Issue 5, 2007
From the journal:

Natural Product Reports

Iron–sulfur proteins as initiators of radical chemistry†

Andrée Marquet,*a   Bernadette Tse Sum Bui,a   Alison G. Smithb  and  Martin J. Warrenc  

* Corresponding authors

a Université Pierre et Marie Curie–Paris 6, CNRS UMR 7613, (Synthèse, Structure et Fonction de Molécules Bioactives), FR2769, Case courrier 182, 4 place Jussieu, Paris, France
E-mail: marquet@ccr.jussieu.fr

b Department of Plant Sciences, University of Cambridge, Downing Street, Cambridge, UK

c Department of Biosciences, University of Kent, Canterbury, Kent, UK

Abstract

Covering: January 1995 to August 2007

Iron–sulfur proteins are very versatile biological entities for which many new functions are continuously being unravelled. This review focus on their role in the initiation of radical chemistry, with special emphasis on ‘radical-SAM’ enzymes, since several members of the family catalyse key steps in the biosynthetic pathways of cofactors such as biotin, lipoate, thiamine, heme and the molybdenum cofactor. It will also include other examples to show the chemical logic which is emerging from the presently available data on this family of enzymes. The common step in all the (quite different) reactions described here is the monoelectronic reductive cleavage of SAM by a reduced [4Fe–4S]1+ cluster, producing methionine and a highly oxidising deoxyadenosyl radical, which can initiate chemically difficult reactions. This set of enzymes, which represent a means to perform oxidation under reductive conditions, are often present in anaerobic organisms. Some other, non-SAM-dependent, radical reactions obeying the same chemical logic are also covered.

Graphical abstract: Iron–sulfur proteins as initiators of radical chemistry

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Article information

DOI
https://doi.org/10.1039/B703109M
Article type
Review Article
Submitted
21 Jun 2007
First published
11 Sep 2007

Nat. Prod. Rep., 2007,24, 1027-1040

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Iron–sulfur proteins as initiators of radical chemistry

A. Marquet, B. Tse Sum Bui, A. G. Smith and M. J. Warren, Nat. Prod. Rep., 2007, 24, 1027 DOI: 10.1039/B703109M

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