Iron-Sulfur Cluster Biosynthesis: Toward an Understanding of Cellular Machinery and Molecular Mechanism

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• 作者：Sheref S. Mansy and J. A. Cowan
• 刊名：Accounts of Chemical Research
• 出版年：2004
• 出版时间：September 2004
• 年：2004
• 卷：37
• 期：9
• 页码：719 - 725
• 全文大小：221K
• 年卷期：v.37,no.9(September 2004)
• ISSN：1520-4898

文摘

Iron-sulfur clusters are among the most complex metal-containingprosthetic centers in biology. Most if not all of the proteins involvedin the biosynthesis of "simple" Fe-S clusters have been identified.The structural and functional chemistry of these proteins has beenthe subject of intense research efforts, and many of the key detailsare now understood in structural and mechanistic detail. The factthat Fe-S cluster-binding proteins can be reconstituted in vitrowith no accessory proteins provides an important indicator of theintracellular roles for many proteins on the Fe-S cluster assemblypathway. Indeed, such proteins are more correctly viewed as carrierproteins, rather than as catalysts for the reaction, that both avoidthe toxicity associated with free iron and sulfide and allow deliveryat lower intracellular concentrations of these species. The IscU (orISU) family of proteins serves a key role as scaffolding proteins onwhich [2Fe-2S] building blocks are assembled prior to transfer tofinal apo target proteins. IscU in particular exhibits highly unusualconformational flexibility that appears critical to its function.