{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,30]],"date-time":"2026-09-30T15:05:17Z","timestamp":1790780717672,"version":"4.1.0"},"reference-count":48,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2018,9,1]],"date-time":"2018-09-01T00:00:00Z","timestamp":1535760000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2018,9,1]],"date-time":"2018-09-01T00:00:00Z","timestamp":1535760000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2018,8,8]],"date-time":"2018-08-08T00:00:00Z","timestamp":1533686400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"Structural Genomics Consortium","award":["1097737"],"award-info":[{"award-number":["1097737"]}]},{"DOI":"10.13039\/100006483","name":"AbbVie","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100006483","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Bayer Pharma AG"},{"DOI":"10.13039\/100001003","name":"Boehringer Ingelheim","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100001003","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000196","name":"Canada Foundation for Innovation","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100000196","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100009744","name":"Eshelman Institute for Innovation","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100009744","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100008762","name":"Genome Canada","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100008762","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100010767","name":"Innovative Medicines Initiative","doi-asserted-by":"publisher","award":["115766"],"award-info":[{"award-number":["115766"]}],"id":[{"id":"10.13039\/501100010767","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Janssen, Merck & Co"},{"name":"Novartis Pharma AG"},{"DOI":"10.13039\/501100000192","name":"Ontario Ministry of Economic Development and Innovation","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100000192","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100004319","name":"Pfizer","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100004319","id-type":"DOI","asserted-by":"publisher"}]},{"name":"S\u00e3o Paulo Research Foundation-FAPESP"},{"DOI":"10.13039\/100004440","name":"Wellcome Trust","doi-asserted-by":"publisher","award":["092809\/Z\/10\/Z"],"award-info":[{"award-number":["092809\/Z\/10\/Z"]}],"id":[{"id":"10.13039\/100004440","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Pfizer Rare Disease Consortium"}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Biochimie"],"published-print":{"date-parts":[[2018,9]]},"DOI":"10.1016\/j.biochi.2018.07.012","type":"journal-article","created":{"date-parts":[[2018,7,20]],"date-time":"2018-07-20T11:02:16Z","timestamp":1532084536000},"page":"211-218","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":25,"special_numbering":"C","title":["Zinc(II) binding on human wild-type ISCU and Met140 variants modulates NFS1 desulfurase activity"],"prefix":"10.1016","volume":"152","author":[{"given":"Nicholas G.","family":"Fox","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alain","family":"Martelli","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9600-2347","authenticated-orcid":false,"given":"Joseph F.","family":"Nabhan","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jay","family":"Janz","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Oktawia","family":"Borkowska","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christine","family":"Bulawa","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Wyatt W.","family":"Yue","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.biochi.2018.07.012_bib1","doi-asserted-by":"crossref","first-page":"247","DOI":"10.1146\/annurev.biochem.74.082803.133518","article-title":"Structure, function, and formation of biological iron-sulfur clusters","volume":"74","author":"Johnson","year":"2005","journal-title":"Annu. Rev. Biochem."