Marquet, A. and Bui, B.T.S. and Smith, A.G. and Warren, M.J. (2007) Iron-sulfur proteins as initiators of radical chemistry. Natural Product Reports, 24 (2). pp. 1027-1040. ISSN 0265-0568 .
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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.
|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:||14 Jan 2010 14:08|
|Resource URI:||http://kar.kent.ac.uk/id/eprint/2594 (The current URI for this page, for reference purposes)|
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