{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,23]],"date-time":"2026-10-23T14:32:45Z","timestamp":1792765965822,"version":"4.5.0"},"reference-count":32,"publisher":"American Society for Microbiology","issue":"23","license":[{"start":{"date-parts":[[2007,12,1]],"date-time":"2007-12-01T00:00:00Z","timestamp":1196467200000},"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":["Appl Environ Microbiol"],"published-print":{"date-parts":[[2007,12]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            In the bacterial degradation of polycyclic aromatic hydrocarbons (PAHs), salicylate hydroxylases catalyze essential reactions at the junction between the so-called upper and lower catabolic pathways. Unlike the salicylate 1-hydroxylase from pseudomonads, which is a well-characterized flavoprotein, the enzyme found in sphingomonads appears to be a three-component Fe-S protein complex, which so far has not been characterized. Here, the salicylate 1-hydroxylase from\n            <jats:italic>Sphingomonas<\/jats:italic>\n            sp. strain CHY-1 was purified, and its biochemical and catalytic properties were characterized. The oxygenase component, designated PhnII, exhibited an \u03b1\n            <jats:sub>3<\/jats:sub>\n            \u03b2\n            <jats:sub>3<\/jats:sub>\n            heterohexameric structure and contained one Rieske-type [2Fe-2S] cluster and one mononuclear iron per \u03b1 subunit. In the presence of purified reductase (PhnA4) and ferredoxin (PhnA3) components, PhnII catalyzed the hydroxylation of salicylate to catechol with a maximal specific activity of 0.89 U\/mg and showed an apparent\n            <jats:italic>\n              K\n              <jats:sub>m<\/jats:sub>\n            <\/jats:italic>\n            for salicylate of 1.1 \u00b1 0.2 \u03bcM. The hydroxylase exhibited similar activity levels with methylsalicylates and low activity with salicylate analogues bearing additional hydroxyl or electron-withdrawing substituents. PhnII converted anthranilate to 2-aminophenol and exhibited a relatively low affinity for this substrate (\n            <jats:italic>\n              K\n              <jats:sub>m<\/jats:sub>\n            <\/jats:italic>\n            , 28 \u00b1 6 \u03bcM). 1-Hydroxy-2-naphthoate, which is an intermediate in phenanthrene degradation, was not hydroxylated by PhnII, but it induced a high rate of uncoupled oxidation of NADH. It also exerted strong competitive inhibition of salicylate hydroxylation, with a\n            <jats:italic>\n              K\n              <jats:sub>i<\/jats:sub>\n            <\/jats:italic>\n            of 0.68 \u03bcM. The properties of this three-component hydroxylase are compared with those of analogous bacterial hydroxylases and are discussed in light of our current knowledge of PAH degradation by sphingomonads.\n          <\/jats:p>","DOI":"10.1128\/aem.01519-07","type":"journal-article","created":{"date-parts":[[2007,9,29]],"date-time":"2007-09-29T01:04:31Z","timestamp":1191027871000},"page":"7515-7521","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":49,"title":["Purification and Characterization of a Three-Component Salicylate 1-Hydroxylase from\n            <i>Sphingomonas<\/i>\n            sp. Strain CHY-1"],"prefix":"10.1128","volume":"73","author":[{"given":"Yves","family":"Jouanneau","sequence":"first","affiliation":[{"name":"CEA, DSV, iRTSV, Laboratoire de Chimie et Biologie des Me\u0301taux, 17 rue des Martyrs, F-38054 Grenoble, CNRS, UMR 5249, F-38054 Grenoble, and Universite\u0301 Joseph Fourier, F-38000 Grenoble, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Julien","family":"Micoud","sequence":"additional","affiliation":[{"name":"CEA, DSV, iRTSV, Laboratoire de Chimie et Biologie des Me\u0301taux, 17 rue des Martyrs, F-38054 Grenoble, CNRS, UMR 5249, F-38054 Grenoble, and Universite\u0301 Joseph Fourier, F-38000 Grenoble, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christine","family":"Meyer","sequence":"additional","affiliation":[{"name":"CEA, DSV, iRTSV, Laboratoire de Chimie et Biologie des Me\u0301taux, 17 rue des Martyrs, F-38054 Grenoble, CNRS, UMR 5249, F-38054 Grenoble, and Universite\u0301 Joseph Fourier, F-38000 Grenoble, France"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1023\/A:1013126723719","volume":"12","year":"2001","unstructured":"Balashova, N. V., A. Stolz, H. J. Knackmuss, I. A. Kosheleva, A. V. Naumov, and A. M. Boronin. 