{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,29]],"date-time":"2026-09-29T14:19:26Z","timestamp":1790691566425,"version":"4.1.0"},"reference-count":49,"publisher":"Elsevier BV","issue":"41","license":[{"start":{"date-parts":[[2013,10,1]],"date-time":"2013-10-01T00:00:00Z","timestamp":1380585600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2020,9,8]],"date-time":"2020-09-08T00:00:00Z","timestamp":1599523200000},"content-version":"vor","delay-in-days":2534,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Journal of Biological Chemistry"],"published-print":{"date-parts":[[2013,10]]},"DOI":"10.1074\/jbc.m113.497453","type":"journal-article","created":{"date-parts":[[2013,9,4]],"date-time":"2013-09-04T02:17:33Z","timestamp":1378261053000},"page":"29736-29745","source":"Crossref","is-referenced-by-count":52,"title":["Identification of a Bis-molybdopterin Intermediate in Molybdenum Cofactor Biosynthesis in Escherichia coli"],"prefix":"10.1016","volume":"288","author":[{"given":"Stefan","family":"Reschke","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kajsa G.V.","family":"Sigfridsson","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Paul","family":"Kaufmann","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nils","family":"Leidel","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sebastian","family":"Horn","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Klaus","family":"Gast","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Carola","family":"Schulzke","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michael","family":"Haumann","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Silke","family":"Leimk\u00fchler","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1074\/jbc.M113.497453_bib1","doi-asserted-by":"crossref","first-page":"2757","DOI":"10.1021\/cr950061t","article-title":"The mononuclear molybdenum enzymes","volume":"96","author":"Hille","year":"1996","journal-title":"Chem. Rev"},{"key":"10.1074\/jbc.M113.497453_bib2","doi-asserted-by":"crossref","first-page":"10199","DOI":"10.1016\/S0021-9258(19)50001-1","article-title":"The pterin molybdenum cofactors","volume":"267","author":"Rajagopalan","year":"1992","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M113.497453_bib3","first-page":"674","article-title":"Biosynthesis of the molybdenum cofactor","volume":"I","author":"Rajagopalan","year":"1996"},{"key":"10.1074\/jbc.M113.497453_bib4","doi-asserted-by":"crossref","first-page":"1129","DOI":"10.1016\/j.ccr.2010.12.003","article-title":"The history of the discovery of the molybdenum cofactor and novel aspects of its biosynthesis in bacteria","volume":"255","author":"Leimk\u00fchler","year":"2011","journal-title":"Coord. Chem. Rev"},{"key":"10.1074\/jbc.M113.497453_bib5","doi-asserted-by":"crossref","first-page":"12870","DOI":"10.1073\/pnas.0404624101","article-title":"Crystal structure of the S-adenosylmethionine-dependent enzyme MoaA and its implications for molybdenum cofactor deficiency in humans","volume":"101","author":"H\u00e4nzelmann","year":"2004","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.M113.497453_bib6","doi-asserted-by":"crossref","first-page":"7019","DOI":"10.1021\/ja401781t","article-title":"Identification of a cyclic nucleotide as a cryptic intermediate in molybdenum cofactor biosynthesis","volume":"135","author":"Hover","year":"2013","journal-title":"J. Am. Chem. Soc"},{"key":"10.1074\/jbc.M113.497453_bib7","doi-asserted-by":"crossref","first-page":"13506","DOI":"10.1016\/S0021-9258(19)38678-8","article-title":"In vitro synthesis of molybdopterin from precursor Z using purified converting factor. Role of protein-bound sulfur in formation of the dithiolene","volume":"268","author":"Pitterle","year":"1993","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M113.497453_bib8","doi-asserted-by":"crossref","first-page":"36268","DOI":"10.1074\/jbc.M105321200","article-title":"Thiocarboxylation of molybdopterin synthase provides evidence for the mechanism of dithiolene formation in metal-binding pterins","volume":"276","author":"Gutzke","year":"2001","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M113.497453_bib9","doi-asserted-by":"crossref","first-page":"14514","DOI":"10.1074\/jbc.M300449200","article-title":"Structural studies of molybdopterin synthase provide insights into its catalytic mechanism","volume":"278","author":"Rudolph","year":"2003","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M113.497453_bib10","doi-asserted-by":"crossref","first-page":"14523","DOI":"10.1074\/jbc.M300453200","article-title":"Mechanistic and mutational studies of Escherichia