{"id":"26771eba-aaa8-5b1b-8289-9b524bcd05ad","stable_key":"6612c190-1948-5bcf-bbe3-a7f6c50fa3cf:l-proline-ros-source-boundary","predicate":"drives_indirect_mitochondrial_ros","statement":"During proline oxidation in ZR75-30 mitochondria, the main measured ROS sources were complex I and 2-oxoglutarate dehydrogenase, with no significant direct PRODH contribution under the tested substrate/inhibitor conditions.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"c497dad7-0fbf-5a41-8a96-2f0a59efb599","mechanism_event_label":"A pathway can increase ROS without its first enzyme being the direct ROS-producing site.","subject":{"id":"70ccd53c-83ad-5251-a4f5-6370973bc40a","slug":"l-proline","display_name":"L-Proline","entity_type_key":"small_molecule"},"object":{"id":"c0517840-0850-5e25-a527-eec96c806137","slug":"human-zr7530-proline-ros-sites","display_name":"Sites of ROS formation during proline oxidation in ZR75-30 mitochondria","entity_type_key":"cellular_process"},"evidence_count":1,"mechanism_event":{"id":"c497dad7-0fbf-5a41-8a96-2f0a59efb599","stable_key":"6612c190-1948-5bcf-bbe3-a7f6c50fa3cf:l-proline-ros-source-boundary-event","event_type":"observed_relationship","label":"A pathway can increase ROS without its first enzyme being the direct ROS-producing site.","description":"During proline oxidation in ZR75-30 mitochondria, the main measured ROS sources were complex I and 2-oxoglutarate dehydrogenase, with no significant direct PRODH contribution under the tested substrate/inhibitor conditions.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"70ccd53c-83ad-5251-a4f5-6370973bc40a","slug":"l-proline","display_name":"L-Proline","entity_type_key":"small_molecule"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"c0517840-0850-5e25-a527-eec96c806137","slug":"human-zr7530-proline-ros-sites","display_name":"Sites of ROS formation during proline oxidation in ZR75-30 mitochondria","entity_type_key":"cellular_process"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"5e13a254-f92e-5317-abb5-2c683b178d39","slug":"prodh","display_name":"Human proline dehydrogenase / PRODH","entity_type_key":"protein"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""},{"entity":{"id":"8d8cf36b-d1f4-57eb-8ce2-798d6f3c30b9","slug":"oxoglutarate-dehydrogenase-complex","display_name":"2-Oxoglutarate dehydrogenase complex","entity_type_key":"protein_complex"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":3,"notes":""}]},"contexts":[{"dimension":"evidence_access","value_text":"Primary full text","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Isolated human mitochondria; inhibitor combinations used to distinguish ROS-generating sites.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Results in Drosophila instead emphasized complexes I and II; these species-specific observations do not identify a universal source.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"L-Proline collection; species, compartment, exposure, co-substrates and manipulation remain explicit.","comparator":null,"unit":null,"notes":"","entity":{"slug":"l-proline","display_name":"L-Proline","entity_type_key":"small_molecule"}},{"dimension":"plain_language","value_text":"A pathway can increase ROS without its first enzyme being the direct ROS-producing site.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"Sources of superoxide/H2O2 during mitochondrial proline oxidation. · 2014 · https://pubmed.ncbi.nlm.nih.gov/25184115/ · DOI 10.1016/j.redox.2014.07.003","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"a9dc00d1-2249-581a-8fe6-789853c3a180","evidence_kind":"source_excerpt","locator":"Lines 142-148","start_line":142,"end_line":148,"excerpt":"## l-proline-ros-source-boundary\nA pathway can increase ROS without its first enzyme being the direct ROS-producing site.\nDuring proline oxidation in ZR75-30 mitochondria, the main measured ROS sources were complex I and 2-oxoglutarate dehydrogenase, with no significant direct PRODH contribution under the tested substrate/inhibitor conditions.\nModel: Isolated human mitochondria; inhibitor combinations used to distinguish ROS-generating sites.\nLimitations: Results in Drosophila instead emphasized complexes I and II; these species-specific observations do not identify a universal source.\nEvidence access: Primary full text\nSources of superoxide/H2O2 during mitochondrial proline oxidation. · 2014 · https://pubmed.ncbi.nlm.nih.gov/25184115/ · DOI 10.1016/j.redox.2014.07.003","model_system":"Isolated human mitochondria; inhibitor combinations used to distinguish ROS-generating sites.","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":"e5aa7fc5-ee52-5376-8169-416082a89fd1","stable_key":"import-6612c190-1948-5bcf-bbe3-a7f6c50fa3cf","title":"L-Proline: synthesis, collagen processing, redox metabolism 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. 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