Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2009-8-21
pubmed:abstractText
The transformation of explosives, including hexahydro-1,3,5-trinitro-1,3,5-triazine (RDX), by xenobiotic reductases XenA and XenB (and the bacterial strains harboring these enzymes) under both aerobic and anaerobic conditions was assessed. Under anaerobic conditions, Pseudomonas fluorescens I-C (XenB) degraded RDX faster than Pseudomonas putida II-B (XenA), and transformation occurred when the cells were supplied with sources of both carbon (succinate) and nitrogen (NH4+), but not when only carbon was supplied. Transformation was always faster under anaerobic conditions compared to aerobic conditions, with both enzymes exhibiting a O2 concentration-dependent inhibition of RDX transformation. The primary degradation pathway for RDX was conversion to methylenedinitramine and then to formaldehyde, but a minor pathway that produced 4-nitro-2,4-diazabutanal (NDAB) also appeared to be active during transformation by whole cells of P. putida II-B and purified XenA. Both XenA and XenB also degraded the related nitramine explosives octahydro-1,3,5,7-tetranitro-1,3,5,7-tetrazocine and 2,4,6,8,10,12-hexanitro-2,4,6,8,10,12-hexaazaisowurtzitane. Purified XenB was found to have a broader substrate range than XenA, degrading more of the explosive compounds examined in this study. The results show that these two xenobiotic reductases (and their respective bacterial strains) have the capacity to transform RDX as well as a wide variety of explosive compounds, especially under low oxygen concentrations.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/2,4,6,8,10,12-hexanitro-2,4,6,8,10,1..., http://linkedlifedata.com/resource/pubmed/chemical/Aza Compounds, http://linkedlifedata.com/resource/pubmed/chemical/Azocines, http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Explosive Agents, http://linkedlifedata.com/resource/pubmed/chemical/Flavoproteins, http://linkedlifedata.com/resource/pubmed/chemical/Heterocyclic Compounds, http://linkedlifedata.com/resource/pubmed/chemical/Oxidoreductases, http://linkedlifedata.com/resource/pubmed/chemical/Triazines, http://linkedlifedata.com/resource/pubmed/chemical/XenA protein, Pseudomonas putida, http://linkedlifedata.com/resource/pubmed/chemical/XenB protein, Pseudomonas, http://linkedlifedata.com/resource/pubmed/chemical/Xenobiotics, http://linkedlifedata.com/resource/pubmed/chemical/cyclonite, http://linkedlifedata.com/resource/pubmed/chemical/octogen
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
1432-0614
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
84
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
535-44
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
Transformation of RDX and other energetic compounds by xenobiotic reductases XenA and XenB.
pubmed:affiliation
Shaw Environmental, Inc, 17 Princess Road, Lawrenceville, NJ 08648, USA. mark.fuller@shawgrp.com
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't, Evaluation Studies, Research Support, N.I.H., Extramural