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Applied and Environmental Microbiology, August 1998, p. 2864-2868, Vol. 64, No. 8
Institute of Biotechnology,
Received 17 February 1998/Accepted 2 June 1998
Enterobacter cloacae PB2 was originally isolated on the
basis of its ability to utilize nitrate esters, such as pentaerythritol tetranitrate (PETN) and glycerol trinitrate, as the sole nitrogen source for growth. The enzyme responsible is an NADPH-dependent reductase designated PETN reductase. E. cloacae PB2 was
found to be capable of slow aerobic growth with 2,4,6-trinitrotoluene (TNT) as the sole nitrogen source. Dinitrotoluenes were not produced and could not be used as nitrogen sources. Purified PETN reductase was
found to reduce TNT to its hydride-Meisenheimer complex, which was
further reduced to the dihydride-Meisenheimer complex. Purified PETN
reductase and recombinant Escherichia coli expressing PETN reductase were able to liberate nitrogen as nitrite from TNT. The
ability to remove nitrogen from TNT suggests that PB2 or recombinant organisms expressing PETN reductase may be useful for bioremediation of
TNT-contaminated soil and water.
0099-2240/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
Aerobic Degradation of 2,4,6-Trinitrotoluene by
Enterobacter cloacae PB2 and by Pentaerythritol
Tetranitrate Reductase

*
Corresponding author. Mailing address: Institute of
Biotechnology, University of Cambridge, Tennis Court Rd., Cambridge,
CB2 1QT, United Kingdom. Phone: 44 (0) 1223 334168. Fax: 44 (0) 1223 334162. E-mail: n.bruce{at}biotech.cam.ac.uk.
Present address: Institute of Cell and Molecular Biology,
University of Edinburgh, Edinburgh EH9 3JR, United Kingdom.
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