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Ferroxidase Activity in Eukaryotic Ferritin is Controlled by Accessory‐Iron‐Binding Sites in the Catalytic Cavity
Author(s) -
Bernacchioni Caterina,
Pozzi Cecilia,
Di Pisa Flavio,
Mangani Stefano,
Turano Paola
Publication year - 2016
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201602842
Subject(s) - ceruloplasmin , ferritin , catalysis , chemistry , nanocages , residue (chemistry) , metalloprotein , crystallography , stereochemistry , biochemistry , enzyme
Ferritins are iron‐storage nanocage proteins that catalyze the oxidation of Fe 2+ to Fe 3+ 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 Fe 2+ substrate to the diferric ferroxidase sites with the same coordination geometries as in the wild‐type cages.