Structural highlights
Function
FRI2_LITCT Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Has ferroxidase activity. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation.
Publication Abstract from PubMed
Ferritins are iron-storage nanocage proteins that catalyze the oxidation of Fe2+ to Fe3+ at ferroxidase sites. By a combination of structural and spectroscopic techniques, Asp140, together with previously identified Glu57 and Glu136, is demonstrated to be an essential residue to promote the iron oxidation at the ferroxidase site. However, the presence of these three carboxylate moieties in close proximity to the catalytic centers is not essential to achieve binding of the Fe2+ substrate to the diferric ferroxidase sites with the same coordination geometries as in the wild-type cages.
Ferroxidase Activity in Eukaryotic Ferritin is Controlled by Accessory-Iron-Binding Sites in the Catalytic Cavity.,Bernacchioni C, Pozzi C, Di Pisa F, Mangani S, Turano P Chemistry. 2016 Sep 21. doi: 10.1002/chem.201602842. PMID:27650996[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Bernacchioni C, Pozzi C, Di Pisa F, Mangani S, Turano P. Ferroxidase Activity in Eukaryotic Ferritin is Controlled by Accessory-Iron-Binding Sites in the Catalytic Cavity. Chemistry. 2016 Sep 21. doi: 10.1002/chem.201602842. PMID:27650996 doi:http://dx.doi.org/10.1002/chem.201602842