coli molybdopterin synthase clarify the final step of molybdopterin biosynthesis","volume":"278","author":"Wuebbens","year":"2003","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M113.497453_bib11","doi-asserted-by":"crossref","first-page":"4310","DOI":"10.1128\/jb.178.14.4310-4312.1996","article-title":"Molybdenum cofactor biosynthesis in Escherichia coli mod and mog mutants","volume":"178","author":"Joshi","year":"1996","journal-title":"J. Bacteriol"},{"key":"10.1074\/jbc.M113.497453_bib12","doi-asserted-by":"crossref","first-page":"36","DOI":"10.1016\/S0003-9861(02)00714-2","article-title":"The active site of the molybdenum cofactor biosynthestic protein domain Cnx1G","volume":"411","author":"Kuper","year":"2003","journal-title":"Arch. Biochem. Biophys"},{"key":"10.1074\/jbc.M113.497453_bib13","doi-asserted-by":"crossref","first-page":"55241","DOI":"10.1074\/jbc.M409862200","article-title":"Synthesis of adenylated molybdopterin. An essential step for molybdenum insertion","volume":"279","author":"Llamas","year":"2004","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M113.497453_bib14","doi-asserted-by":"crossref","first-page":"687","DOI":"10.1111\/j.1432-1033.1994.tb18913.x","article-title":"Isolation of protein FA, a product of the mob locus required for molybdenum cofactor biosynthesis in Escherichia coli","volume":"222","author":"Palmer","year":"1994","journal-title":"Eur. J. Biochem"},{"key":"10.1074\/jbc.M113.497453_bib15","doi-asserted-by":"crossref","first-page":"21891","DOI":"10.1074\/jbc.M109.008565","article-title":"MocA is a specific cytidylyltransferase involved in molybdopterin cytosine dinucleotide biosynthesis in Escherichia coli","volume":"284","author":"Neumann","year":"2009","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M113.497453_bib16","doi-asserted-by":"crossref","first-page":"2762","DOI":"10.1111\/j.1742-4658.2009.07000.x","article-title":"A periplasmic aldehyde oxidoreductase represents the first molybdopterin cytosine dinucleotide cofactor containing molybdo-flavoenzyme from Escherichia coli","volume":"276","author":"Neumann","year":"2009","journal-title":"FEBS J"},{"key":"10.1074\/jbc.M113.497453_bib17","doi-asserted-by":"crossref","first-page":"850924","DOI":"10.1155\/2011\/850924","article-title":"The role of system-specific molecular chaperones in the maturation of molybdoenzymes in bacteria","volume":"2011","author":"Neumann","year":"2011","journal-title":"Biochem. Res. Int"},{"key":"10.1074\/jbc.M113.497453_bib18","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1006\/abbi.1996.0017","article-title":"Identification of the molybdenum cofactor of dimethyl sulfoxide reductase from Rhodobacter sphaeroides f. sp. denitrificans as bis(molybdopterin guanine dinucleotide)molybdenum","volume":"325","author":"Hilton","year":"1996","journal-title":"Arch. Biochem. Biophys"},{"key":"10.1074\/jbc.M113.497453_bib19","doi-asserted-by":"crossref","first-page":"875","DOI":"10.1111\/j.1365-2958.1996.tb02525.x","article-title":"Involvement of the narJ and mob gene products in the biosynthesis of the molybdoenzyme nitrate reductase in Escherichia coli","volume":"20","author":"Palmer","year":"1996","journal-title":"Mol. Microbiol"},{"key":"10.1074\/jbc.M113.497453_bib20","doi-asserted-by":"crossref","first-page":"23706","DOI":"10.1074\/jbc.M301485200","article-title":"Insight into the role of Escherichia coli MobB in molybdenum cofactor biosynthesis based on the high resolution crystal structure","volume":"278","author":"McLuskey","year":"2003","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M113.497453_bib21","doi-asserted-by":"crossref","first-page":"1086","DOI":"10.1016\/j.bbabio.2012.11.007","article-title":"Molybdenum enzymes, their maturation and molybdenum cofactor biosynthesis in Escherichia coli","volume":"1827","author":"Iobbi-Nivol","year":"2013","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1074\/jbc.M113.497453_bib22","doi-asserted-by":"crossref","first-page":"40202","DOI":"10.1074\/jbc.M007407200","article-title":"Mechanism of assembly of the bis(molybdopterin guanine dinucleotide)molybdenum cofactor in Rhodobacter sphaeroides dimethyl sulfoxide reductase","volume":"275","author":"Temple","year":"2000","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M113.497453_bib23","doi-asserted-by":"crossref","first-page":"1400","DOI":"10.1074\/jbc.M110.155671","article-title":"Molybdopterin dinucleotide biosynthesis in Escherichia coli. Identification of amino acid residues of molybdopterin dinucleotide transferases that determine specificity for binding of guanine or cytosine