Simultaneous Degradation of 4-Nitrophenol and Picric Acid by Two Different Mechanisms of Rhodococcus sp. PN1

Takeo, Masahiro; Abe, Yoshikatsu; Negoro, Seiji; Heiss, Gesche

doi:10.1252/jcej.36.1178

Cited by 13 publications

(14 citation statements)

References 25 publications

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“…introduced into the StuI site of pKPN3 (44) in the same transcriptional direction as nphA1 to construct pKPN32. Similarly, the same amplified fragment was inserted into the EcoRV site of pKPN3 in the same transcriptional direction as nphR to construct pKPN35.…”

Section: Methodsmentioning

confidence: 99%

“…This bacterium can degrade not only mono-NPs, including 4-NP, but also poly-NPs, such as 2,4-dinitrophenol and 2,4,6-trinitrophenol (picric acid) (1). Analyses of the metabolites in NP degradation revealed that PN1 degrades 4-NP through the 4-NC pathway, whereas it also degrades 2,4-dinitrophenol and picric acid via the corresponding hydride-Meisenheimer complexes (1,13,44). Thus, PN1 has at least two quite different pathways for NP degradation.…”

mentioning

confidence: 99%

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Mechanism of 4-Nitrophenol Oxidation in Rhodococcus sp. Strain PN1: Characterization of the Two-Component 4-Nitrophenol Hydroxylase and Regulation of Its Expression

et al. 2008

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Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 99%

Mechanism of 4-Nitrophenol Oxidation in Rhodococcus sp. Strain PN1: Characterization of the Two-Component 4-Nitrophenol Hydroxylase and Regulation of Its Expression

et al. 2008

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“…The results of comparative genomics suggest that homologs of these proteins are exclusively encoded by the genera Nocardioides, Rhodococcus, and Nocardia among presently sequenced organisms. Empirical studies consistently indicate that equivalent enzymatic pathways can degrade nitroaromatic compounds in five additional Rhodococcus species (398,(436)(437)(438) and three Nocardioides species (54,396,397,432,439). Beyond picrate and 2,4-dinitrophenol, LLHTs are involved in the biodegradation of other nitroaromatic compounds.…”

Section: Fdors: Flavin/deazaflavin Oxidoreductase Superfamilymentioning

confidence: 97%

“…For example, mycobacterial flavin/deazaflavin oxidoreductases can degrade coumarin derivatives (28,55), while rhodococcal luciferase-like hydride transferases can reduce polynitroaromatic compounds (438,440). While the physiological advantage conferred by this promiscuity has not been fully resolved, it does provide a basis for the exploitation of F 420 in bioremediation applications (470).…”

Section: Bioremediationmentioning

confidence: 99%

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Physiology, Biochemistry, and Applications of F₄₂₀- and F_o-Dependent Redox Reactions

Greening

Ahmed

Mohamed

et al. 2016

Microbiol Mol Biol Rev

152

208

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SUMMARY5-Deazaflavin cofactors enhance the metabolic flexibility of microorganisms by catalyzing a wide range of challenging enzymatic redox reactions. While structurally similar to riboflavin, 5-deazaflavins have distinctive and biologically useful electrochemical and photochemical properties as a result of the substitution of N-5 of the isoalloxazine ring for a carbon. 8-Hydroxy-5-deazaflavin (Fo) appears to be used for a single function: as a light-harvesting chromophore for DNA photolyases across the three domains of life. In contrast, its oligoglutamyl derivative F420is a taxonomically restricted but functionally versatile cofactor that facilitates many low-potential two-electron redox reactions. It serves as an essential catabolic cofactor in methanogenic, sulfate-reducing, and likely methanotrophic archaea. It also transforms a wide range of exogenous substrates and endogenous metabolites in aerobic actinobacteria, for example mycobacteria and streptomycetes. In this review, we discuss the physiological roles of F420in microorganisms and the biochemistry of the various oxidoreductases that mediate these roles. Particular focus is placed on the central roles of F420in methanogenic archaea in processes such as substrate oxidation, C1pathways, respiration, and oxygen detoxification. We also describe how two F420-dependent oxidoreductase superfamilies mediate many environmentally and medically important reactions in bacteria, including biosynthesis of tetracycline and pyrrolobenzodiazepine antibiotics by streptomycetes, activation of the prodrugs pretomanid and delamanid byMycobacterium tuberculosis, and degradation of environmental contaminants such as picrate, aflatoxin, and malachite green. The biosynthesis pathways of Foand F420are also detailed. We conclude by considering opportunities to exploit deazaflavin-dependent processes in tuberculosis treatment, methane mitigation, bioremediation, and industrial biocatalysis.

