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Applied and Environmental Microbiology, July 2006, p. 5126-5131, Vol. 72, No. 7
0099-2240/06/$08.00+0 doi:10.1128/AEM.00437-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.
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Institute of Biochemistry and Molecular Biology,1 Institute of Organic Chemistry and Biochemistry, University of Freiburg, Freiburg, Germany2
Received 23 February 2006/ Accepted 4 May 2006
Two Arthrobacter nicotinovorans molybdenum enzymes hydroxylate the pyridine ring of nicotine. Molybdopterin cytosine dinucleotide (MCD) was determined to be a cofactor of these enzymes. A mobA gene responsible for the formation of MCD could be identified and its function shown to be required for assembly of the heterotrimeric molybdenum enzymes.
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