{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,7,28]],"date-time":"2025-07-28T21:45:59Z","timestamp":1753739159590},"reference-count":31,"publisher":"American Society for Microbiology","issue":"8","license":[{"start":{"date-parts":[[2008,4,15]],"date-time":"2008-04-15T00:00:00Z","timestamp":1208217600000},"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":[[2008,4,15]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            <jats:italic>Pseudomonas butanovora<\/jats:italic>\n            possesses an alcohol-inducible alkane monooxygenase, butane monooxygenase (BMO), that initiates growth on C\n            <jats:sub>2<\/jats:sub>\n            -C\n            <jats:sub>9<\/jats:sub>\n            alkanes. A\n            <jats:italic>lacZ<\/jats:italic>\n            transcriptional reporter strain,\n            <jats:italic>P. butanovora bmoX<\/jats:italic>\n            ::\n            <jats:italic>lacZ<\/jats:italic>\n            , in which the BMO promoter controls the expression of \u03b2-galactosidase activity, was used to show that 1-butanol induced the BMO promoter in the presence or absence of O\n            <jats:sub>2<\/jats:sub>\n            when lactate-grown, BMO-repressed cells were washed free of lactate and incubated in NH\n            <jats:sub>4<\/jats:sub>\n            Cl-KNa phosphate buffer. In contrast, when lactate-grown cells of the reporter strain were incubated in phosphate buffer containing the mineral salts of standard growth medium, 1-butanol-dependent induction was significantly repressed at low O\n            <jats:sub>2<\/jats:sub>\n            (1 to 2% [vol\/vol]) and totally repressed under anoxic conditions. The repressive effect of the mineral salts was traced to its copper content. In cells exposed to 1% (vol\/vol) O\n            <jats:sub>2<\/jats:sub>\n            , CuSO\n            <jats:sub>4<\/jats:sub>\n            (0.5 \u03bcM) repressed 1-butanol-dependent induction of \u03b2-galactosidase activity. Under oxic conditions (20% O\n            <jats:sub>2<\/jats:sub>\n            [vol\/vol]), significantly higher concentrations of CuSO\n            <jats:sub>4<\/jats:sub>\n            (2 \u03bcM) were required for almost complete repression of induction in lactate-grown cells. A combination of the Cu\n            <jats:sup>2+<\/jats:sup>\n            reducing agent Na ascorbate (100 \u03bcM) and CuSO\n            <jats:sub>4<\/jats:sub>\n            (0.5 \u03bcM) repressed the induction of \u03b2-galactosidase activity under oxic conditions to the same extent that 0.5 \u03bcM CuSO\n            <jats:sub>4<\/jats:sub>\n            alone repressed it under anoxic conditions. Under oxic conditions, 2 \u03bcM CuSO\n            <jats:sub>4<\/jats:sub>\n            repressed induction of the BMO promoter less effectively in butyrate-grown cells of the\n            <jats:italic>bmoX<\/jats:italic>\n            ::\n            <jats:italic>lacZ<\/jats:italic>\n            strain and of an R8-\n            <jats:italic>bmoX<\/jats:italic>\n            ::\n            <jats:italic>lacZ<\/jats:italic>\n            mutant reporter strain with a putative BMO regulator, BmoR, inactivated. Under anoxic conditions, CuSO\n            <jats:sub>4<\/jats:sub>\n            repression remained highly effective, regardless of the growth substrate, in both BmoR-positive and -negative reporter strains.