Mammalian iron–sulphur proteins: novel insights into biogenesis and function
Mammalian iron–sulphur proteins: novel insights into biogenesis and function
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DOI：
10.1038/nrm3909
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发表时间：
2014-11
影响因子：
112.7
通讯作者：
T. Rouault
中科院分区：
文献类型：
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作者：
T. Rouault
铁硫（Fe-S）簇是无机辅因子，几乎存在于所有物种中，由铁和硫原子的各种组合组成。Fe-S团簇可以接受或贡献单电子，进行氧化还原反应，促进电子传输。这些复杂的模块化结构如何组装并连接到哺乳动物细胞的线粒体、核和胞质区室中的细胞蛋白的许多细节仍然不清楚。最近的证据表明，在一些Fe-S受体蛋白中发现的Leu-Tyr-Arg（LYR）三肽基序可以促进Fe-S簇从支架到客户蛋白的直接和屏蔽转移。Fe-S簇可能是许多已知蛋白质的未识别和难以捉摸的辅因子。
Iron–sulphur (Fe–S) clusters are inorganic cofactors that are found in nearly all species and are composed of various combinations of iron and sulphur atoms. Fe–S clusters can accept or donate single electrons to carry out oxidation and reduction reactions and to facilitate electron transport. Many details of how these complex modular structures are assembled and ligated to cellular proteins in the mitochondrial, nuclear and cytosolic compartments of mammalian cells remain unclear. Recent evidence indicates that a Leu-Tyr-Arg (LYR) tripeptide motif found in some Fe–S recipient proteins may facilitate the direct and shielded transfer of Fe–S clusters from a scaffold to client proteins. Fe–S clusters are probably an unrecognized and elusive cofactor of many known proteins.