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The\n                    <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">M. catarrhalis<\/jats:named-content>\n                    genome encodes a predicted truncated denitrification pathway that reduces nitrate to nitrous oxide. We have previously shown that expression of both the\n                    <jats:italic>M. catarrhalis aniA<\/jats:italic>\n                    (encoding a nitrite reductase) and\n                    <jats:italic>norB<\/jats:italic>\n                    (encoding a putative nitric oxide reductase) genes is repressed by the transcriptional regulator NsrR under aerobic conditions and that\n                    <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">M. catarrhalis<\/jats:named-content>\n                    O35E\n                    <jats:italic>nsrR<\/jats:italic>\n                    mutants are unable to grow in the presence of low concentrations of nitrite (W. Wang, et al., J. Bacteriol. 190:7762\u20137772, 2008). In this study, we constructed an\n                    <jats:italic>M. catarrhalis norB<\/jats:italic>\n                    mutant and showed that planktonic growth of this mutant is inhibited by low levels of nitrite, whether or not an\n                    <jats:italic>nsrR<\/jats:italic>\n                    mutation is present. To determine the importance of NorB in this truncated denitrification pathway, we analyzed the metabolism of nitrogen oxides by\n                    <jats:italic>norB<\/jats:italic>\n                    ,\n                    <jats:italic>aniA norB<\/jats:italic>\n                    , and\n                    <jats:italic>nsrR norB<\/jats:italic>\n                    mutants. We found that\n                    <jats:italic>norB<\/jats:italic>\n                    mutants are unable to reduce nitric oxide and produce little or no nitrous oxide from nitrite. Furthermore, nitric oxide produced from nitrite by the AniA protein is bactericidal for a\n                    <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Moraxella catarrhalis<\/jats:named-content>\n                    O35E\n                    <jats:italic>norB<\/jats:italic>\n                    mutant but not for wild-type O35E bacteria under aerobic growth conditions\n                    <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">in vitro<\/jats:named-content>\n                    , suggesting that nitric oxide catabolism in\n                    <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">M. catarrhalis<\/jats:named-content>\n                    is accomplished primarily by the\n                    <jats:italic>norB<\/jats:italic>\n                    gene product. Measurement of bacterial protein\n                    <jats:italic>S<\/jats:italic>\n                    -nitrosylation directly implicates nitrosative stress resulting from AniA-dependent nitric oxide formation as a cause of the growth inhibition of\n                    <jats:italic>norB<\/jats:italic>\n                    and\n                    <jats:italic>nsrR<\/jats:italic>\n                    mutants by nitrite.\n                  <\/jats:p>","DOI":"10.1128\/jb.00139-11","type":"journal-article","created":{"date-parts":[[2011,3,26]],"date-time":"2011-03-26T20:13:53Z","timestamp":1301170433000},"page":"2804-2813","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":24,"title":["The Moraxella catarrhalis Nitric Oxide Reductase Is Essential for Nitric Oxide Detoxification"],"prefix":"10.1128","volume":"193","author":[{"given":"Wei","family":"Wang","sequence":"first","affiliation":[{"name":"Department of Microbiology, University of Texas Southwestern Medical Center, Dallas, Texas 75390"},{"name":"Food and Drug Administration, Center for Biologics Evaluation and Research, Office of Vaccine Research and Review, Bethesda, Maryland 20892"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Traci","family":"Kinkel","sequence":"additional","affiliation":[{"name":"Departments of Laboratory Medicine, University of Washington, Seattle, Washington 98195"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Willm","family":"Martens-Habbena","sequence":"additional","affiliation":[{"name":"Civil and Environmental Engineering, University of Washington, Seattle, Washington 98195"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"David A.","family":"Stahl","sequence":"additional","affiliation":[{"name":"Civil and Environmental Engineering, University of Washington, Seattle, Washington 98195"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ferric C.","family":"Fang","sequence":"additional","affiliation":[{"name":"Departments of Laboratory Medicine, University of Washington, Seattle, Washington 98195"},{"name":"Microbiology, University of Washington, Seattle, Washington 98195"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Eric J.","family":"Hansen","sequence":"additional","affiliation":[{"name":"Department of Microbiology, University of Texas Southwestern Medical Center, Dallas, Texas 75390"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1128\/iai.64.6.2024-2030.1996"},{"key":"e_1_3_2_3_2","first-page":"321","article-title":"The effect of melatonin on lipid peroxidation and nitrite\/nitrate levels, and on superoxide dismutase and catalase activities in kainic acid-induced injury","volume":"10","author":"Akcay Y. 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