{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,18]],"date-time":"2026-08-18T01:31:12Z","timestamp":1787016672700,"version":"build-2736575974"},"reference-count":47,"publisher":"American Society for Microbiology","issue":"23","license":[{"start":{"date-parts":[[2001,12,1]],"date-time":"2001-12-01T00:00:00Z","timestamp":1007164800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["J Bacteriol"],"published-print":{"date-parts":[[2001,12]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:p>\n                    In cell extracts of\n                    <jats:italic>Pseudaminobacter salicylatoxidans<\/jats:italic>\n                    strain BN12, an enzymatic activity was detected which converted salicylate in an oxygen-dependent but NAD(P)H-independent reaction to a product with an absorbance maximum at 283 nm. This metabolite was isolated, purified, and identified by mass spectrometry and\n                    <jats:sup>1<\/jats:sup>\n                    H and\n                    <jats:sup>13<\/jats:sup>\n                    C nuclear magnetic resonance spectroscopy as 2-oxohepta-3,5-dienedioic acid. This metabolite could be formed only by direct ring fission of salicylate by a 1,2-dioxygenase reaction. Cell extracts from\n                    <jats:italic>P. salicylatoxidans<\/jats:italic>\n                    also oxidized 5-aminosalicylate, 3-, 4-, and 5-chlorosalicylate, 3-, 4-, and 5-methylsalicylate, 3- and 5-hydroxysalicylate (gentisate), and 1-hydroxy-2-naphthoate. The dioxygenase was purified and shown to consist of four identical subunits with a molecular weight of about 45,000. The purified enzyme showed higher catalytic constants with gentisate or 1-hydroxy-2-naphthoate than with salicylate. It was therefore concluded that\n                    <jats:italic>P. salicylatoxidans<\/jats:italic>\n                    synthesized a gentisate 1,2-dioxygenase with an extraordinary substrate range, which also allowed the oxidation of salicylate.\n                  <\/jats:p>","DOI":"10.1128\/jb.183.23.6936-6942.2001","type":"journal-article","created":{"date-parts":[[2002,7,27]],"date-time":"2002-07-27T05:58:18Z","timestamp":1027749498000},"page":"6936-6942","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":73,"title":["Direct Ring Fission of Salicylate by a Salicylate 1,2-Dioxygenase Activity from\n                    <i>Pseudaminobacter salicylatoxidans<\/i>"],"prefix":"10.1128","volume":"183","author":[{"given":"Jan-Peter","family":"Hintner","sequence":"first","affiliation":[{"name":"<!--label omitted: 1-->Institut fu\u0308r Mikrobiologie, Universita\u0308t Stuttgart, 70569 Stuttgart,1and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christa","family":"Lechner","sequence":"additional","affiliation":[{"name":"<!--label omitted: 1-->Institut fu\u0308r Mikrobiologie, Universita\u0308t Stuttgart, 70569 Stuttgart,1and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ulrich","family":"Riegert","sequence":"additional","affiliation":[{"name":"<!--label omitted: 1-->Institut fu\u0308r Mikrobiologie, Universita\u0308t Stuttgart, 70569 Stuttgart,1and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Andrea Elisabeth","family":"Kuhm","sequence":"additional","affiliation":[{"name":"<!--label omitted: 1-->Institut fu\u0308r Mikrobiologie, Universita\u0308t Stuttgart, 70569 Stuttgart,1and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Thomas","family":"Storm","sequence":"additional","affiliation":[{"name":"<!