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Applied and Environmental Microbiology, April 2007, p. 2479-2485, Vol. 73, No. 8
0099-2240/07/$08.00+0 doi:10.1128/AEM.02668-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Institute for Biochemistry and Molecular Biology, Centre for Biochemistry and Molecular Cell Research,1 Institute of Organic Chemistry and Biochemistry, Albert Ludwigs University, Freiburg, Germany,2 Department of Medicine, Emory University School of Medicine, Atlanta, Georgia,3 Department of Molecular and Experimental Biology, Alexandru Ioan Cuza University, Iasi, Romania4
Received 15 November 2006/ Accepted 31 January 2007
An NAD(P)H-nicotine blue (quinone) oxidoreductase was discovered as a member of the nicotine catabolic pathway of Arthrobacter nicotinovorans. Transcriptional analysis and electromobility shift assays showed that the enzyme gene was expressed in a nicotine-dependent manner under the control of the transcriptional activator PmfR and thus was part of the nicotine regulon of A. nicotinovorans. The flavin mononucleotide-containing enzyme uses NADH and, with lower efficiency, NADPH to reduce, by a two-electron transfer, nicotine blue to the nicotine blue leuco form (hydroquinone). Besides nicotine blue, several other quinones were reduced by the enzyme. The NAD(P)H-nicotine blue oxidoreductase may prevent intracellular one-electron reductions of nicotine blue which may lead to semiquinone radicals and potentially toxic reactive oxygen species.
Published ahead of print on 9 February 2007.
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