Accession Number:

ADA588963

Title:

Diaphorase Catalyzed Biotransformation of RDX via N-denitration Mechanism

Descriptive Note:

Journal article

Corporate Author:

AIR FORCE RESEARCH LAB TYNDALL AFB FL

Report Date:

2002-01-01

Pagination or Media Count:

7.0

Abstract:

Previously, we hypothesized that hexahydro-1,3,5-trinitro-1,3,5-triazine RDX can be biotransformed by anaerobic sludge via three different routes 1 direct ring cleavage via a-hydroxylation of a-CH2 group, 2 reduction of one of the NO2 groups to NO, 3 N-denitration prior to ring cleavage. The present study describes biotransformation of RDX via route 3 by a diaphorase EC 1.8.1.4 from Clostridium kluyveri using NADH as electron donor. The removal of RDX was accompanied by the formation and accumulation of nitrite ion NO 2 , formaldehyde HCHO, ammonium NH 4 , and nitrous oxide N2O. None of the RDX-nitroso products were detected. The ring cleavage product methylenedinitramine was detected as the transient intermediate. Product stoichiometry showed that each reacted RDX molecule produced one nitrite ion and the product distribution gave a carbon C and nitrogen N mass balance of 91 and 92, respectively, supporting the occurrence of a mono-denitration step prior to the ring cleavage and decomposition. Severe oxygen mediated inhibition 92 inhibition of RDX biotransformation and superoxide dismutase-sensitive cytochrome c reduction indicated the potential involvement of an anion radical RDX prior to denitration. A comparative study between native- and apo-enzymes showed the possible involvement of flavin mononucleotide FMN in catalyzing the transfer of a redox equivalent eH from NADH to RDX to produce RDX responsible for secondary decomposition.

Subject Categories:

  • Organic Chemistry
  • Ammunition and Explosives

Distribution Statement:

APPROVED FOR PUBLIC RELEASE