Auxiliary iron-sulfur cofactors in radical SAM enzymes

作者：Lanz Nicholas D; Booker Squire J^*

来源：Biochimica et Biophysica Acta-Molecular Cell Research, 2015, 1853(6): 1316-1334.

DOI：10.1016/j.bbamcr.2015.01.002

• Radical SAM
• Iron-sulfur cluster
• S-adenosylmethionine
• Cofactor maturation
• Radical-dependent post-translational modification
• SPASM/twitch domain

A vast number of enzymes are now known to belong to a superfamily known as radical SAM, which all contain a [4Fe-4S] cluster ligated by three cysteine residues. The remaining, unligated, iron ion of the cluster binds in contact with the alpha-amino and alpha-carboxylate groups of S-adenosyl-L-methionine (SAM). This binding mode facilitates inner-sphere electron transfer from the reduced form of the cluster into the sulfur atom of SAM, resulting in a reductive cleavage of SAM to methionine and a 5'-deoxyadenosyl radical. The 5'-deoxyadenosyl radical then abstracts a target substrate hydrogen atom, initiating a wide variety of radical-based transformations. A subset of radical SAM enzymes contains one or more additional iron-sulfur clusters that are required for the reactions they catalyze. However, outside of a subset of sulfur insertion reactions, very little is known about the roles of these additional clusters. This review will highlight the most recent advances in the identification and characterization of radical SAM enzymes that harbor auxiliary iron-sulfur clusters. This article is part of a Special Issue entitled: Fe/S proteins: Analysis, structure, function, biogenesis and diseases.

• 出版日期2015-6