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Chemistry at the protein–mineral interface in L-ferritin assists the assembly of a functional (μ³-oxo)Tris[(μ²-peroxo)] triiron(III) cluster

After 60 min exposure to a ferrous solution, a fully assembled (μ3-oxo)Tris[(μ2-peroxo)(μ2-glutamato-κO:κO′)](glutamato-κO)(diaquo)triiron(III) anionic cluster appears in human L-ferritin.

Pozzi C. et al., Proceedings of the National Academy of Sciences 2017

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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, authors 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.
 

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Chemistry at the protein–mineral interface in L-ferritin assists the assembly of a functional (μ3-oxo)Tris[(μ2-peroxo)] triiron(III) cluster; Pozzi C., Ciambellotti S., Bernacchioni C., Di Pisa F., Mangani S., and Turano P.
Proceedings of the National Academy of Sciences 2017
doi: 10.1073/pnas.1614302114

Last Updated on Wednesday, 08 March 2017 17:14