},{"key":"10.1016\/j.biochi.2018.07.012_bib2","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1038\/nrm3909","article-title":"Mammalian iron-sulphur proteins: novel insights into biogenesis and function","volume":"16","author":"Rouault","year":"2015","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"10.1016\/j.biochi.2018.07.012_bib3","doi-asserted-by":"crossref","first-page":"9132","DOI":"10.1021\/bi1013062","article-title":"Human frataxin is an allosteric switch that activates the Fe-S cluster biosynthetic complex","volume":"49","author":"Tsai","year":"2010","journal-title":"Biochem"},{"key":"10.1016\/j.biochi.2018.07.012_bib4","doi-asserted-by":"crossref","first-page":"831","DOI":"10.1038\/nature08301","article-title":"Function and biogenesis of iron-sulphur proteins","volume":"460","author":"Lill","year":"2009","journal-title":"Nature"},{"key":"10.1016\/j.biochi.2018.07.012_bib5","doi-asserted-by":"crossref","first-page":"82","DOI":"10.1080\/07853890802322229","article-title":"The power plant of the cell is also a smithy: the emerging role of mitochondria in cellular iron homeostasis,","volume":"41","author":"Sheftel","year":"2009","journal-title":"Ann. Med."},{"key":"10.1016\/j.biochi.2018.07.012_bib6","doi-asserted-by":"crossref","first-page":"457","DOI":"10.1146\/annurev.cellbio.22.010305.104538","article-title":"Iron-sulfur protein biogenesis in eukaryotes: components and mechanisms","volume":"22","author":"Lill","year":"2006","journal-title":"Annu. Rev. Cell Dev. Biol."},{"key":"10.1016\/j.biochi.2018.07.012_bib7","doi-asserted-by":"crossref","first-page":"1287","DOI":"10.1038\/s41467-017-01497-1","article-title":"Structure and functional dynamics of the mitochondrial Fe\/S cluster synthesis complex","volume":"8","author":"Boniecki","year":"2017","journal-title":"Nat. Commun."},{"key":"10.1016\/j.biochi.2018.07.012_bib8","doi-asserted-by":"crossref","first-page":"E5325","DOI":"10.1073\/pnas.1702849114","article-title":"Structure of human Fe-S assembly subcomplex reveals unexpected cysteine desulfurase architecture and acyl-ACP-ISD11 interactions","volume":"114","author":"Cory","year":"2017","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.biochi.2018.07.012_bib9","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.17828","article-title":"The mitochondrial acyl Carrier protein (ACP) coordinates mitochondrial fatty acid synthesis with iron sulfur cluster biogenesis","volume":"5","author":"Van Vranken","year":"2016","journal-title":"Elife"},{"key":"10.1016\/j.biochi.2018.07.012_bib10","doi-asserted-by":"crossref","first-page":"4714","DOI":"10.1021\/bi00181a031","article-title":"Mechanism for the desulfurization of L-cysteine catalyzed by the nifS gene product","volume":"33","author":"Zheng","year":"1994","journal-title":"Biochem"},{"key":"10.1016\/j.biochi.2018.07.012_bib11","doi-asserted-by":"crossref","first-page":"12014","DOI":"10.1021\/bi802161u","article-title":"Kinetic analysis of cysteine desulfurase CD0387 from Synechocystis sp PCC 6803: formation of the persulfide intermediate","volume":"48","author":"Behshad","year":"2009","journal-title":"Biochem"},{"key":"10.1016\/j.biochi.2018.07.012_bib12","doi-asserted-by":"crossref","first-page":"1341","DOI":"10.1093\/molbev\/msl001","article-title":"Evolution of the Isd11-IscS complex reveals a single alpha-proteobacterial endosymbiosis for all eukaryotes","volume":"23","author":"Richards","year":"2006","journal-title":"Mol. Biol. Evol."},{"key":"10.1016\/j.biochi.2018.07.012_bib13","doi-asserted-by":"crossref","first-page":"174","DOI":"10.1038\/sj.emboj.7600905","article-title":"The Nfs1 interacting protein Isd11 has an essential role in Fe\/S cluster biogenesis in mitochondria,","volume":"25","author":"Adam","year":"2006","journal-title":"EMBO J."},{"key":"10.1016\/j.biochi.2018.07.012_bib14","doi-asserted-by":"crossref","first-page":"184","DOI":"10.1038\/sj.emboj.7600906","article-title":"Essential role of Isd11 in mitochondrial iron-sulfur cluster synthesis on Isu scaffold proteins","volume":"25","author":"Wiedemann","year":"2006","journal-title":"EMBO J."