Iron-sulfur cluster biosynthesis.
Iron-sulfur cluster biosynthesis.
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DOI：
10.1042/bst0361112
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发表时间：
2008-12
影响因子：
3.9
通讯作者：
Johnson MK
中科院分区：
文献类型：
--
作者：
Bandyopadhyay S;Chandramouli K;Johnson MK
铁硫簇存在于 200 多种不同类型的酶或蛋白质中，构成最古老、最普遍且结构多样的生物修复基团之一。因此，铁硫生物合成过程对于几乎所有生命形式都是必需的，并且在原核和真核生物中非常保守。细菌中已经建立了三种不同类型的铁硫簇组装机制，称为 NIF、ISC 和 SUF 系统，每种情况的总体机制都涉及半胱氨酸脱硫酶介导的支架蛋白上瞬时簇的组装以及随后将预先形成的簇转移到载脂蛋白上。现在，通过体内和体外方法的结合，人们开始在分子水平上理解铁硫簇组装和转移的复杂过程。本文重点介绍了铁硫簇组装和转移机制的最新进展，涉及普遍存在的 U 型支架蛋白，以及 Nfu 蛋白和单硫醇谷氧还蛋白等辅助蛋白在铁硫簇组装、储存或转移中的潜在作用。
Iron-sulphur clusters are present in more than 200 different types of enzymes or proteins and constitute one of the most ancient, ubiquitous and structurally diverse classes of biological prosthetic groups. Hence the process of iron-sulphur biosynthesis is essential to almost all forms of life and is remarkably conserved in prokaryotic and eukaryotic organisms. Three distinct types of iron-sulphur cluster assembly machinery have been established in bacteria, termed the NIF, ISC and SUF systems, and in each case the overall mechanism involves cysteine desulphurase-mediated assembly of transient clusters on scaffold proteins and subsequent transfer of preformed clusters to apo proteins. A molecular level understanding of the complex processes of iron-sulphur cluster assembly and transfer is now beginning to emerge from the combination of in vivo and in vitro approaches. This review highlights recent developments in understanding the mechanism of iron-sulphur cluster assembly and transfer involving the ubiquitous U-type scaffold proteins and the potential roles of accessory proteins such as Nfu proteins and monothiol glutaredoxins in the assembly, storage or transfer of iron-sulphur clusters.