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Copper promotes E. coli laccase-mediated TNT biotransformation and alters the toxicity of TNT metabolites toward Tigriopus japonicus

https://doi.org/10.1016/j.ecoenv.2019.02.056
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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

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CueO Is a Multi-copper Oxidase That Confers Copper Tolerance in Escherichia coli
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Ecotoxicological Characterization of Energetic Substances Using a Soil Extraction Procedure
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Biodegradation of Lignin by White Rot Fungi
inferredcites →https://doi.org/10.1007/978-3-319-01083-0openalex-snapshot
Biological Remediation of Explosive Residues
inferredcites →https://doi.org/10.1007/978-3-319-01083-0_2openalex-snapshot
Microbial Degradation of 2,4,6-Trinitrotoluene In Vitro and in Natural Environments
inferredcites →https://doi.org/10.1007/bf00292610openalex-snapshot
Non-genotoxicity of 2,4,6-Trinitrotoluene (TNT) to the mouse bone marrow and the rat liver: implications for its carcinogenicity
inferredcites →https://doi.org/10.1007/s00018-014-1827-5openalex-snapshot
Three-dimensional structures of laccases
inferredcites →https://doi.org/10.1007/s002440010253openalex-snapshot
Development of Marine Toxicity Data for Ordnance Compounds
inferredcites →https://doi.org/10.1007/s002440010284openalex-snapshot
Interaction of 2,4,6-Trinitrotoluene (TNT) and 4-Amino-2,6-Dinitrotoluene with Humic Monomers in the Presence of Oxidative Enzymes
inferredcites →https://doi.org/10.1007/s00253-005-1950-1openalex-snapshot
Purification and characterization of NAD(P)H-dependent nitroreductase I from Klebsiella sp. C1 and enzymatic transformation of 2,4,6-trinitrotoluene
inferredcites →https://doi.org/10.1007/s00253-007-1008-7openalex-snapshot
TNT biotransformation: when chemistry confronts mineralization
inferredcites →https://doi.org/10.1007/s00253-010-2830-xopenalex-snapshot
Microbial 2,4,6-trinitrotoluene degradation: could we learn from (bio)chemistry for bioremediation and vice versa?
inferredcites →https://doi.org/10.1007/s00253-010-3009-1openalex-snapshot
Oxidation of polycyclic aromatic hydrocarbons by the bacterial laccase CueO from E. coli
inferredcites →https://doi.org/10.1007/s002849900216openalex-snapshot
Aerobic Gram-Positive and Gram-Negative Bacteria Exhibit Differential Sensitivity to and Transformation of 2,4,6-Trinitrotoluene (TNT)
inferredcites →https://doi.org/10.1007/s10438-005-0009-5openalex-snapshot
Sensitivity of various Escherichia coli strains to 2,4,6-trinitrotoluene
inferredcites →https://doi.org/10.1007/s10529-006-9244-yopenalex-snapshot
TNT transformation products are affected by the growth conditions of Raoultella terrigena
inferredcites →https://doi.org/10.1007/s10532-012-9611-4openalex-snapshot
Effect of ferrihydrite on 2,4,6-trinitrotoluene biotransformation by an aerobic yeast
inferredcites →https://doi.org/10.1007/s10750-016-2859-7openalex-snapshot
The challenging role of life cycle monitoring: evidence from bisphenol A on the copepod Tigriopus japonicus
inferredcites →https://doi.org/10.1016/j.bbrc.2005.01.084openalex-snapshot
Copper sensitivity of cueO mutants of Escherichia coli K-12 and the biochemical suppression of this phenotype
inferredcites →https://doi.org/10.1016/j.bbrc.2006.12.116openalex-snapshot
Crystal structures of E. coli laccase CueO at different copper concentrations
inferredcites →https://doi.org/10.1016/j.biortech.2017.01.036openalex-snapshot