--label omitted: 2-->Fachgebiet Wasserreinhaltung, Technische Universita\u0308t Berlin, Sekr. KF4, 10623 Berlin,2 Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Thorsten","family":"Reemtsma","sequence":"additional","affiliation":[{"name":"<!--label omitted: 2-->Fachgebiet Wasserreinhaltung, Technische Universita\u0308t Berlin, Sekr. KF4, 10623 Berlin,2 Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Andreas","family":"Stolz","sequence":"additional","affiliation":[{"name":"<!--label omitted: 1-->Institut fu\u0308r Mikrobiologie, Universita\u0308t Stuttgart, 70569 Stuttgart,1and"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_1_2_2","doi-asserted-by":"publisher","DOI":"10.1128\/JB.181.3.757-763.1999"},{"key":"e_1_3_1_3_2","doi-asserted-by":"crossref","first-page":"607","DOI":"10.1042\/bj1940607","article-title":"2,3-Dihydroxybenzoate pathway in Pseudomonas putida","volume":"194","author":"Andreoni V.","year":"1981","unstructured":"Andreoni V. Canonica L. Galli E. Gennari C. Treccani V. 2,3-Dihydroxybenzoate pathway in Pseudomonas putida.Biochem. J.1941981607610","journal-title":"Biochem. J."},{"key":"e_1_3_1_4_2","doi-asserted-by":"publisher","DOI":"10.1016\/0003-2697(76)90527-3"},{"key":"e_1_3_1_5_2","doi-asserted-by":"publisher","DOI":"10.1128\/aem.42.1.39-43.1981"},{"key":"e_1_3_1_6_2","doi-asserted-by":"publisher","DOI":"10.1128\/aem.42.1.44-55.1981"},{"key":"e_1_3_1_7_2","doi-asserted-by":"publisher","DOI":"10.1128\/jb.121.3.794-799.1975"},{"key":"e_1_3_1_8_2","doi-asserted-by":"publisher","DOI":"10.1128\/aem.38.3.379-384.1979"},{"key":"e_1_3_1_9_2","doi-asserted-by":"crossref","first-page":"330","DOI":"10.1007\/s002030050787","article-title":"Genetic and biochemical comparison of 2-aminophenol 1,6-dioxygenase of Pseudomonas pseudoalcaligenes JS45 to meta-cleavage dioxygenases: divergent evolution of 2-aminophenol meta-cleavage pathway","volume":"172","author":"Davis J. K.","year":"1999","unstructured":"Davis J. K. He Z. Somerville C. C. Spain J. C. Genetic and biochemical comparison of 2-aminophenol 1,6-dioxygenase of Pseudomonas pseudoalcaligenes JS45 to meta-cleavage dioxygenases: divergent evolution of 2-aminophenol meta-cleavage pathway.Arch. Microbiol.1721999330339","journal-title":"Arch. Microbiol."},{"key":"e_1_3_1_10_2","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1007\/BF00696222","article-title":"Isolation and characterization of a 3-chlorobenzoate degrading pseudomonad","volume":"99","author":"Dorn E.","year":"1974","unstructured":"Dorn E. Hellwig M. Reineke W. Knackmuss H. J. Isolation and characterization of a 3-chlorobenzoate degrading pseudomonad.Arch. Microbiol.9919746170","journal-title":"Arch. Microbiol."},{"key":"e_1_3_1_11_2","doi-asserted-by":"crossref","first-page":"447","DOI":"10.1021\/jo00204a004","article-title":"Synthesis and interconversion of the four isomeric 6-oxo-2,4-heptadienoic acids","volume":"50","author":"Feliu A. L.","year":"1985","unstructured":"Feliu A. L. Seltzer S. Synthesis and interconversion of the four isomeric 6-oxo-2,4-heptadienoic acids.J. Org. Chem.501985447451","journal-title":"J. Org. Chem."