2001. Purification and characterization of a salicylate hydroxylase involved in 1-hydroxy-2-naphthoic acid hydroxylation from the naphthalene- and phenanthrene-degrading bacterial strain Pseudomonas putida BS202-P1. Biodegradation12:179-188.","journal-title":"Biodegradation"},{"key":"e_1_3_2_3_2","doi-asserted-by":"publisher","DOI":"10.1016\/0039-9140(61)80006-4"},{"key":"e_1_3_2_4_2","doi-asserted-by":"publisher","DOI":"10.1128\/JB.181.8.2315-2322.1999"},{"key":"e_1_3_2_5_2","doi-asserted-by":"publisher","DOI":"10.1016\/0003-2697(76)90527-3"},{"key":"e_1_3_2_6_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0065-2911(08)60155-1"},{"key":"e_1_3_2_7_2","doi-asserted-by":"publisher","DOI":"10.1128\/JB.185.19.5871-5881.2003"},{"key":"e_1_3_2_8_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.bbrc.2004.12.060"},{"key":"e_1_3_2_9_2","doi-asserted-by":"publisher","DOI":"10.1016\/0378-1119(93)90533-9"},{"key":"e_1_3_2_10_2","doi-asserted-by":"publisher","DOI":"10.1128\/AEM.70.11.6714-6725.2004"},{"key":"e_1_3_2_11_2","doi-asserted-by":"publisher","DOI":"10.1128\/JB.183-1.109-118.2001"},{"key":"e_1_3_2_12_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.273.16.9622"},{"key":"e_1_3_2_13_2","doi-asserted-by":"publisher","DOI":"10.1128\/AEM.00395-06"},{"key":"e_1_3_2_14_2","doi-asserted-by":"publisher","DOI":"10.1021\/bi0611311"},{"key":"e_1_3_2_15_2","doi-asserted-by":"publisher","DOI":"10.1016\/0005-2728(95)00106-X"},{"key":"e_1_3_2_16_2","doi-asserted-by":"publisher","DOI":"10.1038\/sj.jim.2900724"},{"key":"e_1_3_2_17_2","doi-asserted-by":"publisher","DOI":"10.1128\/AEM.68.12.6021-6028.2002"},{"key":"e_1_3_2_18_2","doi-asserted-by":"publisher","DOI":"10.1128\/JB.181.9.2719-2725.1999"},{"key":"e_1_3_2_19_2","doi-asserted-by":"publisher","DOI":"10.1128\/AEM.70.4.1944-1955.2004"},{"key":"e_1_3_2_20_2","doi-asserted-by":"publisher","DOI":"10.1016\/0003-2697(78)90355-X"},{"key":"e_1_3_2_21_2","doi-asserted-by":"publisher","DOI":"10.2323\/jgam.49.1"},{"key":"e_1_3_2_22_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1574-6968.2000.tb09327.x"},{"key":"e_1_3_2_23_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0006-291X(02)03036-X"},{"key":"e_1_3_2_24_2","doi-asserted-by":"publisher","DOI":"10.1128\/JB.181.5.1585-1602.1999"},{"key":"e_1_3_2_25_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(19)45437-9"},{"key":"e_1_3_2_26_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.femsle.2004.10.012"},{"key":"e_1_3_2_27_2","doi-asserted-by":"publisher","DOI":"10.1128\/aem.58.3.1005-1010.1992"},{"key":"e_1_3_2_28_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M209604200"},{"key":"e_1_3_2_29_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M007795200"},{"key":"e_1_3_2_30_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(18)97232-7"},{"key":"e_1_3_2_31_2","doi-asserted-by":"publisher","DOI":"10.1021\/bi00220a028"},{"key":"e_1_3_2_32_2","doi-asserted-by":"publisher","DOI":"10.1128\/JB.184.6.1547-1555.2002"},{"key":"e_1_3_2_33_2","doi-asserted-by":"publisher","DOI":"10.1038\/sj.jim.2900475"}],"container-title":["Applied and Environmental Microbiology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/journals.asm.org\/doi\/pdf\/10.1128\/AEM.01519-07","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/journals.asm.org\/doi\/pdf\/10.1128\/AEM.01519-07","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,2,23]],"date-time":"2022-02-23T21:07:28Z","timestamp":1645650448000},"score":1,"resource":{"primary":{"URL":"https:\/\/journals.asm.org\/doi\/10.1128\/AEM.01519-07"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2007,12]]},"references-count":32,"journal-issue":{"issue":"23","published-print":{"date-parts":[[2007,12]]}},"alternative-id":["10.1128\/AEM.01519-07"],"URL":"https:\/\/doi.org\/10.1128\/aem.01519-07","relation":{},"ISSN":["0099-2240","1098-5336"],"issn-type":[{"value":"0099-2240","type":"print"},{"value":"1098-5336","type":"electronic"}],"subject":[],"published":{"date-parts":[[2007,12]]},"assertion":[{"value":"2007-07-05","order":0,"name":"received","label":"Received","group":{"name":"publication_history","label":"Publication History"}},{"value":"2007-09-19","order":1,"name":"accepted","label":"Accepted","group":{"name":"publication_history","label":"Publication History"}},{"value":"2007-12-01","order":2,"name":"published","label":"Published","group":{"name":"publication_history","label":"Publication History"}}]}}