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Issue 5, 2007
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Iron–sulfur proteins as initiators of radical chemistry

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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

21 Jun 2007
First published
11 Sep 2007

Nat. Prod. Rep., 2007,24, 1027-1040
Article type
Review Article

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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