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We addressed here the function of one of these genes,<jats:italic>ytjD<\/jats:italic>, which we renamed<jats:italic>cinD<\/jats:italic>(<jats:underline><jats:underline>c<\/jats:underline><\/jats:underline>opper-<jats:underline><jats:underline>i<\/jats:underline><\/jats:underline>nduced<jats:underline><jats:underline>n<\/jats:underline><\/jats:underline>itroreductase). Copper, cadmium, and silver induced<jats:italic>cinD in vivo<\/jats:italic>, as shown by real-time quantitative PCR. A knockout mutant of<jats:italic>cinD<\/jats:italic>was more sensitive to oxidative stress exerted by 4-nitroquinoline-<jats:italic>N<\/jats:italic>-oxide and copper. Purified CinD is a flavoprotein and reduced 2,6-dichlorophenolindophenol and 4-nitroquinoline-<jats:italic>N<\/jats:italic>-oxide with<jats:italic>k<\/jats:italic><jats:sub>cat<\/jats:sub>values of 27 and 11 s<jats:sup>\u22121<\/jats:sup>, respectively, using NADH as a reductant. CinD also exhibited significant catalase activity<jats:italic>in vitro<\/jats:italic>. The X-ray structure of CinD was resolved at 1.35 A\u030a and resembles those of other nitroreductases. CinD is thus a nitroreductase which can protect<jats:italic>L. lactis<\/jats:italic>against oxidative stress that could be exerted by nitroaromatic compounds and copper.<\/jats:p>","DOI":"10.1128\/jb.00372-10","type":"journal-article","created":{"date-parts":[[2010,6,21]],"date-time":"2010-06-21T00:23:18Z","timestamp":1277079798000},"page":"4172-4180","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":35,"title":["Structure and Function of CinD (YtjD) of<i>Lactococcus lactis<\/i>, a Copper-Induced Nitroreductase Involved in Defense against Oxidative Stress"],"prefix":"10.1128","volume":"192","author":[{"given":"Me\u0301lanie","family":"Mermod","sequence":"first","affiliation":[{"name":"Department of Clinical Pharmacology and Visceral Research"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Fre\u0301de\u0301ric","family":"Mourlane","sequence":"additional","affiliation":[{"name":"Department of Clinical Pharmacology and Visceral Research"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sandro","family":"Waltersperger","sequence":"additional","affiliation":[{"name":"Department of Chemistry and Biochemistry, University of Berne, 3010 Berne, Switzerland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anselm E.","family":"Oberholzer","sequence":"additional","affiliation":[{"name":"Department of Chemistry and Biochemistry, University of Berne, 3010 Berne, Switzerland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ulrich","family":"Baumann","sequence":"additional","affiliation":[{"name":"Department of Chemistry and Biochemistry, University of Berne, 3010 Berne, Switzerland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marc","family":"Solioz","sequence":"additional","affiliation":[{"name":"Department of Clinical Pharmacology and Visceral Research"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"crossref","first-page":"844","DOI":"10.1111\/j.1365-2958.2009.06699.x","volume":"72","year":"2009","unstructured":"Anjem, A., S. 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