Iron-sulfur clusters are among the most complex metal-containing prosthetic centers in biology. Most if not all of the proteins involved in the biosynthesis of "simple" Fe-S clusters have been identified. The structural and functional chemistry of these proteins has been the subject of intense research efforts, and many of the key details are now understood in structural and mechanistic detail. The fact that Fe-S cluster-binding proteins can be reconstituted in vitro with no accessory proteins provides an important indicator of the intracellular roles for many proteins on the Fe-S cluster assembly pathway. Indeed, such proteins are more correctly viewed as carrier proteins, rather than as catalysts for the reaction, that both avoid the toxicity associated with free iron and sulfide and allow delivery at lower intracellular concentrations of these species. The IscU (or ISU) family of proteins serves a key role as scaffolding proteins on which [2Fe-2S] building blocks are assembled prior to transfer to final apo target proteins. IscU in particular exhibits highly unusual conformational flexibility that appears critical to its function.

Iron-sulfur cluster biosynthesis: toward an understanding of cellular machinery and molecular mechanism / Mansy, Sheref Samir; J. A., Cowan. - In: ACCOUNTS OF CHEMICAL RESEARCH. - ISSN 0001-4842. - STAMPA. - 37:(2004), pp. 719-725. [10.1021/ar0301781]

Iron-sulfur cluster biosynthesis: toward an understanding of cellular machinery and molecular mechanism.

Mansy, Sheref Samir;
2004-01-01

Abstract

Iron-sulfur clusters are among the most complex metal-containing prosthetic centers in biology. Most if not all of the proteins involved in the biosynthesis of "simple" Fe-S clusters have been identified. The structural and functional chemistry of these proteins has been the subject of intense research efforts, and many of the key details are now understood in structural and mechanistic detail. The fact that Fe-S cluster-binding proteins can be reconstituted in vitro with no accessory proteins provides an important indicator of the intracellular roles for many proteins on the Fe-S cluster assembly pathway. Indeed, such proteins are more correctly viewed as carrier proteins, rather than as catalysts for the reaction, that both avoid the toxicity associated with free iron and sulfide and allow delivery at lower intracellular concentrations of these species. The IscU (or ISU) family of proteins serves a key role as scaffolding proteins on which [2Fe-2S] building blocks are assembled prior to transfer to final apo target proteins. IscU in particular exhibits highly unusual conformational flexibility that appears critical to its function.
2004
Mansy, Sheref Samir; J. A., Cowan
Iron-sulfur cluster biosynthesis: toward an understanding of cellular machinery and molecular mechanism / Mansy, Sheref Samir; J. A., Cowan. - In: ACCOUNTS OF CHEMICAL RESEARCH. - ISSN 0001-4842. - STAMPA. - 37:(2004), pp. 719-725. [10.1021/ar0301781]
File in questo prodotto:
Non ci sono file associati a questo prodotto.

I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione

Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11572/89318
 Attenzione

Attenzione! I dati visualizzati non sono stati sottoposti a validazione da parte dell'ateneo

Citazioni
  • ???jsp.display-item.citation.pmc??? 26
  • Scopus 88
  • ???jsp.display-item.citation.isi??? 82
social impact