\n          <\/jats:p>","DOI":"10.1128\/jb.01409-07","type":"journal-article","created":{"date-parts":[[2008,2,16]],"date-time":"2008-02-16T02:05:25Z","timestamp":1203127525000},"page":"2933-2938","update-policy":"http:\/\/dx.doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":4,"title":["Evidence for Involvement of Copper Ions and Redox State in Regulation of Butane Monooxygenase in\n            <i>Pseudomonas butanovora<\/i>"],"prefix":"10.1128","volume":"190","author":[{"given":"D. M.","family":"Doughty","sequence":"first","affiliation":[{"name":"Department of Microbiology"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"E. G.","family":"Kurth","sequence":"additional","affiliation":[{"name":"Department of Botany and Plant Pathology"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"L. A.","family":"Sayavedra-Soto","sequence":"additional","affiliation":[{"name":"Department of Botany and Plant Pathology"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"D. J.","family":"Arp","sequence":"additional","affiliation":[{"name":"Department of Botany and Plant Pathology"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"P. J.","family":"Bottomley","sequence":"additional","affiliation":[{"name":"Department of Microbiology"},{"name":"Department of Crop and Soil Science, Oregon State University, Corvallis, Oregon 97331-3804"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1099\/00207713-50-4-1563"},{"key":"e_1_3_2_3_2","doi-asserted-by":"crossref","first-page":"1442","DOI":"10.1021\/bi051815t","volume":"45","year":"2006","unstructured":"Choi, D. W., C. J. Zea, Y. S. Do, J. D. Semrau, W. E. Antholine, M. S. Hargrove, N. L. Pohl, E. S. Boyd, G. G. Geesey, S. C. Hartsel, P. H. Shafe, M. T. McEllistrem, C. J. Kisting, D. Campbell, V. Rao, A. M. de la Mora, and A. A. DiSpirito. 2006. Spectral, kinetic, and thermodynamic properties of Cu(I) and Cu(II) binding by methanobactin from Methylosinus trichosporium OB3b. Biochemistry 45 : 1442-1453.","journal-title":"Biochemistry"},{"key":"e_1_3_2_4_2","doi-asserted-by":"crossref","first-page":"1228","DOI":"10.1111\/j.1462-2920.2006.01015.x","volume":"8","year":"2006","unstructured":"Coleman, N. V., N. B. Bui, and A. J. Holmes. 2006. Soluble di-iron monooxygenase gene diversity in soils, sediments, and ethene enrichments. Environ. Microbiol. 8 : 1228-1239.","journal-title":"Environ. Microbiol."},{"key":"e_1_3_2_5_2","doi-asserted-by":"crossref","first-page":"1785","DOI":"10.1099\/mic.0.26061-0","volume":"149","year":"2003","unstructured":"Csaki, R., L. Bodrossy, J. Klem, J. C. Murrell, and K. L. Kovacs. 2003. Genes involved in the copper-dependent regulation of soluble methane monooxygenase of Methylococcus capsulatus (Bath): cloning, sequencing and mutational analysis. Microbiology 149 : 1785-1795.","journal-title":"Microbiology"},{"key":"e_1_3_2_6_2","doi-asserted-by":"crossref","first-page":"371","DOI":"10.1007\/s002030050585","volume":"169","year":"1998","unstructured":"Dixon, R. 1998. The oxygen-responsive NifL-NifA complex: a novel two-component regulatory system controlling nitrogenase synthesis in gamma-proteobacteria. Arch. Microbiol. 169 : 371-380.","journal-title":"Arch. Microbiol."},{"key":"e_1_3_2_7_2","doi-asserted-by":"crossref","first-page":"3722","DOI":"10.1099\/mic.0.2007\/008441-0","volume":"153","year":"2007","unstructured":"Doughty, D. M., K. H. Halsey, L. A. Sayavedra-Soto, D. J. Arp, and P. J. Bottomley. 2007. Alkane monooxygenase inactivation by propionate in Pseudomonas butanovora; physiological and biochemical implications. Microbiology 153 : 3722-3729.","journal-title":"Microbiology"},{"key":"e_1_3_2_8_2","doi-asserted-by":"publisher","DOI":"10.1128\/AEM.71.10.6054-6059.2005"},{"key":"e_1_3_2_9_2","doi-asserted-by":"publisher","DOI":"10.1128\/JB.188.7.2586-2592.2006"},{"key":"e_1_3_2_10_2","doi-asserted-by":"crossref","first-page":"2314","DOI":"10.1126\/science.1059361","volume":"292","year":"2001","unstructured":"Georgellis, D., O. Kwon, and E. C. Lin. 2001. Quinones as the redox signal for the Arc two-component system of bacteria. Science 292 : 2314-2316.","journal-title":"Science"},{"key":"e_1_3_2_11_2","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/S0065-2911(08)60129-0","volume":"40","year":"1998","unstructured":"Goodwin, M. G., and C. Anthony. 1998. The biochemistry, physiology, and genetics of P and P containing enzymes. Adv. Microb. Physiol. 