Isolation, one-step affinity purification, and characterization of a polyextremotolerant laccase from the halophilic bacterium Aquisalibacillus elongatus and its application in the delignification of sugar beet pulp
inferredcites →https://doi.org/10.1016/j.chemosphere.2005.12.034openalex-snapshot
Coupling of 2,4,6-trinitrotoluene (TNT) metabolites onto humic monomers by a new laccase from Trametes modesta
inferredcites →https://doi.org/10.1016/j.dt.2018.01.004openalex-snapshot
Biotransformation and degradation of 2,4,6-trinitrotoluene by microbial metabolism and their interaction
inferredcites →https://doi.org/10.1016/j.ecoenv.2007.03.006openalex-snapshot
Toxicity of explosive compounds to the marine mussel, Mytilus galloprovincialis, in aqueous exposures
inferredcites →https://doi.org/10.1016/j.ecoenv.2010.02.007openalex-snapshot
Toxicity of trinitrotoluene to sheepshead minnows in water exposures
inferredcites →https://doi.org/10.1016/j.ecoenv.2016.12.012openalex-snapshot
Enhancement of microbial 2,4,6-trinitrotoluene transformation with increased toxicity by exogenous nutrient amendment
inferredcites →https://doi.org/10.1016/j.enzmictec.2017.04.004openalex-snapshot
High-level expression of a bacterial laccase, CueO from Escherichia coli K12 in Pichia pastoris GS115 and its application on the decolorization of synthetic dyes
inferredcites →https://doi.org/10.1016/j.jenvman.2007.06.009openalex-snapshot
Microbial remediation of nitro-aromatic compounds: An overview
inferredcites →https://doi.org/10.1016/j.jenvman.2011.12.010openalex-snapshot
The role of nutrients in the biodegradation of 2,4,6-trinitrotoluene in liquid and soil
inferredcites →https://doi.org/10.1016/j.jhazmat.2018.01.039openalex-snapshot
The integrated analysis of transcriptome and proteome for exploring the biodegradation mechanism of 2, 4, 6-trinitrotoluene by Citrobacter sp
inferredcites →https://doi.org/10.1016/j.jmb.2008.01.004openalex-snapshot
Crystal Structure of a Minimal Nitroreductase, ydjA, from Escherichia coli K12 with and without FMN Cofactor
inferredcites →https://doi.org/10.1016/j.micres.2005.12.001openalex-snapshot
Determination of laccase gene expression during degradation of 2,4,6-trinitrotoluene and its catabolic intermediates in Trametes versicolor
inferredcites →https://doi.org/10.1016/s0304-4165(97)00117-7openalex-snapshot
Electrochemical analysis of the interactions of laccase mediators with lignin model compounds
inferredcites →https://doi.org/10.1016/s1389-1723(03)80163-9openalex-snapshot
Optimization for Biodegradation of 2,4,6-Trinitrotoluene (TNT) by Pseudomonas putida
inferredcites →https://doi.org/10.1021/es9803308openalex-snapshot
Metabolism of 2,4,6-Trinitrotoluene by Pseudomonas sp. JLR11
inferredcites →https://doi.org/10.1039/b502796aopenalex-snapshot
Bacterial pathways for degradation of nitroaromatics
inferredcites →https://doi.org/10.1039/c4em00627eopenalex-snapshot
Properties of bacterial laccases and their application in bioremediation of industrial wastes
inferredcites →https://doi.org/10.1073/pnas.052710499openalex-snapshot
Crystal structure and electron transfer kinetics of CueO, a multicopper oxidase required for copper homeostasis in Escherichia coli
inferredcites →https://doi.org/10.1073/pnas.120163297openalex-snapshot
One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
inferredcites →https://doi.org/10.1074/jbc.m116.729103openalex-snapshot
The Tat Substrate CueO Is Transported in an Incomplete Folding State
inferredcites →https://doi.org/10.1080/10643380902945706openalex-snapshot
Laccase: A Review of Its Past and Its Future in Bioremediation
inferredcites →https://doi.org/10.1093/femsle/fnx256openalex-snapshot
Biotransformation of trinitrotoluene by Citrobacter sp. YC4 and evaluation of its cyto-toxicological effects