},{"key":"e_1_3_1_12_2","doi-asserted-by":"publisher","DOI":"10.1128\/AEM.65.3.946-950.1999"},{"key":"e_1_3_1_13_2","doi-asserted-by":"crossref","first-page":"439","DOI":"10.1007\/s007920050090","article-title":"Gentisate 1,2-dioxygenase from Haloferax sp. D1227","volume":"2","author":"Fu W.","year":"1998","unstructured":"Fu W. Oriel P. Gentisate 1,2-dioxygenase from Haloferax sp. D1227.Extremophiles21998439446","journal-title":"Extremophiles"},{"key":"e_1_3_1_14_2","doi-asserted-by":"crossref","first-page":"6301","DOI":"10.1016\/S0021-9258(19)39326-3","article-title":"Gentisate 1,2-dioxygenase from Pseudomonas. Purification, characterization, and comparison of the enzymes from Pseudomonas testosteroni and Pseudomonas acidovorans","volume":"265","author":"Harpel M. R.","year":"1990","unstructured":"Harpel M. R. Lipscomb J. D. Gentisate 1,2-dioxygenase from Pseudomonas. Purification, characterization, and comparison of the enzymes from Pseudomonas testosteroni and Pseudomonas acidovorans.J. Biol. Chem.265199063016311","journal-title":"J. Biol. Chem."},{"key":"e_1_3_1_15_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(18)45688-8"},{"key":"e_1_3_1_16_2","doi-asserted-by":"crossref","first-page":"8332","DOI":"10.1074\/jbc.273.14.8332","article-title":"Biochemical and molecular characterization of 1-hydroxy-2-naphthoate dioxygenase from Nocardioides sp. KP7","volume":"273","author":"Iwabuchi T.","year":"1998","unstructured":"Iwabuchi T. Harayama S. Biochemical and molecular characterization of 1-hydroxy-2-naphthoate dioxygenase from Nocardioides sp. KP7.J. Biol. Chem.273199883328336","journal-title":"J. Biol. Chem."},{"key":"e_1_3_1_17_2","doi-asserted-by":"crossref","first-page":"887","DOI":"10.1099\/00207713-49-2-887","article-title":"Description of Pseudaminobacter gen. nov. with two new species, Pseudaminobacter salicylatoxidans sp. nov. and Pseudaminobacter defluvii sp. nov","volume":"49","author":"K\u00e4mpfer P.","year":"1999","unstructured":"K\u00e4mpfer P. M\u00fcller C. Mau M. Neef A. Auling G. Busse H.-J. Osborn A. M. Stolz A. Description of Pseudaminobacter gen. nov. with two new species, Pseudaminobacter salicylatoxidans sp. nov. and Pseudaminobacter defluvii sp. nov.Int. J. Syst. Bacteriol.491999887897","journal-title":"Int. J. Syst. Bacteriol."},{"key":"e_1_3_1_18_2","first-page":"705","article-title":"Enzymatic conversion of 1-hydroxy-2-naphthoate in phenanthrene-grown Aeromonas sp. S45P1","volume":"41","author":"Kiyohara H.","year":"1977","unstructured":"Kiyohara H. Nakao K. Enzymatic conversion of 1-hydroxy-2-naphthoate in phenanthrene-grown Aeromonas sp. S45P1.Agric. Biol. Chem.411977705707","journal-title":"Agric. Biol. Chem."},{"key":"e_1_3_1_19_2","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1099\/00221287-105-1-69","article-title":"The catabolism of phenanthrene and naphthalene by bacteria","volume":"105","author":"Kiyohara H.","year":"1978","unstructured":"Kiyohara H. Nakao K. The catabolism of phenanthrene and naphthalene by bacteria.J. Gen. Microbiol.10519786975","journal-title":"J. Gen. Microbiol."},{"key":"e_1_3_1_20_2","doi-asserted-by":"publisher","DOI":"10.1128\/jb.173.12.3795-3802.1991"},{"key":"e_1_3_1_21_2","doi-asserted-by":"crossref","first-page":"9484","DOI":"10.1016\/S0021-9258(18)98376-6","article-title":"Purification and properties of 2\u2032-hydroxybenzalpyruvate aldolase from a bacterium that degrades naphthalenesulfonates","volume":"268","author":"Kuhm A. E.","year":"1993","unstructured":"Kuhm A. E. Knackmuss H.-J. Stolz A. Purification and properties of 2\u2032-hydroxybenzalpyruvate aldolase from a bacterium that degrades naphthalenesulfonates.J. Biol. Chem.268199394849489","journal-title":"J. Biol. Chem."},{"key":"e_1_3_1_22_2","doi-asserted-by":"crossref","first-page":"155","DOI":"10.1007\/BF00695117","article-title":"2-Hydroxychromene-2-carboxylate isomerase from bacteria that degrade naphthalenesulfonates","volume":"4","author":"Kuhm A. E.","year":"1993","unstructured":"Kuhm A. E. Knackmuss H.