Synthetic Models for Iron–Oxygen Aggregation and Biomineralization
Synthetic Models for Iron–Oxygen Aggregation and Biomineralization
复制标题
铁氧聚集和生物矿化的合成模型
DOI：
10.1002/anie.199210101
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发表时间：
1992
影响因子：
--
通讯作者：
K. Hagen
中科院分区：
文献类型：
--
作者：
K. Hagen
Iron, the most abundant transition element in the earth’s crust, plays a major role in biological systems primarily because of its rich redox chemistry, and to a lesser extent the structural and magnetic properties of its various mineral forms. A streamlined biological apparatus for handling free iron is imperative, since free Fe (r1) ions will react with dioxygen to form highly reactive and destructive radicals, whereas uncomplexed Fe (rir) ions form insoluble iron hydroxide under physiological conditions. The iron-storage protein ferritin, made up of 24 subunits forming a shell approximately 70 8, in diameter which can contain up to 4500 iron atoms, is primarily responsible for solubilization and storage of excess Fe (In).[’l The structure of the hydroxo (oxo) iron core of ferritin is not well-defined and is variable in composition. The best information is obtained under low phosphate concentrations for which considerable long-range order, resembling that of the mineral ferrihydrite, is detected by X-ray diffraction and electron microscopy. The variable phosphate component in the core is thought not to play a dominant structural role, although phosphate may play a significant role in binding to isolated iron ions, small aggregates, or the surface of large crystallites.Iron oxides have a rich mineral chemistry, and more than twenty years ago stable, soluble nanoparticles averaging 70 A in diameter were prepared by hydrolytic polymerization of iron (iiI).[2] Yet the chemistry of molecular iron-oxygen clusters has been dominated by the fundamental oxobridged diiron (n1) unitc3’and the trinuclear basic iron carboxylates. The crystal structure determination in 198 1 of a binuclear iron-oxygen species in hemerythrin and the discovery of related 0x0-bridged bimetallic centers in other proteins has revived the study of iron-oxygen chemistry. An