nucleotides","volume":"286","author":"Neumann","year":"2011","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M113.497453_bib24","doi-asserted-by":"crossref","first-page":"40211","DOI":"10.1074\/jbc.M007406200","article-title":"The crystal structure of the Escherichia coli MobA protein provides insight into molybdopterin guanine dinucleotide biosynthesis","volume":"275","author":"Lake","year":"2000","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M113.497453_bib25","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1111\/j.1574-6968.2009.01660.x","article-title":"Multiple roles of TorD-like chaperones in the biogenesis of molybdoenzymes","volume":"297","author":"Genest","year":"2009","journal-title":"FEMS Microbiol. Lett"},{"key":"10.1074\/jbc.M113.497453_bib26","doi-asserted-by":"crossref","first-page":"15644","DOI":"10.1074\/jbc.M501119200","article-title":"TorD, an essential chaperone for TorA molybdoenzyme maturation at high temperature","volume":"280","author":"Genest","year":"2005","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M113.497453_bib27","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1111\/j.1574-6968.2006.00468.x","article-title":"Chaperone protection of immature molybdoenzyme during molybdenum cofactor limitation","volume":"265","author":"Genest","year":"2006","journal-title":"FEMS Microbiol. Lett"},{"key":"10.1074\/jbc.M113.497453_bib28","doi-asserted-by":"crossref","first-page":"21433","DOI":"10.1074\/jbc.M802954200","article-title":"Dedicated metallochaperone connects apoenzyme and molybdenum cofactor biosynthesis components","volume":"283","author":"Genest","year":"2008","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M113.497453_bib29","doi-asserted-by":"crossref","first-page":"281","DOI":"10.1006\/abbi.2000.2089","article-title":"Optimization of expression of human sulfite oxidase and its molybdenum domain","volume":"383","author":"Temple","year":"2000","journal-title":"Arch. Biochem. Biophys"},{"key":"10.1074\/jbc.M113.497453_bib30","doi-asserted-by":"crossref","first-page":"299","DOI":"10.1016\/S0969-2126(01)00588-3","article-title":"The crystal structure of Escherichia coli MoeA and its relationship to the multifunctional protein gephyrin","volume":"9","author":"Xiang","year":"2001","journal-title":"Structure"},{"key":"10.1074\/jbc.M113.497453_bib31","doi-asserted-by":"crossref","first-page":"1814","DOI":"10.1074\/jbc.275.3.1814","article-title":"Crystal structure of the gephyrin-related molybdenum cofactor biosynthesis protein MogA from Escherichia coli","volume":"275","author":"Liu","year":"2000","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M113.497453_bib32","doi-asserted-by":"crossref","first-page":"15701","DOI":"10.1074\/jbc.M601617200","article-title":"Rhodobacter capsulatus XdhC is involved in molybdenum cofactor binding and insertion into xanthine dehydrogenase","volume":"281","author":"Neumann","year":"2006","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M113.497453_bib33","doi-asserted-by":"crossref","first-page":"5678","DOI":"10.1111\/j.1742-4658.2008.06694.x","article-title":"Heavy metal ions inhibit molybdoenzyme activity by binding to the dithiolene moiety of molybdopterin in Escherichia coli","volume":"275","author":"Neumann","year":"2008","journal-title":"FEBS J"},{"key":"10.1074\/jbc.M113.497453_bib34","series-title":"Total Reflection X-ray Fluorescence Analysis","author":"Klockenk\u00e4mper","year":"1996"},{"key":"10.1074\/jbc.M113.497453_bib35","doi-asserted-by":"crossref","first-page":"5414","DOI":"10.1016\/S0021-9258(18)91027-6","article-title":"The pterin component of the molybdenum cofactor. Structural characterization of two fluorescent derivatives","volume":"259","author":"Johnson","year":"1984","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M113.497453_bib36","doi-asserted-by":"crossref","first-page":"3190","DOI":"10.1073\/pnas.87.8.3190","article-title":"Molybdopterin guanine dinucleotide. A modified form of molybdopterin identified in the molybdenum cofactor of dimethyl sulfoxide reductase from Rhodobacter sphaeroides forma specialis denitrificans","volume":"87","author":"Johnson","year":"1990","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.M113.497453_bib37","doi-asserted-by":"crossref","first-page":"741","DOI":"10.1021\/ic101291j","article-title":"Structure of the molybdenum site in YedY, a sulfite oxidase homologue from Escherichia coli","volume":"50","author":"Havelius","year":"2011","journal-title":"Inorg. Chem"},{"key":"10.1074\/jbc.M113.497453_bib38","doi-asserted-by":"crossref","first-page":"562","DOI":"10.1007\/s00216-003-1982-2","article-title":"X-ray