{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,7]],"date-time":"2026-10-07T02:30:06Z","timestamp":1791340206678,"version":"4.3.1"},"reference-count":66,"publisher":"American Society for Microbiology","issue":"24","license":[{"start":{"date-parts":[[2001,12,15]],"date-time":"2001-12-15T00:00:00Z","timestamp":1008374400000},"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":[[2001,12,15]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            The\n            <jats:italic>cydAB<\/jats:italic>\n            genes from\n            <jats:italic>Mycobacterium smegmatis<\/jats:italic>\n            have been cloned and characterized. The\n            <jats:italic>cydA<\/jats:italic>\n            and\n            <jats:italic>cydB<\/jats:italic>\n            genes encode the two subunits of a cytochrome\n            <jats:italic>bd<\/jats:italic>\n            oxidase belonging to the widely distributed family of quinol oxidases found in prokaryotes. The\n            <jats:italic>cydD<\/jats:italic>\n            and\n            <jats:italic>cydC<\/jats:italic>\n            genes located immediately downstream of\n            <jats:italic>cydB<\/jats:italic>\n            encode a putative ATP-binding cassette-type transporter. At room temperature, reduced minus oxidized difference spectra of membranes purified from wild-type\n            <jats:italic>M. smegmatis<\/jats:italic>\n            displayed spectral features that are characteristic of the \u03b3-proteobacterial type cytochrome\n            <jats:italic>bd<\/jats:italic>\n            oxidase. Inactivation of\n            <jats:italic>cydA<\/jats:italic>\n            or\n            <jats:italic>cydB<\/jats:italic>\n            by insertion of a kanamycin resistance marker resulted in loss of\n            <jats:italic>d-<\/jats:italic>\n            heme absorbance at 631 nm. The\n            <jats:italic>d<\/jats:italic>\n            -heme could be restored by transformation of the\n            <jats:italic>M. smegmatis cyd<\/jats:italic>\n            mutants with a replicating plasmid carrying the highly homologous\n            <jats:italic>cydABDC<\/jats:italic>\n            gene cluster from\n            <jats:italic>Mycobacterium tuberculosis<\/jats:italic>\n            . Inactivation of\n            <jats:italic>cydA<\/jats:italic>\n            had no effect on the ability of\n            <jats:italic>M. smegmatis<\/jats:italic>\n            to exit from stationary phase at 37 or 42\u00b0C. The growth rate of the\n            <jats:italic>cydA<\/jats:italic>\n            mutant was tested under oxystatic conditions. Although no discernible growth defect was observed under moderately aerobic conditions (9.2 to 37.5 \u00d7 10\n            <jats:sup>2<\/jats:sup>\n            Pa of pO\n            <jats:sub>2<\/jats:sub>\n            or 5 to 21% air saturation), the mutant displayed a significant growth disadvantage when cocultured with the wild type under extreme microaerophilia (0.8 to 1.7 \u00d7 10\n            <jats:sup>2<\/jats:sup>\n            Pa of pO\n            <jats:sub>2<\/jats:sub>\n            or 0.5 to 1% air saturation). These observations were in accordance with the two- to threefold increase in\n            <jats:italic>cydAB<\/jats:italic>\n            gene expression observed upon reduction of the pO\n            <jats:sub>2<\/jats:sub>\n            of the growth medium from 21 to 0.5% air saturation and with the concomitant increase in\n            <jats:italic>d<\/jats:italic>\n            -heme absorbance in spectra of membranes isolated from wild-type\n            <jats:italic>M. smegmatis<\/jats:italic>\n            cultured at 1% air saturation. Finally, the\n            <jats:italic>cydA<\/jats:italic>\n            mutant displayed a competitive growth disadvantage in the presence of the terminal oxidase inhibitor, cyanide, when cocultured with wild type at 21% air saturation in an oxystat. In conjunction with these findings, our results suggest that cytochrome\n            <jats:italic>bd<\/jats:italic>\n            is an important terminal oxidase in\n            <jats:italic>M. smegmatis.<\/jats:italic>\n          <\/jats:p>","DOI":"10.1128\/jb.183.24.7076-7086.2001","type":"journal-article","created":{"date-parts":[[2002,7,27]],"date-time":"2002-07-27T10:01:09Z","timestamp":1027764069000},"page":"7076-7086","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":151,"title":["Characterization of the\n            <i>cydAB<\/i>\n            -Encoded Cytochrome\n            <i>bd<\/i>\n            Oxidase from\n            <i>Mycobacterium smegmatis<\/i>"],"prefix":"10.1128","volume":"183","author":[{"given":"Bavesh D.","family":"Kana","sequence":"first","affiliation":[{"name":"<!--label omitted: 1-->MRC\/SAIMR\/WITS Molecular Mycobacteriology Research Unit, South African Institute for Medical Research,1 and"},{"name":"<!--label omitted: 2-->Department of Molecular Medicine and Hematology, School of Pathology, University of the Witwatersrand,2 Johannesburg, South Africa, and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Edward A.","family":"Weinstein","sequence":"additional","affiliation":[{"name":"<!--label omitted: 3-->Division of Infectious Diseases, University of Pennsylvania, Philadelphia, Pennsylvania3"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"David","family":"Avarbock","sequence":"additional","affiliation":[{"name":"<!--label omitted: 3-->Division of Infectious Diseases, University of Pennsylvania, Philadelphia, Pennsylvania3"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Stephanie S.","family":"Dawes","sequence":"additional","affiliation":[{"name":"<!--label omitted: 1-->MRC\/SAIMR\/WITS Molecular Mycobacteriology Research Unit, South African Institute for Medical Research,1 and"},{"name":"<!--label omitted: 2-->Department of Molecular Medicine and Hematology, School of Pathology, University of the Witwatersrand,2 Johannesburg, South Africa, and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Harvey","family":"Rubin","sequence":"additional","affiliation":[{"name":"<!--label omitted: 3-->Division of Infectious Diseases, University of Pennsylvania, Philadelphia, Pennsylvania3"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Valerie","family":"Mizrahi","sequence":"additional","affiliation":[{"name":"<!--label omitted: 1-->MRC\/SAIMR\/WITS Molecular Mycobacteriology Research Unit, South African Institute for Medical Research,1 and"},{"name":"<!--label omitted: 2-->Department of Molecular Medicine and Hematology, School of Pathology, University of the Witwatersrand,2 Johannesburg, South Africa, and"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","first-page":"4002","article-title":"Oxidative phosphorylation in fractionated bacterial systems. 18. 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