{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Pandey A"],"funding":["American Heart Association","NIDDK NIH HHS","NIA NIH HHS","National Institutes of Health","NIGMS NIH HHS"],"pagination":["539-49"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3462219"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["12(5)"],"pubmed_abstract":["Cysteine desulfurases generate a covalent persulfide intermediate from cysteine, and this activated form of sulfur is essential for the synthesis of iron-sulfur (Fe-S) clusters. In yeast mitochondria, there is a complete machinery for Fe-S cluster synthesis, including a cysteine desulfurase, Nfs1p. Here we show that following supplementation of isolated mitochondria with [(35)S]cysteine, a radiolabeled persulfide could be detected on Nfs1p. The persulfide persisted under conditions that did not permit Fe-S cluster formation, such as nucleotide and/or iron depletion of mitochondria. By contrast, under permissive conditions, the radiolabeled Nfs1p persulfide was greatly reduced and radiolabeled aconitase was formed, indicating transfer of persulfide to downstream Fe-S cluster recipients. Nfs"],"journal":["Mitochondrion"],"pubmed_title":["Identification of a Nfs1p-bound persulfide intermediate in Fe-S cluster synthesis by intact mitochondria."],"pmcid":["PMC3462219"],"funding_grant_id":["R37 DK053953","R37DK053953","R01 GM087965","GM087965","09GRNT2260364","AG030504","R01 AG030504"],"pubmed_authors":["Pain D","Yoon H","Dancis A","Pandey A","Lyver ER"],"additional_accession":[]},"is_claimable":false,"name":"Identification of a Nfs1p-bound persulfide intermediate in Fe-S cluster synthesis by intact mitochondria.","description":"Cysteine desulfurases generate a covalent persulfide intermediate from cysteine, and this activated form of sulfur is essential for the synthesis of iron-sulfur (Fe-S) clusters. In yeast mitochondria, there is a complete machinery for Fe-S cluster synthesis, including a cysteine desulfurase, Nfs1p. Here we show that following supplementation of isolated mitochondria with [(35)S]cysteine, a radiolabeled persulfide could be detected on Nfs1p. The persulfide persisted under conditions that did not permit Fe-S cluster formation, such as nucleotide and/or iron depletion of mitochondria. By contrast, under permissive conditions, the radiolabeled Nfs1p persulfide was greatly reduced and radiolabeled aconitase was formed, indicating transfer of persulfide to downstream Fe-S cluster recipients. Nfs","dates":{"release":"2012-01-01T00:00:00Z","publication":"2012 Sep","modification":"2025-04-04T00:48:34.445Z","creation":"2019-03-27T00:58:35Z"},"accession":"S-EPMC3462219","cross_references":{"pubmed":["22813754"],"doi":["10.1016/j.mito.2012.07.103"]}}