inferredcites →https://doi.org/10.1111/j.1365-2958.2011.07824.xopenalex-snapshot
Evolution of catabolic pathways and their regulatory systems in synthetic nitroaromatic compounds degrading bacteria
inferredcites →https://doi.org/10.1111/j.1462-2920.2007.01272.xopenalex-snapshot
Escherichia coli has multiple enzymes that attack TNT and release nitrogen for growth
inferredcites →https://doi.org/10.1111/j.1574-6968.2002.tb10988.xopenalex-snapshot
Copper and cadmium increase laccase activity inPleurotus ostreatus
inferredcites →https://doi.org/10.1111/j.1574-6976.2008.00107.xopenalex-snapshot
Reduction of polynitroaromatic compounds: the bacterial nitroreductases
inferredcites →https://doi.org/10.1111/j.1751-7915.2009.00085.xopenalex-snapshot
Microbial responses to xenobiotic compounds. Identification of genes that allow Pseudomonas putida KT2440 to cope with 2,4,6‐trinitrotoluene
inferredcites →https://doi.org/10.1128/aem.00386-08openalex-snapshot
Subfunctionality of Hydride Transferases of the Old Yellow Enzyme Family of Flavoproteins of Pseudomonas putida
inferredcites →https://doi.org/10.1128/aem.01052-06openalex-snapshot
Aerobic Growth of Escherichia coli with 2,4,6-Trinitrotoluene (TNT) as the Sole Nitrogen Source and Evidence of TNT Denitration by Whole Cells and Cell-Free Extracts
inferredcites →https://doi.org/10.1128/aem.66.11.4742-4750.2000openalex-snapshot
Transformation of 2,4,6-Trinitrotoluene by Purified Xenobiotic Reductase B from Pseudomonas fluorescens I-C
inferredcites →https://doi.org/10.1128/jb.183.16.4866-4875.2001openalex-snapshot
Oxidation of Phenolate Siderophores by the Multicopper Oxidase Encoded by theEscherichia coli yacKGene
inferredcites →https://doi.org/10.1128/mmbr.00006-10openalex-snapshot
Nitroaromatic Compounds, from Synthesis to Biodegradation
inferredcites →https://doi.org/10.1128/mmbr.65.3.335-352.2001openalex-snapshot
Biological Degradation of 2,4,6-Trinitrotoluene
inferredcites →https://doi.org/10.1201/9781420004342openalex-snapshot
Ecotoxicology of Explosives
inferredcites →https://doi.org/10.1201/9781420004342-11openalex-snapshot
Aquatic Toxicology of Explosives
inferredcites →https://doi.org/10.1201/9781420004342.ch4openalex-snapshot
Aquatic Toxicology of Explosives
inferredcites →https://doi.org/10.1520/stp12237sopenalex-snapshot
Ecotoxicity of Nitroaromatics to Aquatic and Terrestrial Species at Army Superfund Sites
inferredcites →https://doi.org/10.1520/stp1317-ebopenalex-snapshot
Environmental Toxicology and Risk Assessment: Modeling and Risk Assessment Sixth Volume
inferredcites →https://doi.org/10.1590/s1517-838246120140026openalex-snapshot
Degradation of 2,4,6-trinitrotoluene by P. aeruginosa and characterization of some metabolites
inferredcites →https://doi.org/10.1897/03-272openalex-snapshot
Developmental toxicity of p,p′-dichlorodiphenyltrichloroethane, 2,4,6-trinitrotoluene, their metabolites, and benzo[a]pyrene in Xenopus laevis embryos
inferredcites →https://doi.org/10.2478/s11756-014-0441-1openalex-snapshot
Biodegradation of 2,4,6-trinitrotoluene (TNT) under sulfate and nitrate reducing conditions
inferredcites →https://doi.org/10.5860/choice.48-1218openalex-snapshot
Encyclopedia of industrial biotechnology: bioprocess, bioseparation, and cell technology

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

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Cu( II ) nonspecifically binding chromate reductase NfoR promotes Cr( VI ) reduction
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In Silico Screening of Laccases with Universality based on Structural Analysis
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