-J. Stolz A. 2-Hydroxychromene-2-carboxylate isomerase from bacteria that degrade naphthalenesulfonates.Biodegradation41993155162","journal-title":"Biodegradation"},{"key":"e_1_3_1_23_2","doi-asserted-by":"crossref","first-page":"680","DOI":"10.1038\/227680a0","article-title":"Cleavage of structural proteins during the assembly of the head of bacteriophage T4","volume":"227","author":"Laemmli U. K.","year":"1970","unstructured":"Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4.Nature (London)2271970680685","journal-title":"Nature (London)"},{"key":"e_1_3_1_24_2","doi-asserted-by":"crossref","first-page":"544","DOI":"10.1006\/bbrc.1996.0097","article-title":"Nucleotide sequence of salicylate hydroxylase gene and its 5\u2032-flanking region of Pseudomonas putida KF715","volume":"218","author":"Lee J.","year":"1996","unstructured":"Lee J. Oh J. Min K. R. Kim Y. Nucleotide sequence of salicylate hydroxylase gene and its 5\u2032-flanking region of Pseudomonas putida KF715.Biochem. Biophys. Res. Commun.2181996544548","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"e_1_3_1_25_2","doi-asserted-by":"publisher","DOI":"10.1128\/jb.178.21.6227-6232.1996"},{"key":"e_1_3_1_26_2","unstructured":"N\u00f6rtemann\nB.\nBakterieller Abbau von Amino- und Hydroxynaphthalin-sulfons\u00e4uren. Thesis.\n1987\nUniversity of Stuttgart\nStuttgart Germany"},{"key":"e_1_3_1_27_2","doi-asserted-by":"publisher","DOI":"10.1128\/aem.52.5.1195-1202.1986"},{"key":"e_1_3_1_28_2","doi-asserted-by":"crossref","first-page":"320","DOI":"10.1007\/BF00303587","article-title":"Conversion of substituted naphthalenesulfonates by Pseudomonas sp. BN6","volume":"161","author":"N\u00f6rtemann B.","year":"1994","unstructured":"N\u00f6rtemann B. Kuhm A. E. Knackmuss H.-J. Stolz A. Conversion of substituted naphthalenesulfonates by Pseudomonas sp. BN6.Arch. Microbiol.1611994320327","journal-title":"Arch. Microbiol."},{"key":"e_1_3_1_29_2","first-page":"1419","article-title":"Degradation of 2-naphthylamine-1-sulfonic acid by Pseudomonas strain TA-1","volume":"50","author":"Ohe T.","year":"1986","unstructured":"Ohe T. Watanabe Y. Degradation of 2-naphthylamine-1-sulfonic acid by Pseudomonas strain TA-1.Agric. Biol. Chem.50198614191426","journal-title":"Agric. Biol. Chem."},{"key":"e_1_3_1_30_2","first-page":"2409","article-title":"Microbial degradation of 1,6- and 2,6-naphthalenedisulfonic acid by Pseudomonas sp. S-1","volume":"52","author":"Ohe T.","year":"1988","unstructured":"Ohe T. Watanabe Y. Microbial degradation of 1,6- and 2,6-naphthalenedisulfonic acid by Pseudomonas sp. S-1.Agric. Biol. Chem.52198824092414","journal-title":"Agric. Biol. Chem."},{"key":"e_1_3_1_31_2","first-page":"669","article-title":"Metabolism of naphthalenesulfonic acids by Pseudomonas sp. TA-2","volume":"54","author":"Ohe T.","year":"1990","unstructured":"Ohe T. Ohmoto T. Kobayashi Y. Sato A. Watanabe Y. Metabolism of naphthalenesulfonic acids by Pseudomonas sp. TA-2.Agric. Biol. Chem.541990669675","journal-title":"Agric. Biol. Chem."},{"key":"e_1_3_1_32_2","unstructured":"Rauscher\nK.\nVoigt\nJ.\nWilke\nI.\nWilke\nK.-T.\nChemische Tabellen und Rechentafeln f\u00fcr die analytische Praxis 7. \u00fcberarbeitete Auflage.