40 : 1-80.","journal-title":"Adv. Microb. Physiol."},{"key":"e_1_3_2_12_2","first-page":"18.1","volume":"76","year":"2007","unstructured":"Hakemian, A. S., and A. C. Rosenzweig. 2007. The biochemistry of methane oxidation. Annu. Rev. Microbiol. 76 : 18.1-18.19.","journal-title":"Annu. Rev. Microbiol."},{"key":"e_1_3_2_13_2","doi-asserted-by":"crossref","first-page":"17142","DOI":"10.1021\/ja0558140","volume":"127","year":"2005","unstructured":"Hakemian, A. S., C. E. Tinberg, K. C. Kondapalli, J. Telser, B. M. Hoffman, T. L. Stemmler, and A. C. Rosenzweig. 2005. The copper chelator methanobactin from Methylosinus trichosporium OB3b binds copper(I). J. Am. Chem. Soc. 127 : 17142-17143.","journal-title":"J. Am. Chem. Soc."},{"key":"e_1_3_2_14_2","doi-asserted-by":"publisher","DOI":"10.1128\/JB.00280-06"},{"key":"e_1_3_2_15_2","doi-asserted-by":"crossref","first-page":"3614","DOI":"10.1021\/bi0620407","volume":"46","year":"2007","unstructured":"Key, J., M. Hefti, E. B. Purcell, and K. Moffat. 2007. Structure of the redox sensor domain of Azotobacter vinelandii NifL at atomic resolution: signaling, dimerization, and mechanism. Biochemistry 46 : 3614-3623.","journal-title":"Biochemistry"},{"key":"e_1_3_2_16_2","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1099\/mic.0.2007\/012724-0","volume":"154","year":"2008","unstructured":"Kurth, E. G., D. M. Doughty, P. J. Bottomley, D. J. Arp, and L. A. Sayavedra-Soto. 2008. Involvement of BmoR and BmoG in n-alkane metabolism in Pseudomonas butanovora. Microbiology 154 : 139-147.","journal-title":"Microbiology"},{"key":"e_1_3_2_17_2","doi-asserted-by":"crossref","first-page":"1731","DOI":"10.1111\/j.1365-2958.2004.04089.x","volume":"52","year":"2004","unstructured":"Martinez-Argudo, I., R. Little, and R. Dixon. 2004. Role of the amino-terminal GAF domain of the NifA activator in controlling the response to the antiactivator protein NifL. Mol. Microbiol. 52 : 1731-1744.","journal-title":"Mol. Microbiol."},{"key":"e_1_3_2_18_2","doi-asserted-by":"crossref","first-page":"6111","DOI":"10.1021\/bi990121f","volume":"38","year":"1999","unstructured":"Matsushita, K., T. Yamashita, N. Aoki, H. Toyama, and O. Adachi. 1999. Electron transfer from quinohemoprotein alcohol dehydrogenase to blue copper protein azurin in the alcohol oxidase respiratory chain of Pseudomonas putida HK5. Biochemistry 38 : 6111-6118.","journal-title":"Biochemistry"},{"key":"e_1_3_2_19_2","doi-asserted-by":"crossref","first-page":"970","DOI":"10.1021\/ed076p970","volume":"76","year":"1999","unstructured":"Mowry, S., and P. J. Ogren. 1999. Kinetics of methylene blue reduction by ascorbic acid. J. Chem. Edu. 76 : 970.","journal-title":"J. Chem. Edu."},{"key":"e_1_3_2_20_2","doi-asserted-by":"crossref","first-page":"221","DOI":"10.1016\/S0966-842X(00)01739-X","volume":"8","year":"2000","unstructured":"Murrell, J. C., I. R. McDonald, and B. Gilbert. 2000. Regulation of expression of methane monooxygenases by copper ions. Trends Microbiol. 8 : 221-225.","journal-title":"Trends Microbiol."},{"key":"e_1_3_2_21_2","doi-asserted-by":"crossref","first-page":"831","DOI":"10.1007\/s00775-003-0481-4","volume":"8","year":"2003","unstructured":"Palacios, S., K. Polec-Pawlak, R. Lobinski, M. Capdevila, and P. Gonzalez-Duarte. 2003. Is Ag(I) an adequate probe for Cu(I) in structural copper-metallothionein studies? The binding features of Ag(I) to mammalian metallothionein 1. J. Biol. Inorg. Chem. 8 : 831-842.","journal-title":"J. Biol. Inorg. Chem."},{"key":"e_1_3_2_22_2","doi-asserted-by":"crossref","first-page":"11230","DOI":"10.1074\/jbc.M700728200","volume":"282","year":"2007","unstructured":"Partridge, J. D., G. Sanguinetti, D. P. Dibden, R. E. Roberts, R. K. Poole, and J. Green. 2007. Transition of Escherichia coli from aerobic to micro-aerobic conditions involves fast and slow reacting regulatory components. J. Biol. Chem. 282 : 11230-11237.","journal-title":"J. Biol. Chem."