Brady M C, Lilley K S, Treffry A, Harrison P M, Hider R C, Taylor P D
Krebs Institute of Biomolecular Research, Department of Biochemistry, The University, Sheffield, United Kingdom.
J Inorg Biochem. 1989 Jan;35(1):9-22. doi: 10.1016/0162-0134(89)84002-4.
Ferritin molecules contain 24 subunits forming a shell around an inorganic iron-core. Release of iron(III) from ferritin and its isolated iron-cores by a series of hydroxypyridinone chelators with high affinities for iron(III) has been compared. The results collectively suggest that the chelators act by penetrating the protein shell and interacting directly with the iron-core in ferritin. Iron(III) is probably removed bound to a single ligand, but once outside the protein shell, the trihydroxypyridinone iron(III) complex predominates. The order of effectiveness of a group of pyridinones found for iron removal from ferritin molecules in solution differs from that obtained with hepatocytes in culture or with whole animals, where membrane solubility and other factors may modulate the response.
铁蛋白分子包含24个亚基，围绕着一个无机铁核心形成一个外壳。已经比较了一系列对铁（III）具有高亲和力的羟基吡啶酮螯合剂从铁蛋白及其分离出的铁核心中释放铁（III）的情况。总体结果表明，螯合剂通过穿透蛋白质外壳并直接与铁蛋白中的铁核心相互作用来发挥作用。铁（III）可能以与单个配体结合的形式被去除，但一旦离开蛋白质外壳，三羟基吡啶酮铁（III）络合物就占主导地位。在溶液中从铁蛋白分子中去除铁时发现的一组吡啶酮的有效性顺序与在培养的肝细胞或完整动物中获得的顺序不同，在这些情况下，膜溶解性和其他因素可能会调节反应。
