Iron-sulfur proteins as initiators of radical chemistry

Marquet, Andrée and Bui, Bernadette Tse Sum and Smith, Alison G. and Warren, Martin J. (2007) Iron-sulfur proteins as initiators of radical chemistry. Natural Product Reports, 24 (2). pp. 1027-1040. ISSN 0265-0568 . (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided)

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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.

Item Type: Article
Additional information: Review Article
Subjects: Q Science > QD Chemistry
Q Science > QH Natural history > QH301 Biology
Divisions: Faculties > Science Technology and Medical Studies > School of Biosciences
Depositing User: Suzanne Duffy
Date Deposited: 31 Mar 2008 08:12
Last Modified: 02 May 2014 15:35
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