ArticleJournal of bacteriology2008
Mechanism of 4-nitrophenol oxidation in Rhodococcus sp. Strain PN1: characterization of the two-component 4-nitrophenol hydroxylase and regulation of its expression.
Article in Journal of bacteriology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 81 citations in OpenAlex.
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- Comprehensive Studies of Adsorption Equilibrium and Kinetics for Selected Aromatic Organic Compounds on Activated Carbon.Molecules (Basel, Switzerland) · 2024Article
- The Catabolic System of Acetovanillone and Acetosyringone inApplied and environmental microbiology · 2022Article
- Preliminary study on the effect of catabolite repression gene knockout on p-nitrophenol degradation in Pseudomonas putida DLL-E4.PloS one · 2022Article
- Transcriptomic analysis of Burkholderia cenocepacia CEIB S5-2 during methyl parathion degradation.Environmental science and pollution research international · 2021Article
- Monooxygenation of aromatic compounds by flavin-dependent monooxygenases.Protein science : a publication of the Protein Society · 2019Review
- Catabolism of Alkylphenols inFrontiers in microbiology · 2019Article
- A complete bioconversion cascade for dehalogenation and denitration by bacterial flavin-dependent enzymes.The Journal of biological chemistry · 2018Article
- Oxidative dehalogenation and denitration by a flavin-dependent monooxygenase is controlled by substrate deprotonation.Chemical science · 2018Article
- Two-Component FAD-Dependent Monooxygenases: Current Knowledge and Biotechnological Opportunities.Biology · 2018Review
- On the Enigma of Glutathione-Dependent Styrene Degradation in Gordonia rubripertincta CWB2.Applied and environmental microbiology · 2018Article
- 4-Chlorophenol Oxidation Depends on the Activation of an AraC-Type Transcriptional Regulator, CphR, inFrontiers in microbiology · 2018Article
- Genome Sequencing and Comparative Transcriptomics Provide a Holistic View of 4-Nitrophenol Degradation and Concurrent Fatty Acid Catabolism byFrontiers in microbiology · 2018Article
- Biodegradation of phenol and its derivatives by engineered bacteria: current knowledge and perspectives.World journal of microbiology & biotechnology · 2017Review
- Kinetic Mechanism of the Dechlorinating Flavin-dependent Monooxygenase HadA.The Journal of biological chemistry · 2017Article
- PnpM, a LysR-Type Transcriptional Regulator Activates the Hydroquinone Pathway inFrontiers in microbiology · 2017Article
- Biochemical Characterization of 3-Methyl-4-nitrophenol Degradation in Burkholderia sp. Strain SJ98.Frontiers in microbiology · 2016Article
- Characterization of para-Nitrophenol-Degrading Bacterial Communities in River Water by Using Functional Markers and Stable Isotope Probing.Applied and environmental microbiology · 2015Article
- Transcriptional activation of multiple operons involved in para-nitrophenol degradation by Pseudomonas sp. Strain WBC-3.Applied and environmental microbiology · 2015Article
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7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
4-Nitrophenol (4-NP) is a toxic product of the hydrolysis of organophosphorus pesticides such as parathion in soil. Rhodococcus sp. strain PN1 degrades 4-NP via 4-nitrocatechol (4-NC) for use as the sole carbon, nitrogen, and energy source. A 5-kb EcoRI DNA fragment previously cloned from PN1 contained a gene cluster (nphRA1A2) involved in 4-NP oxidation. From sequence analysis, this gene cluster is expected to encode an AraC/XylS family regulatory protein (NphR) and a two-component 4-NP hydroxylase (NphA1 and NphA2). A transcriptional assay in a Rhodococcus strain revealed that the transcription of nphA1 is induced by only 4-NP (of several phenolic compounds tested) in the presence of nphR, which is constitutively expressed. Disruption of nphR abolished transcriptional activity, suggesting that nphR encodes a positive regulatory protein. The two proteins of the 4-NP hydroxylase, NphA1 and NphA2, were independently expressed in Escherichia coli and purified by ion-exchange chromatography or affinity chromatography. The purified NphA2 reduced flavin adenine dinucleotide (FAD) with the concomitant oxidation of NADH, while the purified NphA1 oxidized 4-NP into 4-NC almost quantitatively in the presence of FAD, NADH, and NphA2. This functional analysis, in addition to the sequence analysis, revealed that this enzyme system belongs to the two-component flavin-diffusible monooxygenase family. The 4-NP hydroxylase showed comparable oxidation activities for phenol and 4-chlorophenol to that for 4-NP and weaker activities for 3-NP and 4-NC.
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