Radical SAM enzymes in methylation and methylthiolation

Radical SAM enzymes in methylation and methylthiolation

Broderick et al., Metallomics, 2012, Advance Article

This minireview article is from Rachel U. Hutchenson and Joan B. Broderick from the Department of Chemistry and Biochemistry and the Astrobiology Biogeocatalysis Research Center, Montana State University. Professor Joan B. Broderick’s  research interests include mechanistic bioinorganic chemistry, with a particular focus on enzymes utilizing iron–sulfur clusters to catalyze radical reactions. Radical S-adenosyl-L-methionine (SAM) enzymes are a large and diverse superfamily with functions ranging from enzyme activation through a single H atom abstraction to complex organic and metal cofactor synthesis involving a series of steps. Although functionally very diverse, this superfamily of enzymes share common structural and mechanistic characteristics. All of them contain a site-differentiated [4Fe–4S] cluster, ligated by a CX3CX2C or similar motif, which binds SAM at the unique iron. This review presents recent highlights in the understanding of radical SAM enzymes with a particular emphasis on enzymes catalyzing methylation and methythiolation reactions. This review will be free to read until Nov 7th.

Radical SAM enzymes in methylation and methylthiolation
Rachel U. Hutcheson and Joan B. Broderick
Metallomics, 2012, Advance Article
DOI: 10.1039/C2MT20136D

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