Iron-sulfur clusters: Nature's modular, multipurpose structures
Iron-sulfur clusters: Nature's modular, multipurpose structures
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DOI：
10.1126/science.277.5326.653
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发表时间：
1997-08-01
期刊：
影响因子：
56.9
通讯作者：
Munck, E
中科院分区：
文献类型：
--
作者：
Beinert, H;Holm, RH;Munck, E
铁硫蛋白存在于所有生命形式中。最常见的是，它们含有Fe2S2，Fe3S4和Fe4S4簇。这些模块簇经历氧化还原反应，可以插入蛋白质或从蛋白质中移除，可以通过优先侧链连接影响蛋白质结构，并且可以相互转化。除了电子传递功能外，铁硫簇合物还充当铁和氧的催化中心和传感器。它们最常见的氧化态是顺磁性的，这对理解混合价体系的磁性提出了重大挑战。铁硫簇现在与血红素和黄素等生物辅基在普遍存在和功能的多样性。
Iron-sulfur proteins are found in all life forms. Most frequently, they contain Fe2S2, Fe3S4, and Fe4S4 clusters. These modular clusters undergo oxidation-reduction reactions, may be inserted or removed from proteins, can influence protein structure by preferential side chain ligation, and can be interconverted. In addition to their electron transfer function, iron-sulfur clusters act as catalytic centers and sensors of iron and oxygen. Their most common oxidation states are paramagnetic and present significant challenges for understanding the magnetic properties of mixed valence systems. Iron-sulfur clusters now rank with such biological prosthetic groups as hemes and flavins in pervasive occurrence and multiplicity of function.