The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.
Ferritins: Dynamic Management of Biological Iron and Oxygen Chemistry
Abstract
Ferritins are spherical, cage-like proteins with nanocavities formed by multiple polypeptide subunits (four-helix bundles) that manage iron/oxygen chemistry. Catalytic coupling yields diferric oxo/hydroxo complexes at ferroxidase sites in maxi-ferritin subunits (24 subunits, 480 kDa; plants, animals, microorganisms). Oxidation occurs at the cavity surface of mini-ferritins/Dps proteins (12 subunits, 240 kDa; bacteria). Oxidation products are concentrated as minerals in the nanocavity for iron-protein cofactor synthesis (maxi-ferritins) or DNA protection (mini-ferritins). The protein cage and nanocavity characterize all ferritins, although amino acid sequences diverge, especially in bacteria. Catalytic oxidation/di-iron coupling in the protein cage (maxi-ferritins, 480 kDa; plants, bacteria and animal cell-specific isoforms) or on the cavity surface (mini-ferritins/Dps proteins, 280 kDa; bacteria) initiates mineralization. Gated pores (eight or four), symmetrically arranged, control iron flow. The multiple ferritin functions combine pore, channel, and catalytic functions in compact protein structures required for life and disease response.
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Metadata
- Authors
- Liu, X., & Theil, E. C.
- Venue
- Accounts of Chemical Research
- Publisher
- American Chemical Society (ACS)
- Published
- 2005-01-29
- Volume
- 38
- Issue
- 3
- Pages
- 167-175
- ISSN
- 0001-4842 (ISSN-L)
- 1520-4898
- OpenAlex
- W2106699885
- Cited by
- 514
- References
- 9
- FWCI
- 14.83
- Type
- journal article
- Language
- en
- Open access
- closed
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