absorption spectroscopy to analyze nuclear geometry and electronic structure of biological metal centers. Potential and questions examined with special focus on the tetra-nuclear manganese complex of oxygenic photosynthesis","volume":"376","author":"Dau","year":"2003","journal-title":"Anal. Bioanal. Chem"},{"key":"10.1074\/jbc.M113.497453_bib39","doi-asserted-by":"crossref","first-page":"2995","DOI":"10.1103\/PhysRevB.52.2995","article-title":"Multiple-scattering calculations of X-ray-absorption spectra","volume":"52","author":"Zabinsky","year":"1995","journal-title":"Phys. Rev. B"},{"key":"10.1074\/jbc.M113.497453_bib40","first-page":"978","article-title":"Bond valence parameters linearly dependent on the molybdenum oxidation states","volume":"47","author":"Chen","year":"2002","journal-title":"Chin. Sci. Bull"},{"key":"10.1074\/jbc.M113.497453_bib41","doi-asserted-by":"crossref","first-page":"4102","DOI":"10.1021\/ic00071a023","article-title":"Bond valence sum analysis of metal-ligand bond lengths in metalloenzymes and model complexes. 2. Refined distances and other enzymes","volume":"32","author":"Liu","year":"1993","journal-title":"Inorg. Chem"},{"key":"10.1074\/jbc.M113.497453_bib42","doi-asserted-by":"crossref","first-page":"24995","DOI":"10.1074\/jbc.M203238200","article-title":"Escherichia coli MoeA and MogA. Function in metal incorporation step of molybdenum cofactor biosynthesis","volume":"277","author":"Nichols","year":"2002","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M113.497453_bib43","doi-asserted-by":"crossref","first-page":"7817","DOI":"10.1074\/jbc.M413783200","article-title":"In vitro molybdenum ligation to molybdopterin using purified components","volume":"280","author":"Nichols","year":"2005","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M113.497453_bib44","doi-asserted-by":"crossref","first-page":"3989","DOI":"10.1021\/bi1001954","article-title":"The structures of the C185S and C185A mutants of sulfite oxidase reveal rearrangement of the active site","volume":"49","author":"Qiu","year":"2010","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.M113.497453_bib45","doi-asserted-by":"crossref","first-page":"4387","DOI":"10.1002\/ejic.201100331","article-title":"A crystallographic and Mo K-edge XAS study of molybdenum oxo bis-, mono-, and non-dithiolene complexes. First-sphere coordination geometry and noninnocence of ligands","volume":"28","author":"Samuel","year":"2011","journal-title":"Eur. J. Inorg. Chem"},{"key":"10.1074\/jbc.M113.497453_bib46","doi-asserted-by":"crossref","first-page":"973","DOI":"10.1016\/S0092-8674(00)80488-2","article-title":"Molecular basis of sulfite oxidase deficiency from the structure of sulfite oxidase","volume":"91","author":"Kisker","year":"1997","journal-title":"Cell"},{"key":"10.1074\/jbc.M113.497453_bib47","doi-asserted-by":"crossref","first-page":"233","DOI":"10.1146\/annurev.biochem.66.1.233","article-title":"Molybdenum-cofactor-containing enzymes. Structure and mechanism","volume":"66","author":"Kisker","year":"1997","journal-title":"Annu. Rev. Biochem"},{"key":"10.1074\/jbc.M113.497453_bib48","doi-asserted-by":"crossref","first-page":"1115","DOI":"10.1016\/S0969-2126(00)00518-9","article-title":"Crystal structure of the molybdenum cofactor biosynthesis protein MobA from Escherichia coli at near-atomic resolution","volume":"8","author":"Stevenson","year":"2000","journal-title":"Structure"},{"key":"10.1074\/jbc.M113.497453_bib49","doi-asserted-by":"crossref","first-page":"48199","DOI":"10.1074\/jbc.M205806200","article-title":"In vivo interactions between gene products involved in the final stages of molybdenum cofactor biosynthesis in Escherichia coli","volume":"277","author":"Magalon","year":"2002","journal-title":"J. Biol. Chem"}],"container-title":["Journal of Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925820487927?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925820487927?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/syndication.highwire.org\/content\/doi\/10.1074\/jbc.M113.497453","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,1,4]],"date-time":"2022-01-04T17:41:15Z","timestamp":1641318075000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0021925820487927"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2013,10]]},"references-count":49,"journal-issue":{"issue":"41","published-print":{"date-parts":[[2013,10]]}},"alternative-id":["S0021925820487927"],"URL":"https:\/\/doi.org\/10.1074\/jbc.m113.497453","relation":{},"ISSN":["0021-9258"],"issn-type":[{"value":"0021-9258","type":"print"}],"subject":[],"published":{"date-parts":[[2013,10]]}}}