Degradation of nitrate ester and nitroaromatic explosives by Enterobacter cloacae PB2.

نویسندگان

  • A Basran
  • C E French
  • R E Williams
  • S Nicklin
  • N C Bruce
چکیده

and van Gorcom, R. F. M. (1996) Appl. Microbiol. Biotechnol. 46, 360-364 25 Panke, S., Sanchez-Romero, J. M. and de Lorenzo, V. (1998) Appl. Environ. Microbiol. 64, 748-751 26 Gouka, R. J., Punt, P. J. and van den Hondel, C. A. M. J. J. (1997) Appl. Microbiol. Biotechnol. 47,l-11 27 Davies, T. H., Cottingham, P. D. (1994) Water Sci. Technol. 29,227-235 28 Foyer, C. H., Descourvitxes, P. and Kunert, K. J. (1994) Plant Cell Environ. 17, 507-523 29 Daniell, H., Datta, R., Varma, S., Gray, S. and Lee, S.-B. (1998). Nat. Biotechnol. 16, 345-348 30 Steegborn, C. and Skliidal, P. (1996) Biosens. Bioelect. 12, 19-27 31 Wiseman, A. and Lynch, J. M. (1998) in Environmental Biomonitoring: The Biotechnology Ecotoxicology Interface (Lynch, J. M. and Wiseman, A., eds.), pp. 287-292, Cambridge University Press, Cambridge

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منابع مشابه

Two-electron reduction of nitroaromatic compounds by Enterobacter cloacae NAD(P)H nitroreductase: description of quantitative structure-activity relationships.

Enterobacter cloacae NAD(P)H:nitroreductase catalyzes the reduction of a series of nitroaromatic compounds with steady-state bimolecular rate constants (kcat/Km) ranging from 10(4) M(-1) s(-1) to 10(7) M(-1) s(-1), and oxidizing 2 moles NADH per mole mononitrocompound. Oxidation of excess NADH by polynitrobenzenes including explosives 2,4,6-trinitrotoluene (TNT) and 2,4,6-trinitrophenyl-N-methy...

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Degradation of explosives by nitrate ester reductases.

Explosive-contaminated land poses a hazard both to the environment and to human health. Microbial enzymes, either in their native or heterologous hosts, are a powerful and low-cost tool for eliminating this environmental hazard. As many explosives have only been present in the environment for 10 years, and with similar molecules not known in Nature, the origin of enzymes specialized for the bre...

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Quantitative structure-activity relationships in two-electron reduction of nitroaromatic compounds by Enterobacter cloacae NAD(P)H:nitroreductase.

Enterobacter cloacae NAD(P)H:nitroreductase (NR; EC 1.6.99.7) catalyzes the reduction of a series of nitroaromatic compounds with steady-state bimolecular rate constants (kcat/Km) ranging from 10(4) to 10(7) M(-1) s(-1). In agreement with a previously proposed scheme of two-step four-electron reduction of nitroaromatics by NR (Koder, R. L., and Miller, A.-F. (1998) Biochim. Biophys. Acta 1387, ...

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Aerobic degradation of 2,4,6-trinitrotoluene by Enterobacter cloacae PB2 and by pentaerythritol tetranitrate reductase.

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 ...

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Retro-nitroreductase, a putative evolutionary precursor to Enterobacter cloacae strain 96-3 nitroreductase.

Enterobacter cloacae strain 96-3 nitroreductase (NR) is a homodimeric flavoenzyme that catalyzes the pyridine nucleotide-dependent four-electron reduction of a variety of nitroaromatic compounds, including the explosives TNT (2,4,6-trinitrotoluene), RDX (1,3,5-trinitro-1,3,5-triazine), tetryl (2,4,6-trinitrophenyl-N-methylnitramine), and pentryl (2,4,6-trinitrophenyl-N-nitroaminoethylnitrate). ...

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عنوان ژورنال:
  • Biochemical Society transactions

دوره 26 4  شماره 

صفحات  -

تاریخ انتشار 1998