Ferroxidase-Mediated Iron Oxide Biomineralization: Novel Pathways to Multifunctional Nanoparticles

Kornelius Zeth, Egbert Hoiczyk, Mitsuhiro Okuda

Research output: Contribution to journalReview articlepeer-review

32 Scopus citations


Iron oxide biomineralization occurs in all living organisms and typically involves protein compartments ranging from 5 to 100 nm in size. The smallest iron-oxo particles are formed inside dodecameric Dps protein cages, while the structurally related ferritin compartments consist of twice as many identical protein subunits. The largest known compartments are encapsulins, icosahedra made of up to 180 protein subunits that harbor additional ferritin-like proteins in their interior. The formation of iron-oxo particles in all these compartments requires a series of steps including recruitment of iron, translocation, oxidation, nucleation, and storage, that are mediated by ferroxidase centers. Thus, compartmentalized iron oxide biomineralization yields uniform nanoparticles strictly determined by the sizes of the compartments, allowing customization for highly diverse nanotechnological applications.

Original languageEnglish (US)
Pages (from-to)190-203
Number of pages14
JournalTrends in biochemical sciences
Issue number2
StatePublished - Feb 1 2016


  • Biomineralization
  • Dps
  • Encapsulin
  • Ferritin
  • Nanobiotechnology

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology


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