\n1982\nVerlag Harri Deutsch\nThun Germany"},{"key":"e_1_3_1_33_2","doi-asserted-by":"crossref","first-page":"229","DOI":"10.1111\/j.1574-6968.1992.tb04814.x","article-title":"Total degradation of 6-aminonaphthalene-2-sulphonic acid by a mixed culture consisting of different bacterial genera","volume":"86","author":"Rozgaj R.","year":"1992","unstructured":"Rozgaj R. Glancer-\u00c4oljan M. Total degradation of 6-aminonaphthalene-2-sulphonic acid by a mixed culture consisting of different bacterial genera.FEMS Microbiol. Ecol.861992229235","journal-title":"FEMS Microbiol. Ecol."},{"key":"e_1_3_1_34_2","doi-asserted-by":"publisher","DOI":"10.1021\/ac950914h"},{"key":"e_1_3_1_35_2","first-page":"45","article-title":"Sulfonic acids","volume":"22","author":"Shultz A.","year":"1983","unstructured":"Shultz A. Sulfonic acids Kirk-Othmer encyclopedia of chemical technology 3rd ed. Grayson V. M. 22 1983 45 63 John Wiley & Sons New York, N.Y","journal-title":"Kirk-Othmer encyclopedia of chemical technology"},{"key":"e_1_3_1_36_2","doi-asserted-by":"crossref","first-page":"391","DOI":"10.1038\/sj.jim.2900725","article-title":"Degradation of substituted naphthalenesulfonic acids by Sphingomonas xenophaga BN6","volume":"23","author":"Stolz A.","year":"1999","unstructured":"Stolz A. Degradation of substituted naphthalenesulfonic acids by Sphingomonas xenophaga BN6.Int. J. Ind. Microbiol. Biotechnology231999391399","journal-title":"Int. J. Ind. Microbiol. Biotechnology"},{"key":"e_1_3_1_37_2","doi-asserted-by":"crossref","first-page":"219","DOI":"10.1111\/j.1574-6968.1993.tb06102.x","article-title":"Degradation of 2,4-dihydroxybenzoate by Pseudomonas sp. BN9","volume":"108","author":"Stolz A.","year":"1993","unstructured":"Stolz A. Knackmuss H.-J. Degradation of 2,4-dihydroxybenzoate by Pseudomonas sp. BN9.FEMS Microbiol. Lett.1081993219224","journal-title":"FEMS Microbiol. Lett."},{"key":"e_1_3_1_38_2","doi-asserted-by":"crossref","first-page":"675","DOI":"10.1042\/bj2820675","article-title":"Bacterial degradation of 5-aminosalicylic acid. Initial ring cleavage","volume":"282","author":"Stolz A.","year":"1992","unstructured":"Stolz A. N\u00f6rtemann B. Knackmuss H.-J. Bacterial degradation of 5-aminosalicylic acid. Initial ring cleavage.Biochem. J.2821992675680","journal-title":"Biochem. J."},{"key":"e_1_3_1_39_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1574-6968.1996.tb08466.x"},{"key":"e_1_3_1_40_2","doi-asserted-by":"crossref","first-page":"14727","DOI":"10.1074\/jbc.272.23.14727","article-title":"Novel genes encoding 2-aminophenol 1,6-dioxygenase from Pseudomonas species AP-3 growing on 2-aminophenol and catalytic properties of the purified enzyme","volume":"272","author":"Takenaka S.","year":"1997","unstructured":"Takenaka S. Murakami S. Shinke R. Hatakeyama K. Yukawa H. Aoki K. Novel genes encoding 2-aminophenol 1,6-dioxygenase from Pseudomonas species AP-3 growing on 2-aminophenol and catalytic properties of the purified enzyme.J. Biol. Chem.27219971472714732","journal-title":"J. Biol. Chem."},{"key":"e_1_3_1_41_2","doi-asserted-by":"publisher","DOI":"10.1128\/JB.180.16.4171-4176.1998"},{"key":"e_1_3_1_42_2","doi-asserted-by":"crossref","first-page":"302","DOI":"10.1007\/BF00406344","article-title":"The metabolism of aromatic acids by Pseudomonas testosteroni and P. acidovorans","volume":"59","author":"Wheelis M. L.","year":"1967","unstructured":"Wheelis M. L. Palleroni N. J. Stanier R. J. The metabolism of aromatic acids by Pseudomonas testosteroni and P. acidovorans.Arch. Mikrobiol.591967302314","journal-title":"Arch. Mikrobiol."