| Résumé | Enzyme catalyzed biotransformation of the energetic chemical octahydro-1,3,5,7-tetranitro-1,3,5,7-tetrazocine (HMX) is not known. The present study describes a xanthine oxidase (XO) catalyzed biotransformation of HMX to provide insight into the biodegradation pathway of this energetic chemical. The rates of biotransformation under aerobic and anaerobic conditions were 1.6+-0.2 and 10.5+-0.9 nmol h-1 mg protein-1, respectively, indicating that anaerobic conditions favored the reaction. The biotransformation rate was about 6-fold higher using NADH as an electron-donor compared to xanthine. During the course of reaction, the products obtained were nitrite (NO2-), methylenedinitramine (MDNA), 4-nitro-2,4-diazabutanal (NDAB), formaldehyde (HCHO), nitrous oxide (N2O), formic acid (HCOOH), and ammonium (NH4+). The product distribution gave carbon and nitrogen mass-balances of 91% and 88%, respectively. A comparative study with native-, deflavo-, and desulfo-XO and the site-specific inhibition studies showed that HMX biotransformation occurred at the FAD-site of XO. Nitrite stoichiometry revealed that an initial single N-denitration step was sufficient for the spontaneous decomposition of HMX. (c) Biosciences Information Services. |
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