Seth-Smith, H M B, Rosser, S J, Basran, A et al. (4 more authors) (2002) Cloning, sequencing, and characterization of the hexahydro-1,3,5-trinitro-1,3,5-triazine degradation gene cluster from Rhodococcus rhodochrous. Applied and Environmental Microbiology. pp. 4764-4771. ISSN 0099-2240
Abstract
Hexahydro-1,3,5-trinitro-1,3,5-triazine (RDX) is a high explosive which presents an environmental hazard as a major land and groundwater contaminant. Rhodococcus rhodochrous strain 11Y was isolated from explosive contaminated land and is capable of degrading RDX when provided as the sole source of nitrogen for growth. Products of RDX degradation in resting-cell incubations were analyzed and found to include nitrite, formaldehyde, and formate. No ammonium was excreted into the medium, and no dead-end metabolites were observed. The gene responsible for the degradation of RDX in strain 11Y is a constitutively expressed cytochrome P450-like gene, xpLA, which is found in a gene cluster with an adrenodoxin reductase homologue, xplB. The cytochrome P450 also has a flavodoxin domain at the N terminus. This study is the first to present a gene which has been identified as being responsible for RDX biodegradation. The mechanism of action of XplA on RDX is thought to involve initial denitration followed by spontaneous ring cleavage and mineralization.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | Copyright © 2002 American Society for Microbiology |
Keywords: | HERBICIDE-INDUCIBLE CYTOCHROMES-P-450,RDX HEXAHYDRO-1,3,5-TRINITRO-1,3,5-TRIAZINE,PHANEROCHAETE-CHRYSOSPORIUM,TNT 2,4,6-TRINITROTOLUENE,STREPTOMYCES-GRISEOLUS,ADRENODOXIN REDUCTASE,BIODEGRADATION,FLAVODOXIN,OPERON,STRAIN |
Dates: |
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Institution: | The University of York |
Academic Units: | The University of York > Faculty of Sciences (York) > Biology (York) > Centre for Novel Agricultural Products (CNAP) (York) |
Depositing User: | Sherpa Assistant |
Date Deposited: | 01 Apr 2005 |
Last Modified: | 16 Oct 2024 11:57 |
Published Version: | https://doi.org/10.1128/AEM.68.10.4764-4771.2002 |
Status: | Published |
Refereed: | Yes |
Identification Number: | 10.1128/AEM.68.10.4764-4771.2002 |
Related URLs: | |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:375 |