{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,3]],"date-time":"2026-04-03T04:31:26Z","timestamp":1775190686727,"version":"3.50.1"},"reference-count":48,"publisher":"Proceedings of the National Academy of Sciences","issue":"9","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2002,4,30]]},"abstract":"<jats:p>\n            <jats:italic>Mycobacterium tuberculosis<\/jats:italic>\n            , the causative agent of human tuberculosis, and\n            <jats:italic>Mycobacterium<\/jats:italic>\n            <jats:italic>bovis<\/jats:italic>\n            each express two genes,\n            <jats:italic>glbN<\/jats:italic>\n            and\n            <jats:italic>glbO<\/jats:italic>\n            , encoding distantly related truncated hemoglobins (trHbs), trHbN and trHbO, respectively. Here we report that disruption of\n            <jats:italic>M. bovis<\/jats:italic>\n            bacillus Calmette\u2013Gu\u00e9rin\n            <jats:italic>glbN<\/jats:italic>\n            caused a dramatic reduction in the NO-consuming activity of stationary phase cells, and that activity could be restored fully by complementing knockout cells with\n            <jats:italic>glbN<\/jats:italic>\n            . Aerobic respiration of knockout cells was inhibited markedly by NO in comparison to that of wild-type cells, indicating a protective function for trHbN. TyrB10, which is highly conserved in trHbs and interacts with the bound oxygen, was found essential for NO consumption. Titration of oxygenated trHbN (trHbN\u22c5O\n            <jats:sub>2<\/jats:sub>\n            ) with NO resulted in stoichiometric oxidation of the protein with nitrate as the major product of the reaction. The second-order rate constant for the reaction between trHbN\u22c5O\n            <jats:sub>2<\/jats:sub>\n            and NO at 23\u00b0C was 745 \u03bcM\n            <jats:sup>\u22121<\/jats:sup>\n            \u22c5s\n            <jats:sup>\u22121<\/jats:sup>\n            , demonstrating that trHbN detoxifies NO 20-fold more rapidly than myoglobin. These results establish a role for a trHb and demonstrate an NO-metabolizing activity in\n            <jats:italic>M. tuberculosis<\/jats:italic>\n            or\n            <jats:italic>M. bovis<\/jats:italic>\n            . trHbN thus might play an important role in persistence of mycobacterial infection by virtue of trHbN\u2032s ability to detoxify NO.\n          <\/jats:p>","DOI":"10.1073\/pnas.092017799","type":"journal-article","created":{"date-parts":[[2002,7,28]],"date-time":"2002-07-28T22:26:28Z","timestamp":1027895188000},"page":"5902-5907","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":233,"title":["Truncated hemoglobin HbN protects\n            <i>Mycobacterium bovis<\/i>\n            from nitric oxide"],"prefix":"10.1073","volume":"99","author":[{"given":"Hugues","family":"Ouellet","sequence":"first","affiliation":[{"name":"Department of Biochemistry and Microbiology, Faculty of Sciences and Engineering, Laval University, QC, Canada G1K 7P4; 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