{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Ye M"],"funding":["Hertz Foundation","National Institute of General Medical Sciences","NIGMS NIH HHS","Division of Graduate Education"],"pagination":["13184-13195"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9526375"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["144(29)"],"pubmed_abstract":["Synthetic [Fe<sub>4</sub>S<sub>4</sub>] clusters with Fe-R groups (R = alkyl/benzyl) are shown to release organic radicals on an [Fe<sub>4</sub>S<sub>4</sub>]<sup>3+</sup>-R/[Fe<sub>4</sub>S<sub>4</sub>]<sup>2+</sup> redox couple, the same that has been proposed for a radical-generating intermediate in the superfamily of radical <i>S</i>-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 \"[Fe<sub>4</sub>S<sub>4</sub>]<sup>+</sup>-like\" core that exists as a physical mixture of <i>S</i> = 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 <i>vs</i> 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."],"journal":["Journal of the American Chemical Society"],"pubmed_title":["Reversible Alkyl-Group Migration between Iron and Sulfur in [Fe<sub>4</sub>S<sub>4</sub>] Clusters."],"pmcid":["PMC9526375"],"funding_grant_id":["1122374","R01 GM136882","R01GM136882"],"pubmed_authors":["Ye M","Brown AC","Suess DLM"],"additional_accession":[]},"is_claimable":false,"name":"Reversible Alkyl-Group Migration between Iron and Sulfur in [Fe<sub>4</sub>S<sub>4</sub>] Clusters.","description":"Synthetic [Fe<sub>4</sub>S<sub>4</sub>] clusters with Fe-R groups (R = alkyl/benzyl) are shown to release organic radicals on an [Fe<sub>4</sub>S<sub>4</sub>]<sup>3+</sup>-R/[Fe<sub>4</sub>S<sub>4</sub>]<sup>2+</sup> redox couple, the same that has been proposed for a radical-generating intermediate in the superfamily of radical <i>S</i>-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 \"[Fe<sub>4</sub>S<sub>4</sub>]<sup>+</sup>-like\" core that exists as a physical mixture of <i>S</i> = 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 <i>vs</i> 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.","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Jul","modification":"2025-04-22T03:33:32.345Z","creation":"2025-02-19T00:23:50.038Z"},"accession":"S-EPMC9526375","cross_references":{"pubmed":["35830717"],"doi":["10.1021/jacs.2c03195"]}}