Iron-sulfur proteins as initiators of radical chemistry

被引:29
作者
Marquet, Andree
Bui, Bernadette Tse Sum
Smith, Alison G.
Warren, Martin J.
机构
[1] Univ Paris 06, CNRS, UMR 7613, F-75005 Paris, France
[2] Univ Cambridge, Dept Plant Sci, Cambridge CB2 3EA, England
[3] Univ Kent, Dept Biosci, Canterbury CT2 7NJ, Kent, England
基金
英国生物技术与生命科学研究理事会;
关键词
COLI BIOTIN SYNTHASE; PYRUVATE FORMATE-LYASE; METHYLERYTHRITOL PHOSPHATE-PATHWAY; SPORE-PHOTOPRODUCT-LYASE; CLUSTER BINDING-SITES; ESCHERICHIA-COLI; S-ADENOSYLMETHIONINE; CRYSTAL-STRUCTURE; LIPOYL SYNTHASE; ISOPRENOID BIOSYNTHESIS;
D O I
10.1039/b703109m
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:1027 / 1040
页数:14
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