XRD1 Highlights
- XRD1 Highlights
- C1–C4 alcohol–cavitand complexes
- Cuprate Superconductor
- Jack Bean Urease
- XRD1 Sample Changer
- Carbonic Anhydrase
- PDI8CN2
- Human Legumain
- Structure of Human NAPE-PLD
- beta-Chitin in Squid Pen
- Enhanced Green Fluorescent Protein
- Multitarget drug design strategy
- Hydrogen-bonded Organic Pigments
- Selectivity of CNG channels
- Polycyclic Aromatic Hydrocarbons
- Cisplatin Encapsulation within the Ferritin Nanocage
- Crystal structure of the earthworm toxin
- Chemistry at the protein–mineral interface in L-ferritin
- Porous N-doped graphene
- Sliding of the human DNA clamp PCNA
- S1′ Pocket of Thermolysin
- microbial NLP cytolysins
- Human ubiquitin
- Photosynthesis
- Nanoparticles
- Anode Materials
- Stone Materials
- Sensor humidity
- Xe shell
- OSC
- Peptide nanotubes
- Amyloid aggregates
- Perovskites optimization
- Hydrocarbons
- CO2 separation
- Flexibility
- All Pages
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 |
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.
Retrieve Article
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. |
