{"corpus_id":29185005,"paper_sha":"70942beca596f8c66ef4e7ad3071f212c5d61d08","doi":"10.1146/ANNUREV.BIOCHEM.74.082803.133518","arxiv_id":null,"pmid":15952888,"pmcid":null,"mag_id":2116472408,"dblp_id":null,"acl_id":null,"title":"Structure, function, and formation of biological iron-sulfur clusters.","year":2005,"publication_date":"2005-06-13","venue":"Annual Review of Biochemistry","journal":{"name":"Annual review of biochemistry","pages":"\n          247-81\n        ","volume":"74"},"journal_issn":null,"journal_title":null,"publication_types":["Review","JournalArticle"],"pubmed_pub_types":["Journal Article","Research Support, N.I.H., Extramural","Research Support, U.S. Gov't, Non-P.H.S.","Research Support, U.S. Gov't, P.H.S.","Review"],"s2_fields_of_study":["Biology","Medicine","Chemistry"],"reference_count":209,"citation_count":1328,"influential_citation_count":51,"is_open_access":false,"arxiv_categories":null,"arxiv_license":null,"arxiv_journal_ref":null,"mesh_headings":[{"d":"Amino Acid Sequence","mj":false,"ui":"D000595"},{"d":"Bacterial Proteins","mj":false,"qs":[{"q":"chemistry","mj":false,"ui":"Q000737"},{"q":"genetics","mj":false,"ui":"Q000235"},{"q":"metabolism","mj":false,"ui":"Q000378"}],"ui":"D001426"},{"d":"Carrier Proteins","mj":false,"qs":[{"q":"chemistry","mj":false,"ui":"Q000737"},{"q":"genetics","mj":false,"ui":"Q000235"},{"q":"metabolism","mj":false,"ui":"Q000378"}],"ui":"D002352"},{"d":"Escherichia coli","mj":false,"qs":[{"q":"genetics","mj":false,"ui":"Q000235"},{"q":"metabolism","mj":false,"ui":"Q000378"}],"ui":"D004926"},{"d":"Escherichia coli Proteins","mj":false,"qs":[{"q":"chemistry","mj":false,"ui":"Q000737"},{"q":"genetics","mj":false,"ui":"Q000235"},{"q":"metabolism","mj":false,"ui":"Q000378"}],"ui":"D029968"},{"d":"Genes, Bacterial","mj":false,"ui":"D005798"},{"d":"Iron-Sulfur Proteins","mj":false,"qs":[{"q":"chemistry","mj":true,"ui":"Q000737"},{"q":"genetics","mj":false,"ui":"Q000235"},{"q":"metabolism","mj":true,"ui":"Q000378"}],"ui":"D007506"},{"d":"Molecular Sequence Data","mj":false,"ui":"D008969"},{"d":"Nitrogenase","mj":false,"qs":[{"q":"chemistry","mj":false,"ui":"Q000737"},{"q":"genetics","mj":false,"ui":"Q000235"},{"q":"metabolism","mj":false,"ui":"Q000378"}],"ui":"D009591"},{"d":"Protein Processing, Post-Translational","mj":false,"ui":"D011499"},{"d":"Sequence Homology, Amino Acid","mj":false,"ui":"D017386"}],"chemicals":[{"n":"Bacterial Proteins","ui":"D001426","reg":"0"},{"n":"Carrier Proteins","ui":"D002352","reg":"0"},{"n":"Escherichia coli Proteins","ui":"D029968","reg":"0"},{"n":"Iron-Sulfur Proteins","ui":"D007506","reg":"0"},{"n":"IscA protein, E coli","ui":"C487901","reg":"0"},{"n":"IscU protein, E coli","ui":"C411665","reg":"0"},{"n":"NifU protein, Bacteria","ui":"C088637","reg":"0"},{"n":"nifS protein, Bacteria","ui":"C080001","reg":"0"},{"n":"Nitrogenase","ui":"D009591","reg":"EC 1.18.6.1"}],"comments_corrections":null,"source_flags":5,"s2_open_access_pdf_url":null,"s2_open_access_landing_url":null,"s2_open_access_license":null,"s2_open_access_status":null,"pmc_open_access_pdf_url":null,"pmc_open_access_landing_url":null,"pmc_open_access_license":null,"pmc_open_access_status":null,"unpaywall_open_access_pdf_url":null,"unpaywall_open_access_landing_url":null,"unpaywall_open_access_license":null,"unpaywall_open_access_status":null,"abstract":"Iron-sulfur [Fe-S] clusters are ubiquitous and evolutionary ancient prosthetic groups that are required to sustain fundamental life processes. Owing to their remarkable structural plasticity and versatile chemical/electronic features [Fe-S] clusters participate in electron transfer, substrate binding/activation, iron/sulfur storage, regulation of gene expression, and enzyme activity. Formation of intracellular [Fe-S] clusters does not occur spontaneously but requires a complex biosynthetic machinery. Three different types of [Fe-S] cluster biosynthetic systems have been discovered, and all of them are mechanistically unified by the requirement for a cysteine desulfurase and the participation of an [Fe-S] cluster scaffolding protein. Important mechanistic questions related to [Fe-S] cluster biosynthesis involve the molecular details of how [Fe-S] clusters are assembled on scaffold proteins, how [Fe-S] clusters are transferred from scaffolds to target proteins, how various accessory proteins participate in [Fe-S] protein maturation, and how the biosynthetic process is regulated.","claims":[{"public_id":"cl_81087b24c492d0998686a9f162645aab","status":"active","text":"All known [Fe-S] cluster biosynthetic systems are mechanistically unified by the requirement for a cysteine desulfurase and an [Fe-S] cluster scaffolding protein.","confidence":0.97,"contributors":[{"id":1,"public_id":"12632b8b5f","public_label":"Anonymous (12632b8b5f)","roles":["extraction"],"url":"https://sah.borca.ai/u/12632b8b5f"}],"url":"https://sah.borca.ai/claims/cl_81087b24c492d0998686a9f162645aab"},{"public_id":"cl_6b247d17e8fdbfe859854a5c6396b82a","status":"active","text":"Intracellular [Fe-S] cluster formation does not occur spontaneously and 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