of the protein shell. It is speculated that this state may represent the nucleation centre of a novel type of Fe(III) cluster, recently observed in Ec-FTN.
对大肠杆菌铁蛋白（Ec-FTN）以及浸泡在硫酸亚铁铵中的Ec-FTN晶体进行的X射线分析表明，每个亚基存在三个铁结合位点。其中两个在亚基中心形成一个双铁位点，正如人类铁蛋白H链的“铁氧化酶中心”所提出的那样。这个位于4-α-螺旋束内的双铁位点类似于核糖核苷酸还原酶、甲烷单加氧酶和蚯蚓血红蛋白的双铁位点。第三个铁由蛋白质外壳内表面Ec-FTN特有的配体结合。据推测，这种状态可能代表了最近在Ec-FTN中观察到的一种新型Fe(III)簇的成核中心。
