X-ray structures of homopolymeric human L-ferritin and horse spleen ferritin were solved by freezing protein crystals at different time intervals after exposure to a ferric salt and revealed the growth of an octa-nuclear iron cluster on the inner surface of the protein cage with a key role played by some glutamate residues. An atomic resolution view of how the cluster formation develops starting from a (μ3-oxo)tris[(μ2-glutamato-κO:κO’)](glutamato-κO)(diaquo)triiron(III) seed is provided. The results support the idea that iron biomineralization in ferritin is a process initiating at the level of the protein surface, capable of contributing coordination bonds and electrostatic guidance.

Iron Biomineral Growth from the Initial Nucleation Seed in L-Ferritin / Ciambellotti S.; Pozzi C.; Mangani S.; Turano P.. - In: CHEMISTRY-A EUROPEAN JOURNAL. - ISSN 0947-6539. - ELETTRONICO. - (2020), pp. 0-0. [10.1002/chem.202000064]

Iron Biomineral Growth from the Initial Nucleation Seed in L-Ferritin

Ciambellotti S.;Turano P.
2020

Abstract

X-ray structures of homopolymeric human L-ferritin and horse spleen ferritin were solved by freezing protein crystals at different time intervals after exposure to a ferric salt and revealed the growth of an octa-nuclear iron cluster on the inner surface of the protein cage with a key role played by some glutamate residues. An atomic resolution view of how the cluster formation develops starting from a (μ3-oxo)tris[(μ2-glutamato-κO:κO’)](glutamato-κO)(diaquo)triiron(III) seed is provided. The results support the idea that iron biomineralization in ferritin is a process initiating at the level of the protein surface, capable of contributing coordination bonds and electrostatic guidance.
2020
0
0
Ciambellotti S.; Pozzi C.; Mangani S.; Turano P.
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Utilizza questo identificatore per citare o creare un link a questa risorsa: https://hdl.handle.net/2158/1189624
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