},{"key":"e_1_3_2_23_2","first-page":"155","volume":"131","year":"1985","unstructured":"Prior, S. D., and H. Dalton. 1985. The effect of copper ions on membrane content and methane monooxygenase activity in methanol-grown cells of Methylococcus capsulatus (Bath). J. Gen. Microbiol. 131 : 155-163.","journal-title":"J. Gen. Microbiol."},{"key":"e_1_3_2_24_2","doi-asserted-by":"crossref","first-page":"114","DOI":"10.1007\/s002030100304","volume":"176","year":"2001","unstructured":"Sayavedra-Soto, L. A., C. M. Byrd, and D. J. Arp. 2001. Induction of butane consumption in Pseudomonas butanovora. Arch. Microbiol. 176 : 114-120.","journal-title":"Arch. Microbiol."},{"key":"e_1_3_2_25_2","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1016\/j.femsle.2005.06.058","volume":"250","year":"2005","unstructured":"Sayavedra-Soto, L. A., D. M. Doughty, E. G. Kurth, P. J. Bottomley, and D. J. Arp. 2005. Product and product-independent induction of butane oxidation in Pseudomonas butanovora. FEMS Microbiol. Lett. 250 : 111-116.","journal-title":"FEMS Microbiol. Lett."},{"key":"e_1_3_2_26_2","doi-asserted-by":"publisher","DOI":"10.1128\/JB.00240-07"},{"key":"e_1_3_2_27_2","doi-asserted-by":"crossref","first-page":"3617","DOI":"10.1099\/00221287-148-11-3617","volume":"148","year":"2002","unstructured":"Sluis, M. K., L. A. Sayavedra-Soto, and D. J. Arp. 2002. Molecular analysis of the soluble butane monooxygenase from \u2018Pseudomonas butanovora\u2019. Microbiology 148 : 3617-3629.","journal-title":"Microbiology"},{"key":"e_1_3_2_28_2","first-page":"1835","volume":"44","year":"1980","unstructured":"Takahashi, J., Y. Ichikawa, H. Sagae, I. Komura, H. Kanou, and K. Yamada. 1980. Isolation and identification of n-butane-assimilating bacterium. Agric. Biol. Chem. 44 : 1835-1840.","journal-title":"Agric. Biol. Chem."},{"key":"e_1_3_2_29_2","doi-asserted-by":"crossref","first-page":"10191","DOI":"10.1021\/bi060693h","volume":"45","year":"2006","unstructured":"Ukaegbu, U. E., S. Henery, and A. C. Rosenzweig. 2006. Biochemical characterization of MmoS, a sensor protein involved in copper-dependent regulation of soluble methane monooxygenase. Biochemistry 45 : 10191-10198.","journal-title":"Biochemistry"},{"key":"e_1_3_2_30_2","doi-asserted-by":"publisher","DOI":"10.1128\/JB.184.7.1916-1924.2002"},{"key":"e_1_3_2_31_2","first-page":"1333","volume":"15","year":"2002","unstructured":"Zhu, B. Z., W. E. Antholine, and B. Frei. 2002. Thiourea protects against copper-induced oxidative damage by formation of a redox-inactive thiourea-copper complex. Free Radic. Biol. Med. 15 : 1333-1338.","journal-title":"Free Radic. Biol. Med."},{"key":"e_1_3_2_32_2","doi-asserted-by":"publisher","DOI":"10.1128\/mmbr.61.4.533-616.1997"}],"container-title":["Journal of Bacteriology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/journals.asm.org\/doi\/pdf\/10.1128\/JB.01409-07","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/journals.asm.org\/doi\/pdf\/10.1128\/JB.01409-07","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,7,29]],"date-time":"2021-07-29T17:45:13Z","timestamp":1627580713000},"score":1,"resource":{"primary":{"URL":"https:\/\/journals.asm.org\/doi\/10.1128\/JB.01409-07"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2008,4,15]]},"references-count":31,"journal-issue":{"issue":"8","published-print":{"date-parts":[[2008,4,15]]}},"alternative-id":["10.1128\/JB.01409-07"],"URL":"https:\/\/doi.org\/10.1128\/jb.01409-07","relation":{},"ISSN":["0021-9193","1098-5530"],"issn-type":[{"value":"0021-9193","type":"print"},{"value":"1098-5530","type":"electronic"}],"subject":[],"published":{"date-parts":[[2008,4,15]]},"assertion":[{"value":"2007-08-30","order":0,"name":"received","label":"Received","group":{"name":"publication_history","label":"Publication History"}},{"value":"2008-02-05","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"}}]}}