{"id":5246,"date":"2015-06-27T05:58:59","date_gmt":"2015-06-27T05:58:59","guid":{"rendered":"https:\/\/mycor.iam.inrae.fr\/IAM\/?p=5246"},"modified":"2015-06-27T05:59:41","modified_gmt":"2015-06-27T05:59:41","slug":"article-acta-biochimica-polonica","status":"publish","type":"post","link":"https:\/\/mycor.iam.inrae.fr\/IAM\/?p=5246","title":{"rendered":"Article: Acta biochimica Polonica"},"content":{"rendered":"<p><a class=\"gsc_a_at\" href=\"http:\/\/www.actabp.pl\/pdf\/Preprint\/2015_1003.pdf\">Quinone-and nitroreductase reactions of Thermotoga maritima thioredoxin reductase.<\/a>\u00a0B Valiauga, N Rouhier, JP Jacquot, N \u010c\u0117nas. Acta biochimica Polonica<\/p>\n<h1>Abstract<\/h1>\n<div class=\"\">\n<p style=\"text-align: justify;\">The Thermotoga maritima NADH:thioredoxin reductase (TmTR) contains FAD and a catalytic disulfide in the active center, and uses a relatively poorly studied physiological oxidant Grx-1-type glutaredoxin. In order to further assess the redox properties of TmTR, we used series of quinoidal and nitroaromatic oxidants with a wide range of single-electron reduction potentials (E17, -0.49-0.09 V). We found that TmTR catalyzed the mixed single- and two-electron reduction of quinones and nitroaromatic compounds, which was much faster than the reduction of Grx-1. The reactivity of both groups of oxidants increased with an increase in their E17, thus pointing to the absence of their structural specificity. The maximal rates of quinone reduction in the steady-state reactions were lower than the maximal rates of reduction of FAD by NADH, obtained in presteady-state experiments. The mixed-type reaction inhibition by NAD+\u00a0was consistent with its competition for a NADH binding site in the oxidized enzyme form, and also with the reoxidation of the reduced enzyme form. The inhibition data yielded a value of the standard potential for TmTR of -0.31\u00b10.03 V at pH 7.0, which may correspond to the FAD\/FADH2\u00a0redox couple. Overall, the mechanism of quinone- and nitroreductase reactions of T. maritima TR was similar to the previously described mechanism of Arabidopsis thaliana TR, and points to their prooxidant and possibly cytotoxic role.<\/p>\n<\/div>\n","protected":false},"excerpt":{"rendered":"<p>Quinone-and nitroreductase reactions of Thermotoga maritima thioredoxin reductase.\u00a0B Valiauga, N Rouhier, JP Jacquot, N \u010c\u0117nas. Acta biochimica Polonica Abstract The Thermotoga maritima NADH:thioredoxin reductase (TmTR) contains FAD and a catalytic disulfide in the active center, and uses a relatively poorly &hellip; <a href=\"https:\/\/mycor.iam.inrae.fr\/IAM\/?p=5246\">Continue reading <span class=\"meta-nav\">&rarr;<\/span><\/a><\/p>\n","protected":false},"author":2,"featured_media":0,"comment_status":"closed","ping_status":"open","sticky":false,"template":"","format":"standard","meta":{"footnotes":""},"categories":[2],"tags":[],"class_list":["post-5246","post","type-post","status-publish","format-standard","hentry","category-academic-productions"],"_links":{"self":[{"href":"https:\/\/mycor.iam.inrae.fr\/IAM\/index.php?rest_route=\/wp\/v2\/posts\/5246","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/mycor.iam.inrae.fr\/IAM\/index.php?rest_route=\/wp\/v2\/posts"}],"about":[{"href":"https:\/\/mycor.iam.inrae.fr\/IAM\/index.php?rest_route=\/wp\/v2\/types\/post"}],"author":[{"embeddable":true,"href":"https:\/\/mycor.iam.inrae.fr\/IAM\/index.php?rest_route=\/wp\/v2\/users\/2"}],"replies":[{"embeddable":true,"href":"https:\/\/mycor.iam.inrae.fr\/IAM\/index.php?rest_route=%2Fwp%2Fv2%2Fcomments&post=5246"}],"version-history":[{"count":0,"href":"https:\/\/mycor.iam.inrae.fr\/IAM\/index.php?rest_route=\/wp\/v2\/posts\/5246\/revisions"}],"wp:attachment":[{"href":"https:\/\/mycor.iam.inrae.fr\/IAM\/index.php?rest_route=%2Fwp%2Fv2%2Fmedia&parent=5246"}],"wp:term":[{"taxonomy":"category","embeddable":true,"href":"https:\/\/mycor.iam.inrae.fr\/IAM\/index.php?rest_route=%2Fwp%2Fv2%2Fcategories&post=5246"},{"taxonomy":"post_tag","embeddable":true,"href":"https:\/\/mycor.iam.inrae.fr\/IAM\/index.php?rest_route=%2Fwp%2Fv2%2Ftags&post=5246"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}