{"id":"45448517-dba8-5fea-b7a3-b83d070f5f20","stable_key":"a8baf7e9-80e4-5d8c-adec-9a63e84d2f21:l-cysteine-fe-s-sulfur-donor","predicate":"supplies_sulfur_to","statement":"Sulfur-35 cysteine supplied sulfur for newly assembled iron–sulfur clusters incorporated into aconitase and ferredoxins in isolated mouse neuronal-cell mitochondria.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"c9126af2-0c44-58f2-a887-5c6105367e29","mechanism_event_label":"Cysteine supplies the sulfur half of an iron–sulfur cofactor.","subject":{"id":"ca899f13-50ad-55e5-ab99-329ae0038c74","slug":"l-cysteine","display_name":"L-Cysteine","entity_type_key":"small_molecule"},"object":{"id":"ce29656b-d3bb-542b-b665-27c59cdcbad9","slug":"mouse-mitochondrial-fe-s-assembly","display_name":"Iron–sulfur cluster assembly in isolated mouse-cell mitochondria","entity_type_key":"cellular_process"},"evidence_count":1,"mechanism_event":{"id":"c9126af2-0c44-58f2-a887-5c6105367e29","stable_key":"a8baf7e9-80e4-5d8c-adec-9a63e84d2f21:l-cysteine-fe-s-sulfur-donor-event","event_type":"observed_relationship","label":"Cysteine supplies the sulfur half of an iron–sulfur cofactor.","description":"Sulfur-35 cysteine supplied sulfur for newly assembled iron–sulfur clusters incorporated into aconitase and ferredoxins in isolated mouse neuronal-cell mitochondria.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"ca899f13-50ad-55e5-ab99-329ae0038c74","slug":"l-cysteine","display_name":"L-Cysteine","entity_type_key":"small_molecule"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"ce29656b-d3bb-542b-b665-27c59cdcbad9","slug":"mouse-mitochondrial-fe-s-assembly","display_name":"Iron–sulfur cluster assembly in isolated mouse-cell mitochondria","entity_type_key":"cellular_process"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"f5cef903-677c-5210-8a13-37f7626fd89f","slug":"mouse-nfs1","display_name":"Mouse cysteine desulfurase / Nfs1","entity_type_key":"protein"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""},{"entity":{"id":"89bcaf42-b4ab-5760-8c2e-44eace10cee0","slug":"iron","display_name":"Iron","entity_type_key":"nutrient_element"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":3,"notes":""}]},"contexts":[{"dimension":"evidence_access","value_text":"Primary abstract","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Mitochondria from mouse Cath.A-derived neuronal cells; radioactive sulfur tracing.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"An isolated-organelle assembly assay is not evidence that more dietary cysteine corrects an iron–sulfur disease.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"L-Cysteine collection; species, compartment, exposure, co-substrates and manipulation remain explicit.","comparator":null,"unit":null,"notes":"","entity":{"slug":"l-cysteine","display_name":"L-Cysteine","entity_type_key":"small_molecule"}},{"dimension":"plain_language","value_text":"Cysteine supplies the sulfur half of an iron–sulfur cofactor.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"Fe-S cluster biogenesis in isolated mammalian mitochondria: coordinated use of persulfide sulfur and iron and requirements for GTP, NADH, and ATP. · 2015 · https://pubmed.ncbi.nlm.nih.gov/25398879/ · DOI 10.1074/jbc.M114.610402","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"38113bb6-f3e4-5ad8-bb9b-8016e28f446a","evidence_kind":"source_excerpt","locator":"Lines 268-274","start_line":268,"end_line":274,"excerpt":"## l-cysteine-fe-s-sulfur-donor\nCysteine supplies the sulfur half of an iron–sulfur cofactor.\nSulfur-35 cysteine supplied sulfur for newly assembled iron–sulfur clusters incorporated into aconitase and ferredoxins in isolated mouse neuronal-cell mitochondria.\nModel: Mitochondria from mouse Cath.A-derived neuronal cells; radioactive sulfur tracing.\nLimitations: An isolated-organelle assembly assay is not evidence that more dietary cysteine corrects an iron–sulfur disease.\nEvidence access: Primary abstract\nFe-S cluster biogenesis in isolated mammalian mitochondria: coordinated use of persulfide sulfur and iron and requirements for GTP, NADH, and ATP. · 2015 · https://pubmed.ncbi.nlm.nih.gov/25398879/ · DOI 10.1074/jbc.M114.610402","model_system":"Mitochondria from mouse Cath.A-derived neuronal cells; radioactive sulfur tracing.","directness":"reported_statement","verification_status":"source_derived_draft","notes":"Original curation paraphrase; evidence access and experimental limitations specified.","relationship":"supports","weight":1.0,"link_notes":"","source":{"id":"654560f6-8d7f-596b-8722-48d94053cfe3","stable_key":"import-a8baf7e9-80e4-5d8c-adec-9a63e84d2f21","title":"L-Cysteine: sulfur allocation, redox supply and cross-nutrient mechanisms (2026-09-19)","document_type":"imported_text","citation_label":"AI-assisted research curation; 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