This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Mihasan, M.
Right arrow Articles by Brandsch, R.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Mihasan, M.
Right arrow Articles by Brandsch, R.
Agricola
Right arrow Articles by Mihasan, M.
Right arrow Articles by Brandsch, R.

 Previous Article  |  Next Article 

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.

An NAD(P)H-Nicotine Blue Oxidoreductase Is Part of the Nicotine Regulon and May Protect Arthrobacter nicotinovorans from Oxidative Stress during Nicotine Catabolism{triangledown}

Marius Mihasan,1,4 Calin-Bogdan Chiribau,1,3 Thorsten Friedrich,2 Vlad Artenie,4 and Roderich Brandsch1*

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.


* Corresponding author. Mailing address: Institute of Biochemistry and Molecular Biology, Hermann-Herder-Str. 7, 79104 Freiburg, Germany. Phone: 49-761-203-5231. Fax: 49-761-203-5253. E-mail: roderich.brandsch{at}biochemie.uni-freiburg.de

{triangledown} Published ahead of print on 9 February 2007.


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.