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An NAD(P)H-nicotine blue oxidoreductase is part of the nicotine regulon and may protect Arthrobacter nicotinovorans from oxidative stress during nicotine catabolism

Article Abstract:

Transcriptional analysis and electronmobility shift assays have shown that the enzyme gene is expressed in a nicotine-dependent manner under the control of the transcriptional activator PmfR and hence a part of the nicotine regulon Arthrobacter nicotinovorans. The NAD(P)H-nicotine blue (quinone) oxidoreductase has prevented intracellular one-electron reductions of nicotine blue, leading to semiquinone radicals and potentially toxic reactive oxygen species.

Author: Friedrich, Thorsten, Chiribau, Calin-Bogdan, Brandsch, Roderich, Mihasan, Marius, Artenie, Vlad
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 2007
Analysis, Oxidoreductases, Quinone, Quinones, Oxidative stress

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Plasmids for nicotine-dependent and -independent gene expression in Arthrobacter nicotinovorans and other Arthrobacter species

Article Abstract:

The first inducible Arthrobacter overexpression systems is described based on the promoter/operator and the repressor of the 6-hydroxynicotine oxidase gene of Arthrobacter nicotinovorans and nicotine-dependent overproduction and affinity purification of recombinant proteins are presented. The system allows the production of complex enzymes and genetic complementation analysis in Arthrobacter species.

Author: Sandu, Cristinel, Chiribau, Calin-Bogdan, Sachelaru, Paula, Brandsch, Roderich
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 2005
Science & research, Research, Genetic aspects, Genetic regulation, Gram-positive bacteria, Nicotinic receptors, Chemical properties

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Catabolism of arylboronic acids by arthrobacter nicotinovorans strain PBA

Article Abstract:

Research demonstrates metabolic conversion of phenylboronic acid to phenol by Arthrobacter sp. strain PBA. The bacterium can also transform other arylboronic acids to monooxygenated products. Data indicate that the oxygen atom in the products is bound to the ring carbon atom previously bearing boronic acid substituent.

Author: Wackett, Lawrence P., Negrete-Raymond, Ana C., Weder, Barbara
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 2003
United States, Physiological aspects, Microbial metabolism, Microbiological synthesis, Catabolism

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