{"id":"f4970e0f-2926-5f52-8168-38c3fae49f35","stable_key":"59b18080-c560-563d-abc5-bac4ee82a27c:ergothioneine-copper-binding","predicate":"forms_complex_with","statement":"Ergothioneine bound copper(I), rather than copper(II), and formed a redox-inactive complex in the tested chemical systems.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"c99dd80e-6231-5a20-a690-2f393f8d9a14","mechanism_event_label":"Copper oxidation state matters for binding.","subject":{"id":"939c92c3-50ea-5a4a-9654-8e3b94448132","slug":"ergothioneine","display_name":"L-Ergothioneine","entity_type_key":"small_molecule"},"object":{"id":"162020b5-1fa5-526e-8405-452891245722","slug":"copper-i","display_name":"Copper(I) ion","entity_type_key":"ion"},"evidence_count":1,"mechanism_event":{"id":"c99dd80e-6231-5a20-a690-2f393f8d9a14","stable_key":"59b18080-c560-563d-abc5-bac4ee82a27c:ergothioneine-copper-binding-event","event_type":"observed_relationship","label":"Copper oxidation state matters for binding.","description":"Ergothioneine bound copper(I), rather than copper(II), and formed a redox-inactive complex in the tested chemical systems.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"939c92c3-50ea-5a4a-9654-8e3b94448132","slug":"ergothioneine","display_name":"L-Ergothioneine","entity_type_key":"small_molecule"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"162020b5-1fa5-526e-8405-452891245722","slug":"copper-i","display_name":"Copper(I) ion","entity_type_key":"ion"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"b9c1084d-e596-5f11-81b9-bf09dda3556e","slug":"ergothioneine-copper-i-complex","display_name":"Ergothioneine-copper(I) complex","entity_type_key":"small_molecule"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""},{"entity":{"id":"2a870bb5-05a0-5e51-a70c-a9a843a8b571","slug":"copper-ii","display_name":"Copper(II) ion","entity_type_key":"ion"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":3,"notes":""},{"entity":{"id":"44374451-3436-5136-a8ae-5dcc6d8c353b","slug":"histidine","display_name":"L-Histidine","entity_type_key":"small_molecule"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":4,"notes":""}]},"contexts":[{"dimension":"evidence_access","value_text":"Primary abstract","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Spectroscopy and competition against histidine/phenanthroline.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"This is not demonstrated copper depletion in humans.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"Ergothioneine collection; molecular form, preparation, species, exposure and manipulation remain explicit.","comparator":null,"unit":null,"notes":"","entity":{"slug":"ergothioneine","display_name":"L-Ergothioneine","entity_type_key":"small_molecule"}},{"dimension":"plain_language","value_text":"Copper oxidation state matters for binding.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"Ergothioneine prevents copper-induced oxidative damage to DNA and protein by forming a redox-inactive ergothioneine-copper complex. · 2011 · https://pubmed.ncbi.nlm.nih.gov/21047085/ · DOI 10.1021/tx100214t","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"1d672fdb-6da1-5b6a-a6d5-78bd17121c9b","evidence_kind":"source_excerpt","locator":"Lines 120-126","start_line":120,"end_line":126,"excerpt":"## ergothioneine-copper-binding\nCopper oxidation state matters for binding.\nErgothioneine bound copper(I), rather than copper(II), and formed a redox-inactive complex in the tested chemical systems.\nModel: Spectroscopy and competition against histidine/phenanthroline.\nLimitations: This is not demonstrated copper depletion in humans.\nEvidence access: Primary abstract\nErgothioneine prevents copper-induced oxidative damage to DNA and protein by forming a redox-inactive ergothioneine-copper complex. · 2011 · https://pubmed.ncbi.nlm.nih.gov/21047085/ · DOI 10.1021/tx100214t","model_system":"Spectroscopy and competition against histidine/phenanthroline.","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":"2f037d98-f3d0-5dbe-80d8-90b738f130d6","stable_key":"import-59b18080-c560-563d-abc5-bac4ee82a27c","title":"Ergothioneine: transport, redox chemistry and cross-nutrient mechanisms (2026-09-19)","document_type":"imported_text","citation_label":"AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text.","file_path":"","sha256":"b6def8119f03cfabeec2fb55ba924340dc612e1dd42f05404201fa2b7ced5259","revision_id":"f88c38e6-ffb5-5a68-83ca-4610ca2c2df4","review_status":"unverified_draft","notes":""}}],"relations":[],"conflicts":[],"corrections":[],"research":null}