{"doi":"10.1371/journal.pone.0135896","title":"Identification of the Mitochondrial Heme Metabolism Complex","abstract":null,"journal":"PLOS ONE","year":2015,"id":669742,"datarank":3.4560351482048777,"base_score":4.709530201312334,"endowment":4.709530201312334,"self_citation_contribution":0.7064295301968502,"citation_network_contribution":2.7496056180080277,"self_endowment_contribution":0.7064295301968502,"citer_contribution":2.7496056180080277,"corpus_percentile":null,"corpus_rank":null,"citation_count":110,"citer_count":85,"citers_with_citation_signal":77,"citers_with_endowment":77,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":null,"is_data_producer":false,"deposit_databanks":null,"is_oa":false,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":null,"fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":1749216,"name":"Mesafint T. Shiferaw","orcid":null,"position":1,"is_corresponding":false},{"id":261362,"name":"Jason R. Marcero","orcid":null,"position":2,"is_corresponding":false},{"id":606126,"name":"Ajay A. Vashisht","orcid":null,"position":3,"is_corresponding":false},{"id":14958,"name":"James A. Wohlschlegel","orcid":"0000-0003-3399-901X","position":4,"is_corresponding":false},{"id":576040,"name":"John D. Phillips","orcid":"0000-0003-1567-1678","position":5,"is_corresponding":false},{"id":695828,"name":"Harry A. Dailey","orcid":null,"position":6,"is_corresponding":false},{"id":259688,"name":"Amy E. Medlock","orcid":"0000-0001-9402-3593","position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Identification of the Mitochondrial Heme Metabolism Complex","abstract":"Heme is an essential cofactor for most organisms and all metazoans. While the individual enzymes involved in synthesis and utilization of heme are fairly well known, less is known about the intracellular trafficking of porphyrins and heme, or regulation of heme biosynthesis via protein complexes. To better understand this process we have undertaken a study of macromolecular assemblies associated with heme synthesis. Herein we have utilized mass spectrometry with coimmunoprecipitation of tagged enzymes of the heme biosynthetic pathway in a developing erythroid cell culture model to identify putative protein partners. The validity of these data obtained in the tagged protein system is confirmed by normal porphyrin/heme production by the engineered cells. Data obtained are consistent with the presence of a mitochondrial heme metabolism complex which minimally consists of ferrochelatase, protoporphyrinogen oxidase and aminolevulinic acid synthase-2. Additional proteins involved in iron and intermediary metabolism as well as mitochondrial transporters were identified as potential partners in this complex. The data are consistent with the known location of protein components and support a model of transient protein-protein interactions within a dynamic protein complex.","is_dataset_classified":null,"base_score":4.709530201312334,"endowment":4.709530201312334,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"26287972","pmcid":"PMC4545792","openalex_id":"https://openalex.org/W2258975283","authors":[],"funders":[{"funder_name":"NIGMS NIH HHS","grant_id":"GM089778","title":null},{"funder_name":"NIDDK NIH HHS","grant_id":"DK020503","title":null},{"funder_name":"NIDDK NIH HHS","grant_id":"DK096051","title":null},{"funder_name":"NIDDK NIH HHS","grant_id":"R56 DK020503","title":null},{"funder_name":"NIDDK NIH HHS","grant_id":"R01 DK020503","title":null},{"funder_name":"NIDDK NIH HHS","grant_id":"R37 DK020503","title":null},{"funder_name":"NIDDK NIH HHS","grant_id":"DK083909","title":null},{"funder_name":"NIGMS NIH HHS","grant_id":"R01 GM089778","title":null},{"funder_name":"NIDDK NIH