Iron storage within the protein shell of ferritin is a venerable area of bioinorganic chemistry. The exact structural nature of the iron(III) oxide hydroxide core therein, however, is poorly defined. Here we present a polynuclear iron(III) complex supported by polyoxometalate ligands. These inorganic scaffolds inhibit nonspecific iron hydrolysis and prevent the formation of insoluble aggregates, a function similar to that of the ferritin protein shell. The complex also features a number of characteristics that closely resemble the ferritin core: (1) It is water-soluble. (2) It contains compact layers of iron(III) oxide hydroxides. (3) The iron core of the model complex includes unusual, 4-coordinate iron centers. The ferritin core itself, suggested by EXAFS data, is a 1/3�2/3 mix of tetrahedral and octahedral iron sites. (4) The core structure features bridging phosphate groups, which are also present in the natural systems.

Polyoxometalate-supported polyiron complex that mimics the mineralization in ferritin

247th National Meeting (2014)

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