Maxi- and mini-ferritins: minerals and protein nanocages.
Maxi- and mini-ferritins: minerals and protein nanocages.
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DOI：
10.1007/978-3-642-21230-7_2
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发表时间：
2011
影响因子：
--
通讯作者：
Theil, Elizabeth C
中科院分区：
文献类型：
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作者：
Bevers, Loes E;Theil, Elizabeth C
铁蛋白合成氧化铁生物矿物质，是所有生命的核心，用于浓缩铁和保护免受亚铁和氧化剂化学的氧化应激。从铁蛋白（24个亚基±血红素）和铁蛋白（Dps）（12个亚基）的广泛生物分布、铁/氧催化位点的保守性、矿物质的形成（步骤i. Fe（II）进入和结合，步骤ii. O2或H2 O2结合和过渡中间体的形成，步骤iii.从活性位点释放不同的含氧矿物前体，步骤iv.成核和矿化）性质的矿物，和蛋白质控制矿物溶解和释放的Fe（II）。铁蛋白蛋白笼中的孔隙控制铁进入矿化和矿物质溶解后铁退出。磷酸盐或存在催化失活亚基（动物L亚基）和铁蛋白铁矿物质紊乱之间的关系是基于新的信息铁蛋白蛋白笼结构的贡献，在蛋白笼亚基通道，出口足够接近的其他亚基和退出矿物核，以促进散装矿物形成的成核。如何以及在哪里质子移入和移出的蛋白质在矿物质的合成和溶解，如何铁蛋白笼组装与12或24个亚基编码的铁蛋白氨基酸序列的差异很大，以及什么是蛋白质的作用，在合成的散装矿物质都被描述为问题，需要新的方法在未来的铁蛋白生物矿物的调查。
Ferritins synthesize ferric oxide biominerals and are central to all life for concentrating iron and protection against oxidative stress from the ferrous and oxidant chemistry. The ferritin protein nanocages and biomineral synthesis are discussed in terms of wide biological distribution of the maxi-ferritins (24 subunit ± heme) and mini-ferritins (Dps) (12 subunit), conservations of the iron/oxygen catalytic sites in the protein cages, mineral formation (step i. Fe(II) entry and binding, step ii. O2 or H2O2 binding and formation of transition intermediates, step iii. release of differric oxo mineral precursors from active sites, step iv. nucleation and mineralization) properties of the minerals, and protein control of mineral dissolution and release of Fe(II). Pores in ferritin protein cages control iron entry for mineralization and iron exit after mineral dissolution. The relationship between phosphate or the presence of catalytically inactive subunits (animal L subunits) and ferritin iron mineral disorder is developed based on new information about contributions of ferritin protein cage structure to nucleation in protein cage subunit channels that exit close enough to those of other subunits and exiting mineral nuclei to facilitate bulk mineral formation. How and where protons move in and out of the protein during mineral synthesis and dissolution, how ferritin cage assembly with 12 or 24 subunits is encoded in the widely divergent ferritin amino acid sequences, and what is the role of the protein in synthesis of the bulk mineral are all described as problems requiring new approaches in future investigations of ferritin biominerals.