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- W1983003735 abstract "Analysis of the biochemical properties of the mutant chl C− of E. coli K12 has given evidence for a chlorate reductase activity independent of nitrate reductase A which is induced by KNO3 in this bacterium. This particulate enzyme is not sensitive to NaN3 or KNC, its Km with respect chlorate is 2.5·10−4 M. Reduced pyridine nucleotides cannot serve as electron donors. FMN (Km = 0.19 mM) and riboflavine (Km = 0.62 mM) are less effective electron donors than benzyl viologen (Km = 0.6·10−4 M). This chlorate reductase activity shows a number of analogies with the chlorate reductase C found in other Enterobacteriaceae. Repressed by NO3− and ClO3− in the mutant chlC−, it is absent in the pleiotropic mutants chl A− and chl B− of Escherichia coli K12 regardless of the culture conditions. It is probable that this enzyme acts as an electron barrier, integral to the multienzyme system that produces gaseous H2 during the fermentation of glucose. Thus, the pleiotropic mutation of chlorate-resistant mutants of E. coli K12 affects three different enzymatic activities: formate dehydrogenase, nitrate reductase, and chlorate reductase. L'analyse des propriétés biochimiques du mutant chl C− d'Escherichia coli K12 nous a permis de mattre en évidence une activit'e chlorate-réductase indépendante de la nitrate-réductase A induite par le KNO3 chez cette bactérie. Cette enzyme de nature particulaire est insensible au NaN3 et au KCN; son Km à l'égard du chlorate est égal à 2.5·10− M. Les pyridine-nucléotides réduites ne peuvent servir de donateurs d'électrons. Le FMN (Km = 0.19 mM) et al riboflavine (Km = 0.62 mM) sont des donateurs d'électrons moins efficaces que le benzyl-viologène (Km = 0.6·10− M). Cette activité présente de nombreuses analogies avec la chlorate-réductase C mise en évidence chez d'autres Entérobactériacées. Réprimée par le NO3− et le ClO3− chez le mutant chl C−, elle est absente des mutants pléiotropes chl A− et chl B− d'E. coli K12 quelles que soient les conditions de culture. Il est probable que cette enzyme fonctionne comme un transporteur d'électrons intégré dans le système multienzymatique qui assure la production d'H2 gazeux au cours de la fermentation du glucose. Ce qui étend l'effect de la mutation chlorate-résistance chez E. coli K12 à 3 activités enzymatiques à savoir, la formiate-déshydrogénase, la nitrate-réductase A et la chlorate-réductase C." @default.
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- W1983003735 date "1971-06-22" @default.
- W1983003735 modified "2023-09-25" @default.
- W1983003735 title "Etude des mutants chlorate-résistants chez Escherichia Coli K12 III. Mise en évidence et étude de l'activité chlorate-réductase c des mutants chl C−" @default.
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- W1983003735 doi "https://doi.org/10.1016/0304-4165(71)90278-9" @default.
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