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英国化学家通过在天然蛋白质的空心中引入磁铁矿(Fe_3O_4)晶核,合成了一种新奇的磁性蛋白质。这种空心的蛋白质宿主是从许多生物体用来储存铁的铁—蛋白质的化合物—铁蛋白中得到的。通常铁是以6nm的水合铁氧化物(5Fe_2O_3·9H_2O)的晶体形式储存的,水合铁氧化物又是由天然铁蛋白经渗析除去空心的多肽壳得到的。这种空心多肽壳也就是人们常说的脱铁铁蛋白,它与Fe(Ⅱ)溶液在氧化条件下反应,便可形成铁磁性的矿物—磁铁矿。
British chemists synthesized a novel magnetic protein by introducing magnetite (Fe_3O_4) nuclei into the hollow of a natural protein. This hollow protein host is derived from ferritin, the iron-protein complex used by many organisms to store iron. Iron is typically stored as a 6 nm crystalline form of hydrated iron oxide (5Fe_2O_3 · 9H_2O), which in turn is obtained by diaphoresis of native ferritin to remove the hollow polypeptide shell. This hollow polypeptide shell, also known as apoferritin, reacts with Fe (II) solution under oxidizing conditions to form a ferromagnetic mineral, magnetite.