Reduction of the explosive 2,4,6-trinitrophenylmethylnitramine (tetryl) catalyzed by oxygen sensitive nitro reductase enzymes
- Tyndall Air Force Base, FL (United States)
Reduction of nitroaromatic compounds by nitroreductase enzymes generally leads to the formation of the corresponding amines. However, we recently found that the incubation of the explosive 2,4,6-trinitrophenylmethylnitramine (tetryl) with ferredoxin-NADP oxidoreductase, an oxygen sensitive nitroreductase from spinach in the presence of NADPH led to the elimination of the nitramine nitro group from tetryl and the formation of N-methylpicramide (NMP). Other oxygen sensitive nitroreductase enzymes including glutathione reductase, xanthine oxidase, and cytochrome c reductase were also able to release nitrite from tetryl. Nitrite was not eliminated from tetryl by an oxygen insensitive nitrobenzene reductase. For every mole of tetryl reduced, one mole each of nitrite and NMP were produced. The rate of nitrite elimination was inhibited under aerobic conditions. Subsequent oxygen uptake studies suggested that under aerobic conditions, molecular oxygen was reduced by FNR and tetryl served as the redox mediator. Our results suggest that under aerobic conditions; tetryl is reduced to the nitroanion radical by the enzyme and this radical is involved in the reduction of molecular oxygen.
- OSTI ID:
- 126596
- Report Number(s):
- CONF-950402-; TRN: 95:006086-0581
- Resource Relation:
- Conference: 209. American Chemical Society (ACS) national meeting, Anaheim, CA (United States), 2-6 Apr 1995; Other Information: PBD: 1995; Related Information: Is Part Of 209th ACS national meeting; PB: 2088 p.
- Country of Publication:
- United States
- Language:
- English
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