},{"key":"10.1016\/j.biochi.2018.07.012_bib15","doi-asserted-by":"crossref","first-page":"929","DOI":"10.1093\/hmg\/ddm038","article-title":"Mitochondrial frataxin interacts with ISD11 of the NFS1\/ISCU complex and multiple mitochondrial chaperones","volume":"16","author":"Shan","year":"2007","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.biochi.2018.07.012_bib16","doi-asserted-by":"crossref","first-page":"3014","DOI":"10.1093\/hmg\/ddp239","article-title":"Human ISD11 is essential for both iron-sulfur cluster assembly and maintenance of normal cellular iron homeostasis","volume":"18","author":"Shi","year":"2009","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.biochi.2018.07.012_bib17","doi-asserted-by":"crossref","first-page":"133","DOI":"10.3390\/biology4010133","article-title":"Eukaryotic LYR proteins interact with mitochondrial protein complexes","volume":"4","author":"Angerer","year":"2015","journal-title":"Biology"},{"key":"10.1016\/j.biochi.2018.07.012_bib18","doi-asserted-by":"crossref","first-page":"9132","DOI":"10.1021\/bi1013062","article-title":"Human frataxin is an allosteric switch that activates the Fe-S cluster biosynthetic complex","volume":"49","author":"Tsai","year":"2010","journal-title":"Biochem"},{"key":"10.1016\/j.biochi.2018.07.012_bib19","doi-asserted-by":"crossref","first-page":"3880","DOI":"10.1021\/bi5014497","article-title":"Frataxin accelerates [2Fe-2S] cluster formation on the human Fe-S assembly complex","volume":"54","author":"Fox","year":"2015","journal-title":"Biochem"},{"key":"10.1016\/j.biochi.2018.07.012_bib20","doi-asserted-by":"crossref","first-page":"2506","DOI":"10.1021\/bi201628j","article-title":"Effector role reversal during evolution: the case of frataxin in Fe-S cluster biosynthesis","volume":"51","author":"Bridwell-Rabb","year":"2012","journal-title":"Biochem"},{"key":"10.1016\/j.biochi.2018.07.012_bib21","doi-asserted-by":"crossref","first-page":"12754","DOI":"10.1074\/jbc.R117.787101","article-title":"Iron-sulfur cluster biogenesis and trafficking in mitochondria","volume":"292","author":"Braymer","year":"2017","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.biochi.2018.07.012_bib22","doi-asserted-by":"crossref","first-page":"9595","DOI":"10.1021\/bi301413y","article-title":"Metamorphic protein IscU changes conformation by cis-trans isomerizations of two peptidyl-prolyl peptide bonds","volume":"51","author":"Dai","year":"2012","journal-title":"Biochem"},{"key":"10.1016\/j.biochi.2018.07.012_bib23","doi-asserted-by":"crossref","first-page":"6062","DOI":"10.1021\/bi9002277","article-title":"Structure and dynamics of the iron-sulfur custer assembly scaffold protein IscU and its interaction with the cochaperone HscB","volume":"48","author":"Kim","year":"2009","journal-title":"Biochem"},{"key":"10.1016\/j.biochi.2018.07.012_bib24","doi-asserted-by":"crossref","first-page":"5557","DOI":"10.1021\/bi300579p","article-title":"Three-dimensional structure and determinants of stability of the iron-sulfur cluster scaffold protein IscU from Escherichia coli","volume":"51","author":"Kim","year":"2012","journal-title":"Biochem"},{"key":"10.1016\/j.biochi.2018.07.012_bib25","doi-asserted-by":"crossref","first-page":"454","DOI":"10.1073\/pnas.1114372109","article-title":"Disordered form of the scaffold protein IscU is the substrate for iron-sulfur cluster assembly on cysteine desulfurase","volume":"109","author":"Kim","year":"2012","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.biochi.2018.07.012_bib26","doi-asserted-by":"crossref","first-page":"1172","DOI":"10.1016\/j.febslet.2013.01.003","article-title":"Metamorphic protein IscU alternates conformations in the course of its role as the scaffold protein for iron-sulfur cluster biosynthesis and delivery","volume":"587","author":"Markley","year":"2013","journal-title":"FEBS Lett."},{"key":"10.1016\/j.biochi.2018.07.012_bib27","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1016\/j.jmb.2008.08.015","article-title":"The asymmetric trimeric architecture of [2Fe-2S] IscU: implications for its scaffolding during iron-sulfur cluster biosynthesis","volume":"383","author":"Shimomura","year":"2008","journal-title":"J.\u00a0Mol. Biol."