},{"key":"e_1_3_1_43_2","first-page":"2358","article-title":"Studies of a flavoprotein, salicylate hydroxylase. I. Preparation, properties, and the uncoupling of oxygen reduction from hydroxylation","volume":"247","author":"White-Stevens R. H.","year":"1972","unstructured":"White-Stevens R. H. Kamin H. Studies of a flavoprotein, salicylate hydroxylase. I. Preparation, properties, and the uncoupling of oxygen reduction from hydroxylation.J. Biol. Chem.247197223582370","journal-title":"J. Biol. Chem."},{"key":"e_1_3_1_44_2","doi-asserted-by":"crossref","first-page":"3154","DOI":"10.1021\/ja00008a052","article-title":"Chemical and enzymatic ketonization of 2-hydroxymuconate, a conjugated enol","volume":"113","author":"Whitman C. P.","year":"1991","unstructured":"Whitman C. P. Aird B. A. Gillespie W. R. Stolowich N. J. Chemical and enzymatic ketonization of 2-hydroxymuconate, a conjugated enol.J. Am. Chem. Soc.113199131543162","journal-title":"J. Am. Chem. Soc."},{"key":"e_1_3_1_45_2","doi-asserted-by":"publisher","DOI":"10.1128\/aem.54.7.1842-1847.1988"},{"key":"e_1_3_1_46_2","doi-asserted-by":"crossref","first-page":"3408","DOI":"10.1016\/S0021-9258(18)97232-7","article-title":"Salicylate hydroxylase, a monooxygenase requiring flavin adenine dinucleotide","volume":"240","author":"Yamamoto S.","year":"1965","unstructured":"Yamamoto S. Katagiri M. Maeno H. Hayaishi O. Salicylate hydroxylase, a monooxygenase requiring flavin adenine dinucleotide.J. Biol. Chem.240196534083413","journal-title":"J. Biol. Chem."},{"key":"e_1_3_1_47_2","doi-asserted-by":"crossref","first-page":"1049","DOI":"10.1016\/0006-291X(90)92000-P","article-title":"Purification and characterization of salicylate hydroxylase from Pseudomonas putida PpG7","volume":"169","author":"You I.-S.","year":"1990","unstructured":"You I.-S. Murray R. I. Jollie D. Gunsalus I. C. Purification and characterization of salicylate hydroxylase from Pseudomonas putida PpG7.Biochem. Biophys. Res. Commun.169199010491054","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"e_1_3_1_48_2","doi-asserted-by":"publisher","DOI":"10.1128\/JB.183.2.700-708.2001"}],"container-title":["Journal of Bacteriology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/journals.asm.org\/doi\/pdf\/10.1128\/JB.183.23.6936-6942.2001","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/journals.asm.org\/doi\/pdf\/10.1128\/JB.183.23.6936-6942.2001","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,7,29]],"date-time":"2021-07-29T14:00:58Z","timestamp":1627567258000},"score":1,"resource":{"primary":{"URL":"https:\/\/journals.asm.org\/doi\/10.1128\/JB.183.23.6936-6942.2001"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2001,12]]},"references-count":47,"journal-issue":{"issue":"23","published-print":{"date-parts":[[2001,12]]}},"alternative-id":["10.1128\/JB.183.23.6936-6942.2001"],"URL":"https:\/\/doi.org\/10.1128\/jb.183.23.6936-6942.2001","relation":{},"ISSN":["0021-9193","1098-5530"],"issn-type":[{"value":"0021-9193","type":"print"},{"value":"1098-5530","type":"electronic"}],"subject":[],"published":{"date-parts":[[2001,12]]},"assertion":[{"value":"2001-06-08","order":0,"name":"received","label":"Received","group":{"name":"publication_history","label":"Publication History"}},{"value":"2001-09-10","order":1,"name":"accepted","label":"Accepted","group":{"name":"publication_history","label":"Publication History"}},{"value":"2020-12-20","order":2,"name":"published","label":"Published","group":{"name":"publication_history","label":"Publication History"}}]}}