{"doi":"10.1038/ncomms6013","title":"Functional reconstitution of mitochondrial Fe/S cluster synthesis on Isu1 reveals the involvement of ferredoxin","abstract":null,"journal":"Nature Communications","year":2014,"id":621604,"datarank":0.779774554689874,"base_score":5.198497031265826,"endowment":5.198497031265826,"self_citation_contribution":0.779774554689874,"citation_network_contribution":0.0,"self_endowment_contribution":0.779774554689874,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":180,"citer_count":0,"citers_with_citation_signal":0,"citers_with_endowment":0,"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":1605285,"name":"Sven-Andreas Freibert","orcid":null,"position":1,"is_corresponding":false},{"id":677259,"name":"Angelo Gallo","orcid":"0000-0001-9778-4822","position":2,"is_corresponding":false},{"id":1605286,"name":"Torsten Heidenreich","orcid":null,"position":3,"is_corresponding":false},{"id":1605287,"name":"Uwe Linne","orcid":null,"position":4,"is_corresponding":false},{"id":1605288,"name":"Stefan Amlacher","orcid":null,"position":5,"is_corresponding":false},{"id":179948,"name":"Ed Hurt","orcid":null,"position":6,"is_corresponding":false},{"id":1605289,"name":"Ulrich Mühlenhoff","orcid":null,"position":7,"is_corresponding":false},{"id":1250894,"name":"Lucia Banci","orcid":"0000-0003-0562-5774","position":8,"is_corresponding":false},{"id":1171473,"name":"Roland Lill","orcid":"0000-0002-8345-6518","position":9,"is_corresponding":false},{"id":1605284,"name":"Holger Webert","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Functional reconstitution of mitochondrial Fe/S cluster synthesis on Isu1 reveals the involvement of ferredoxin","abstract":"Maturation of iron-sulphur (Fe/S) proteins involves complex biosynthetic machinery. In vivo synthesis of [2Fe-2S] clusters on the mitochondrial scaffold protein Isu1 requires the cysteine desulphurase complex Nfs1-Isd11, frataxin, ferredoxin Yah1 and its reductase Arh1. The roles of Yah1-Arh1 have remained enigmatic, because they are not required for in vitro Fe/S cluster assembly. Here, we reconstitute [2Fe-2S] cluster synthesis on Isu1 in a reaction depending on Nfs1-Isd11, frataxin, Yah1, Arh1 and NADPH. Unlike in the bacterial system, frataxin is an essential part of Fe/S cluster biosynthesis and is required simultaneously and stoichiometrically to Yah1. Reduced but not oxidized Yah1 tightly interacts with apo-Isu1 indicating a dynamic interaction between Yah1-apo-Isu1. Nuclear magnetic resonance structural studies identify the Yah1-apo-Isu1 interaction surface and suggest a pathway for electron flow from reduced ferredoxin to Isu1. Together, our study defines the molecular function of the ferredoxin Yah1 and its human orthologue FDX2 in mitochondrial Fe/S cluster synthesis.","is_dataset_classified":null,"base_score":0.0,"endowment":0.0,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"25358379","pmcid":null,"openalex_id":null,"authors":[],"funders":[{"funder_name":"European Commission","grant_id":"261863","title":"NMR for Structural Biology"},{"funder_name":"Deutsche Forschungsgemeinschaft","grant_id":"192445154/SFB 987","title":"Microbial Diversity in Environmental Signal Response"},{"funder_name":"European Commission","grant_id":"261572","title":"A worldwide e-Infrastructure for NMR and structural biology"}],"total_grants":3,"fwci":null,"citation_percentile":null,"influential_citations":0,"citation_trend":[],"oa_status":"gold","license":"Springer Nature TDM","oa_locations":[{"url":"https://www.nature.com/articles/ncomms6013.pdf","host_type":"publisher"},{"url":"https://www.nature.com/articles/ncomms6013","host_type":"publisher"},{"url":"https://doi.org/10.1038/ncomms6013","host_type":""},{"url":"http://dx.doi.org/10.1038/ncomms6013","host_type":""},{"url":"https://pubmed.ncbi.nlm.nih.gov/25358379","host_type":""},{"url":"https://dx.doi.org/10.1038/ncomms6013","host_type":""},{"url":"https://hdl.handle.net/21.11116/0000-0007-BDB3-A","host_type":""},{"url":"https://zenodo.org/records/14351298","host_type":""},{"url":"https://www.openaccessrepository.it/record/92123","host_type":""},{"url":"https://hdl.handle.net/2158/949152","host_type":""}],"fields_of_study":["0301 basic medicine","0303 health sciences","03 medical and health sciences"],"mesh_terms":["Mitochondria","Humans","Escherichia coli","Saccharomyces cerevisiae","Chaetomium","Ferredoxin-NADP Reductase","Sulfurtransferases","Ferredoxins","Iron-Sulfur Proteins","Adrenodoxin","Saccharomyces cerevisiae Proteins","Membrane Proteins","Mitochondrial Proteins","Biocatalysis"],"keywords":["Iron-Sulfur Proteins","EGI Federation","Multidisciplinary","Saccharomyces cerevisiae Proteins","Adrenodoxin","General Physics and Astronomy","Membrane Proteins","General Chemistry","Saccharomyces cerevisiae","Chaetomium","General Biochemistry, Genetics and Molecular Biology","Mitochondria","Ferredoxin-NADP Reductase","Mitochondrial Proteins","Sulfurtransferases","European Geothermal Research and Innovation Search Engine","Biocatalysis","Escherichia coli","Ferredoxins","Humans"],"sdg_mappings":[{"sdg_number":3,"sdg_label":"3. 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