Ferritins: Dynamic management of biological iron and oxygen chemistry

被引:435
作者
Liu, XF [1 ]
Theil, EC [1 ]
机构
[1] Childrens Hosp, Oakland Res Inst, Ctr BioIron, Oakland, CA 94609 USA
关键词
D O I
10.1021/ar0302336
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
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, channelm and catalytic functions in compact protein structures required for life and disease response.
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收藏
页码:167 / 175
页数:9
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