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- W2589084966 abstract "Significance Iron is an essential element in biology but has limited bioavailability. Ferritins are 24-mer iron-storage nanocage proteins that concentrate iron in their inner compartment as a bioavailable iron oxide biomineral. In L-type subunits, abundant in ferritins from organs involved in long-term iron storage, the biomineralization has been proposed to proceed through nucleation events involving iron(II) oxidation at the inner cage surface. Here, we demonstrate the nature and structural features of these nucleation sites. Structures captured during iron uptake show that the formation of the iron biomineral proceeds via the assembly of a tri-nuclear iron cluster, anchored to the protein through glutamic acid side chains, and involving oxo and peroxo ligands that are produced during the iron(II) oxidation by dioxygen." @default.
- W2589084966 created "2017-02-24" @default.
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- W2589084966 date "2017-02-15" @default.
- W2589084966 modified "2023-10-13" @default.
- W2589084966 title "Chemistry at the protein–mineral interface in L-ferritin assists the assembly of a functional (μ <sup>3</sup> -oxo)Tris[(μ <sup>2</sup> -peroxo)] triiron(III) cluster" @default.
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- W2589084966 doi "https://doi.org/10.1073/pnas.1614302114" @default.
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