},{"key":"10.1016\/j.biochi.2018.07.012_bib28","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1371\/journal.pbio.1000354","article-title":"Structural basis for Fe-S cluster assembly and tRNA thiolation mediated by IscS protein-protein interactions","volume":"8","author":"Shi","year":"2010","journal-title":"PLoS Biol."},{"key":"10.1016\/j.biochi.2018.07.012_bib29","doi-asserted-by":"crossref","first-page":"5439","DOI":"10.1002\/anie.201201708","article-title":"(IscS-IscU)2 complex structures provide insights into Fe2S2 biogenesis and transfer","volume":"51","author":"Marinoni","year":"2012","journal-title":"Angew Chem. Int. Ed. Engl."},{"key":"10.1016\/j.biochi.2018.07.012_bib30","doi-asserted-by":"crossref","first-page":"875","DOI":"10.1002\/prot.20421","article-title":"Structural characterization of an iron-sulfur cluster assembly protein IscU in a zinc-bound form","volume":"59","author":"Liu","year":"2005","journal-title":"Proteins"},{"key":"10.1016\/j.biochi.2018.07.012_bib31","doi-asserted-by":"crossref","first-page":"567","DOI":"10.1016\/j.jmb.2004.08.038","article-title":"Solution NMR structure of the iron-sulfur cluster assembly protein U (IscU) with zinc bound at the active site","volume":"344","author":"Ramelot","year":"2004","journal-title":"J.\u00a0Mol. Biol."},{"key":"10.1016\/j.biochi.2018.07.012_bib32","doi-asserted-by":"crossref","first-page":"473","DOI":"10.1042\/BJ20111637","article-title":"Mutation in the Fe-S scaffold protein Isu bypasses frataxin deletion","volume":"441","author":"Yoon","year":"2012","journal-title":"Biochem. J."},{"key":"10.1016\/j.biochi.2018.07.012_bib33","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pgen.1005135","article-title":"Turning Saccharomyces cerevisiae into a frataxin-independent organism","volume":"11","author":"Yoon","year":"2015","journal-title":"PLoS Genet."},{"key":"10.1016\/j.biochi.2018.07.012_bib34","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1042\/BJ20131273","article-title":"Frataxin-bypassing Isu1: characterization of the bypass activity in cells and mitochondria","volume":"459","author":"Yoon","year":"2014","journal-title":"Biochem. J."},{"key":"10.1016\/j.biochi.2018.07.012_bib35","doi-asserted-by":"crossref","first-page":"36773","DOI":"10.1074\/jbc.M113.525857","article-title":"Frataxin directly stimulates mitochondrial cysteine desulfurase by exposing substrate-binding sites, and a mutant Fe-S cluster scaffold protein with frataxin-bypassing ability acts similarly","volume":"288","author":"Pandey","year":"2013","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.biochi.2018.07.012_bib36","doi-asserted-by":"crossref","first-page":"4904","DOI":"10.1021\/bi500532e","article-title":"Human frataxin activates Fe-S cluster biosynthesis by facilitating sulfur transfer chemistry","volume":"53","author":"Bridwell-Rabb","year":"2014","journal-title":"Biochem"},{"key":"10.1016\/j.biochi.2018.07.012_bib37","doi-asserted-by":"crossref","first-page":"9641","DOI":"10.1021\/bi201123z","article-title":"Facilitated transfer of IscU-[2Fe2S] clusters by chaperone-mediated ligand exchange","volume":"50","author":"Bonomi","year":"2011","journal-title":"Biochem"},{"key":"10.1016\/j.biochi.2018.07.012_bib38","doi-asserted-by":"crossref","first-page":"1453","DOI":"10.1002\/1521-4109(200012)12:18<1453::AID-ELAN1453>3.0.CO;2-Z","article-title":"The electrochemical analog of the methylene blue reaction: a novel amperometric approach to the detection of hydrogen sulfide","volume":"12","author":"Lawrence","year":"2000","journal-title":"Electroanalysis"},{"key":"10.1016\/j.biochi.2018.07.012_bib39","doi-asserted-by":"crossref","first-page":"5686","DOI":"10.1038\/ncomms6686","article-title":"Mammalian frataxin directly enhances sulfur transfer of NFS1 persulfide to both ISCU and free thiols","volume":"6","author":"Parent","year":"2015","journal-title":"Nat. Commun."},{"key":"10.1016\/j.biochi.2018.07.012_bib40","doi-asserted-by":"crossref","first-page":"126","DOI":"10.1016\/0003-2697(65)90051-5","article-title":"A\u00a0direct microdetermination for sulfide,","volume":"11","author":"Siegel","year":"1965","journal-title":"Anal. Biochem."