Cloning, sequencing, and characterization of the hexahydro-1,3,5-trinitro-1,3,5-triazine degradation gene cluster from Rhodococcus rhodochrous

H M B Seth-Smith; S J Rosser; A Basran; E R Travis; E R Dabbs; S Nicklin; N C Bruce

doi:10.1128/AEM.68.10.4764-4771.2002

Cloning, sequencing, and characterization of the hexahydro-1,3,5-trinitro-1,3,5-triazine degradation gene cluster from Rhodococcus rhodochrous

H M B Seth-Smith, S J Rosser, A Basran, E R Travis, E R Dabbs, S Nicklin, N C Bruce

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Research output: Contribution to journal › Article › peer-review

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.

Original language	English
Pages (from-to)	4764-4771
Number of pages	8
Journal	Applied and Environmental Microbiology
Volume	68
Issue number	10
DOIs	https://doi.org/10.1128/AEM.68.10.4764-4771.2002
Publication status	Published - Oct 2002

Bibliographical note

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

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@article{e4131152ded14bb1bc95a697d59f1b56,

title = "Cloning, sequencing, and characterization of the hexahydro-1,3,5-trinitro-1,3,5-triazine degradation gene cluster from Rhodococcus rhodochrous",

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.",

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",

author = "Seth-Smith, {H M B} and Rosser, {S J} and A Basran and Travis, {E R} and Dabbs, {E R} and S Nicklin and Bruce, {N C}",

note = "Copyright {\textcopyright} 2002 American Society for Microbiology",

year = "2002",

month = oct,

doi = "10.1128/AEM.68.10.4764-4771.2002",

language = "English",

volume = "68",

pages = "4764--4771",

journal = "Applied and Environmental Microbiology",

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TY - JOUR

T1 - Cloning, sequencing, and characterization of the hexahydro-1,3,5-trinitro-1,3,5-triazine degradation gene cluster from Rhodococcus rhodochrous

AU - Seth-Smith, H M B

AU - Rosser, S J

AU - Basran, A

AU - Travis, E R

AU - Dabbs, E R

AU - Nicklin, S

AU - Bruce, N C

PY - 2002/10

Y1 - 2002/10

N2 - 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.

AB - 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.

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KW - ADRENODOXIN REDUCTASE

KW - BIODEGRADATION

KW - FLAVODOXIN

KW - OPERON

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U2 - 10.1128/AEM.68.10.4764-4771.2002

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JF - Applied and Environmental Microbiology

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ER -