Reversible Alkyl-Group Migration between Iron and Sulfur in [Fe<sub>4</sub>S<sub>4</sub>] Clusters
Mengshan Ye, Alexandra C. Brown, Daniel L. M. Suess
Abstract
Synthetic [Fe4S4] clusters with Fe–R groups (R = alkyl/benzyl) are shown to release organic radicals on an [Fe4S4]3+–R/[Fe4S4]2+ redox couple, the same that has been proposed for a radical-generating intermediate in the superfamily of radical S-adenosyl-l-methionine (SAM) enzymes. In attempts to trap the immediate precursor to radical generation, a species in which the alkyl group has migrated from Fe to S is instead isolated. This S-alkylated cluster is a structurally faithful model of intermediates proposed in a variety of functionally diverse S transferase enzymes and features an “[Fe4S4]+-like” core that exists as a physical mixture of S = 1/2 and 7/2 states. The latter corresponds to an unusual, valence-localized electronic structure as indicated by distortions in its geometric structure and supported by computational analysis. Fe-to-S alkyl group migration is (electro)chemically reversible, and the preference for Fe vs S alkylation is dictated by the redox state of the cluster. These findings link the organoiron and organosulfur chemistry of Fe–S clusters and are discussed in the context of metalloenzymes that are proposed to make and break Fe–S and/or C–S bonds during catalysis.