Iron Biomineral Growth from the Initial Nucleation Seed in L-Ferritin
| Autor: | Silvia Ciambellotti, Paola Turano, Stefano Mangani, Cecilia Pozzi |
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| Rok vydání: | 2020 |
| Předmět: |
Tris
nucleation site Iron Nucleation Salt (chemistry) 010402 general chemistry 01 natural sciences Catalysis 03 medical and health sciences chemistry.chemical_compound medicine Animals Humans Horses 030304 developmental biology Biological Phenomena chemistry.chemical_classification 0303 health sciences biology 010405 organic chemistry Chemistry Organic Chemistry L-ferritin metallocluster General Chemistry biomineralization L-Ferritin X-ray diffraction 0104 chemical sciences Ferritin Crystallography X-ray crystallography Apoferritins Ferritins biology.protein Ferric Protein crystallization medicine.drug Biomineralization |
| Zdroj: | Chemistry (Weinheim an der Bergstrasse, Germany). 26(26) |
| ISSN: | 1521-3765 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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