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Nitrophenols disrupt the expression and activity of biotransformation enzymes (CYP3A and COMT) in chicken ovarian follicles in vivo and in vitro

Kozubek,

Katarzyńska‐Banasik,

Kowalik

et al. 2024

J of Applied Toxicology

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Nitrophenols are environmental pollutants and xenobiotics, the main sources of which are diesel exhaust fumes and pesticides. The biotransformation processes that take place in the liver are defence mechanisms against xenobiotics, such as nitrophenols. Our previous study showed that the chicken ovary is an additional xenobiotic detoxification place and that nitrophenols disrupt steroidogenesis in chicken ovarian follicles. Therefore, the present study aimed to determine the in vivo and in vitro effects of 4‐nitrophenol (PNP) and 3‐methyl‐4‐nitrophenol (PNMC) on the expression and activity of phase I (CYP3A) and phase II (COMT) biotransformation enzymes in chicken ovary. In an in vivo study, hens were treated with a vehicle or 10 mg PNP or PNMC/kg b.wt. per day for 6 days. In an in vitro study, prehierarchical white and yellowish follicles, as well as the granulosa and theca layers of the three largest preovulatory follicles (F3, F2 and F1), were isolated and then incubated in a control medium or medium supplemented with PNP (10−6 M) or PNMC (10−6 M) for 24 or 48 h. Both in vivo and in vitro studies showed that nitrophenols exert tissue‐ and compound‐dependent (PNP or PNMC) effects on CYP3A and COMT gene (real‐time PCR) protein (Western blot) expression and their activity (colorimetric methods). The inhibitory effect of nitrophenols in vivo on the activity of biotransformation enzymes suggest that the ovary has the capacity to metabolise PNP and PNMC.

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Simultaneous Degradation of 4-Nitrophenol and Picric Acid by Two Different Mechanisms of Rhodococcus sp. PN1

Cited by 13 publications

References 25 publications

Mechanism of 4-Nitrophenol Oxidation in Rhodococcus sp. Strain PN1: Characterization of the Two-Component 4-Nitrophenol Hydroxylase and Regulation of Its Expression

Mechanism of 4-Nitrophenol Oxidation in Rhodococcus sp. Strain PN1: Characterization of the Two-Component 4-Nitrophenol Hydroxylase and Regulation of Its Expression

Physiology, Biochemistry, and Applications of F₄₂₀- and F_o-Dependent Redox Reactions

Nitrophenols disrupt the expression and activity of biotransformation enzymes (CYP3A and COMT) in chicken ovarian follicles in vivo and in vitro

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Simultaneous Degradation of 4-Nitrophenol and Picric Acid by Two Different Mechanisms of Rhodococcus sp. PN1

Cited by 13 publications

References 25 publications

Mechanism of 4-Nitrophenol Oxidation in Rhodococcus sp. Strain PN1: Characterization of the Two-Component 4-Nitrophenol Hydroxylase and Regulation of Its Expression

Mechanism of 4-Nitrophenol Oxidation in Rhodococcus sp. Strain PN1: Characterization of the Two-Component 4-Nitrophenol Hydroxylase and Regulation of Its Expression

Physiology, Biochemistry, and Applications of F420- and Fo-Dependent Redox Reactions

Nitrophenols disrupt the expression and activity of biotransformation enzymes (CYP3A and COMT) in chicken ovarian follicles in vivo and in vitro

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Physiology, Biochemistry, and Applications of F₄₂₀- and F_o-Dependent Redox Reactions