HHS","grant_id":"R01 DK096051","title":null},{"funder_name":"NIDDK NIH HHS","grant_id":"U54 DK083909","title":null},{"funder_name":"National Institutes of Health","grant_id":"3R01DK096051-01S1","title":"Erythroid heme synthesis regulation via the ferrochelatase [2Fe-2S] cluster"}],"total_grants":11,"fwci":3.1642,"citation_percentile":0.92631203,"influential_citations":0,"citation_trend":[{"year":2016,"count":7},{"year":2017,"count":7},{"year":2018,"count":9},{"year":2019,"count":11},{"year":2020,"count":14},{"year":2021,"count":13},{"year":2022,"count":16},{"year":2023,"count":9},{"year":2024,"count":13},{"year":2025,"count":7},{"year":2026,"count":4}],"oa_status":"gold","license":"cc-by","oa_locations":[{"url":"https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0135896&type=printable","host_type":"journal"},{"url":"https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0135896&type=printable","host_type":"publisher"},{"url":"http://dx.plos.org/10.1371/journal.pone.0135896","host_type":"publisher"},{"url":"https://doi.org/10.1371/journal.pone.0135896","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/26287972","host_type":"repository"},{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/4545792","host_type":"repository"},{"url":"https://doaj.org/article/ca64578a9d314a46a82369adbe67b493","host_type":"repository"},{"url":"https://escholarship.org/uc/item/8ws7114h","host_type":"repository"},{"url":"https://europepmc.org/articles/PMC4545792","host_type":"Europe_PMC"},{"url":"https://europepmc.org/articles/PMC4545792?pdf=render","host_type":"Europe_PMC"},{"url":"http://dx.doi.org/10.1371/journal.pone.0135896","host_type":""},{"url":"https://dx.doi.org/10.1371/journal.pone.0135896","host_type":""},{"url":"https://escholarship.org/content/qt8ws7114h/qt8ws7114h.pdf","host_type":""},{"url":"https://doi.org/https://doi.org/10.1371/journal.pone.0135896","host_type":""}],"fields_of_study":["Porphyrin Metabolism and Disorders","Heme Oxygenase-1 and Carbon Monoxide","Hemoglobin structure and function","0301 basic medicine","03 medical and health sciences","5-Aminolevulinate Synthetase","ATP-Binding Cassette Transporters","Animals","Cell Line, Tumor","Ferrochelatase","Heme","Humans","Mice","Mitochondria","Multiprotein Complexes","Porphyrins","Protoporphyrinogen Oxidase"],"mesh_terms":["5-Aminolevulinate Synthetase","Animals","Ferrochelatase","Heme","Humans","Mitochondria","Porphyrins","ATP-Binding Cassette Transporters","Cell Line, Tumor","Multiprotein Complexes","Protoporphyrinogen Oxidase","Mice"],"keywords":["Heme","Ferrochelatase","Protoporphyrinogen oxidase","Biochemistry","Hemeprotein","Cofactor","Immunoprecipitation","Heme A","Biology","Metabolism","Mitochondrion","Enzyme","Chemistry","Cell biology","Gene","570","Porphyrins","General Science & Technology","1.1 Normal biological development and functioning","Science","Cell Line","Mice","Cell Line, Tumor","Animals","Humans","Tumor","Q","R","Biological Sciences","Mitochondria","Multiprotein Complexes","Medicine","ATP-Binding Cassette Transporters","Biochemistry and Cell Biology","Generic health relevance","Research Article","5-Aminolevulinate Synthetase"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-15T03:22:58.408751Z","pmid":null,"pmcid":null,"fwci":null,"citation_percentile":null,"influential_citations":0,"oa_status":null,"license":null,"views":0,"total_file_size_bytes":0,"version_count":0,"fair_f":null,"fair_a":null,"fair_i":null,"fair_r":null,"fair_zscore":null,"fair_rationale":null,"fair_model":null,"fair_agent_version":null,"fair_fulltext_source":null,"fair_has_llm":null,"fair_computed_at":null,"clinical_trials":[],"software_tools":[],"db_accessions":[],"linked_datasets":[],"topics":[]}