},{"key":"10.1016\/j.biochi.2018.07.012_bib41","doi-asserted-by":"crossref","first-page":"25178","DOI":"10.1074\/jbc.M804064200","article-title":"A\u00a0novel role for human Nfs1 in the cytoplasm: Nfs1 acts as a sulfur donor for MOCS3, a protein involved in molybdenum cofactor biosynthesis","volume":"283","author":"Marelja","year":"2008","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.biochi.2018.07.012_bib42","doi-asserted-by":"crossref","first-page":"1208","DOI":"10.1002\/pro.2501","article-title":"The role of zinc in the stability of the marginally stable IscU scaffold protein,","volume":"23","author":"Iannuzzi","year":"2014","journal-title":"Protein Sci."},{"key":"10.1016\/j.biochi.2018.07.012_bib43","doi-asserted-by":"crossref","first-page":"487","DOI":"10.1021\/acs.biochem.6b00447","article-title":"Human mitochondrial ferredoxin 1 (FDX1) and ferredoxin 2 (FDX2) both bind cysteine desulfurase and donate electrons for iron-sulfur cluster biosynthesis","volume":"56","author":"Cai","year":"2017","journal-title":"Biochem"},{"key":"10.1016\/j.biochi.2018.07.012_bib44","doi-asserted-by":"crossref","first-page":"28755","DOI":"10.1074\/jbc.M113.482042","article-title":"Human mitochondrial chaperone (mtHSP70) and cysteine desulfurase (NFS1) bind preferentially to the disordered conformation, whereas co-chaperone (HSC20) binds to the structured conformation of the iron-sulfur cluster scaffold protein (ISCU)","volume":"288","author":"Cai","year":"2013","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.biochi.2018.07.012_bib45","doi-asserted-by":"crossref","first-page":"733","DOI":"10.1021\/ja308736e","article-title":"Mammalian frataxin controls sulfur production and iron entry during de Novo Fe4S4 cluster assembly","volume":"135","author":"Colin","year":"2013","journal-title":"J.\u00a0Am. Chem. Soc."},{"issue":"51","key":"10.1016\/j.biochi.2018.07.012_bib46","doi-asserted-by":"crossref","first-page":"18464","DOI":"10.1021\/jacs.7b11307","article-title":"Zinc-Ligand swapping mediated complex formation and sulfur transfer between SufS and SufU for iron-sulfur cluster biogenesis in Bacillus subtilis","volume":"139","author":"Fujishiro","year":"2017","journal-title":"J.\u00a0Am. Chem. Soc."},{"key":"10.1016\/j.biochi.2018.07.012_bib47","doi-asserted-by":"crossref","first-page":"202","DOI":"10.1039\/C4MT00230J","article-title":"Analyzing free zinc(II) ion concentrations in cell biology with fluorescent chelating molecules","volume":"7","author":"Maret","year":"2015","journal-title":"Metall"},{"key":"10.1016\/j.biochi.2018.07.012_bib48","doi-asserted-by":"crossref","first-page":"589","DOI":"10.1016\/j.jinorgbio.2011.02.002","article-title":"Evidence for operation of the direct zinc ligand exchange mechanism for trafficking, transport, and reactivity of zinc in mammalian cells","volume":"105","author":"Costello","year":"2011","journal-title":"J.\u00a0Inorg. Biochem."}],"container-title":["Biochimie"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0300908418302074?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0300908418302074?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2024,6,1]],"date-time":"2024-06-01T08:45:29Z","timestamp":1717231529000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0300908418302074"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2018,9]]},"references-count":48,"alternative-id":["S0300908418302074"],"URL":"https:\/\/doi.org\/10.1016\/j.biochi.2018.07.012","relation":{"has-preprint":[{"id-type":"doi","id":"10.1101\/262477","asserted-by":"object"}]},"ISSN":["0300-9084"],"issn-type":[{"value":"0300-9084","type":"print"}],"subject":[],"published":{"date-parts":[[2018,9]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Zinc(II) binding on human wild-type ISCU and Met140 variants modulates NFS1 desulfurase activity","name":"articletitle","label":"Article Title"},{"value":"Biochimie","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.biochi.2018.07.012","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2018 The Authors. Published by Elsevier B.V.","name":"copyright","label":"Copyright"}]}}