Conspectus Ferritins reversibly synthesize iron-oxy (ferrihydrite) biominerals inside large,
hollow protein nanocages (10–12 nm,∼ 480 000 g/mol); the iron biominerals are metabolic …

Ferritin is a self-assembled 24-mer protein cage which is naturally designed for iron storage.
Other than iron, the apo-ferritin cage template can accommodate various non-natural metal …

Maxi-ferritins are ubiquitous iron-storage proteins with a common cage architecture made up
of 24 identical subunits of five α-helices that drive iron biomineralization through catalytic …

Ferritin molecular cages are marvelous 24-mer supramolecular architectures that enable
massive iron storage (> 2000 iron atoms) within their inner cavity. This cavity is connected to …

Ferritin protein is involved in biological tissues in the storage and management of iron-an
essential micro-nutrient in the majority of living systems. While there are extensive studies …

Twenty four-mer ferritins are present in all kingdoms of life and play an essential role as iron
storage proteins. The formation of a caged iron biomineral is driven by an enzymatic …

Ferritin, a multimeric cage-like enzyme, is integral to iron metabolism across all phyla
through the sequestration and storage of iron through efficient ferroxidase activity. While …

Preparation of modified and hybrid ferritin provides a great opportunity to understand the
mechanisms of iron loading/unloading, protein self-assembly, size constrained nanomaterial …

Ferritins are multimers comprised of 4 α-helical bundle monomers that co-assemble to form
protein shells surrounding an approximately spherical internal cavity. The assembled …

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 …