ArticleApplied and environmental microbiology2007
Purification and characterization of a three-component salicylate 1-hydroxylase from Sphingomonas sp. strain CHY-1.
Article in Applied and environmental microbiology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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20 citing papers in PubMed, 50 citations in OpenAlex.
- Article
- Unveiling the regulatory mechanisms of salicylate degradation gene clusterApplied and environmental microbiology · 2023Article
- The Impact of Anti-Inflammatory Drugs on the Prokaryotic Community Composition and Selected Bacterial Strains Based on Microcosm Experiments.Microorganisms · 2023Article
- Biochemical and structural characterization of an aromatic ring-hydroxylating dioxygenase for terephthalic acid catabolism.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- A Genomic and Transcriptomic Study on the DDT-ResistantMicroorganisms · 2021Article
- Design and evaluation of synthetic bacterial consortia for optimized phenanthrene degradation through the integration of genomics and shotgun proteomics.Biotechnology reports (Amsterdam, Netherlands) · 2021Article
- Structural and Biochemical Analysis Reveals a Distinct Catalytic Site of Salicylate 5-Monooxygenase NagGH from Rieske Dioxygenases.Applied and environmental microbiology · 2021Article
- Conserved Metabolic and Evolutionary Themes in Microbial Degradation of Carbamate Pesticides.Frontiers in microbiology · 2021Review
- Characterization of the Phenanthrene-DegradingMicroorganisms · 2020Article
- Chromosome-free bacterial cells are safe and programmable platforms for synthetic biology.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Salicylate 5-Hydroxylase: Intermediates in Aromatic Hydroxylation by a Rieske Monooxygenase.Biochemistry · 2019Article
- 3,6-Dichlorosalicylate Catabolism Is Initiated by the DsmABC Cytochrome P450 Monooxygenase System in Rhizorhabdus dicambivorans Ndbn-20.Applied and environmental microbiology · 2018Article
- Insights into the genome and proteome of Sphingomonas paucimobilis strain 20006FA involved in the regulation of polycyclic aromatic hydrocarbon degradation.World journal of microbiology & biotechnology · 2017Article
- Novel Three-Component Phenazine-1-Carboxylic Acid 1,2-Dioxygenase in Sphingomonas wittichii DP58.Applied and environmental microbiology · 2017Article
- Characterization of novel polycyclic aromatic hydrocarbon dioxygenases from the bacterial metagenomic DNA of a contaminated soil.Applied and environmental microbiology · 2014Article
- Functional characterization of diverse ring-hydroxylating oxygenases and induction of complex aromatic catabolic gene clusters in Sphingobium sp. PNB.FEBS open bio · 2014Article
- Salicylate degradation by the fungal plant pathogen Sclerotinia sclerotiorum.Current microbiology · 2013Article
- Advances in the field of high-molecular-weight polycyclic aromatic hydrocarbon biodegradation by bacteria.Microbial biotechnology · 2010Review
- Bacterial degradation of aromatic compounds.International journal of environmental research and public health · 2009Review
- Over-the-Counter Monocyclic Non-Steroidal Anti-Inflammatory Drugs in Environment-Sources, Risks, Biodegradation.Water, air, and soil pollutionArticle
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Authors and funding
3 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In the bacterial degradation of polycyclic aromatic hydrocarbons (PAHs), salicylate hydroxylases catalyze essential reactions at the junction between the so-called upper and lower catabolic pathways. Unlike the salicylate 1-hydroxylase from pseudomonads, which is a well-characterized flavoprotein, the enzyme found in sphingomonads appears to be a three-component Fe-S protein complex, which so far has not been characterized. Here, the salicylate 1-hydroxylase from Sphingomonas sp. strain CHY-1 was purified, and its biochemical and catalytic properties were characterized. The oxygenase component, designated PhnII, exhibited an alpha3beta3 heterohexameric structure and contained one Rieske-type [2Fe-2S] cluster and one mononuclear iron per alpha subunit. In the presence of purified reductase (PhnA4) and ferredoxin (PhnA3) components, PhnII catalyzed the hydroxylation of salicylate to catechol with a maximal specific activity of 0.89 U/mg and showed an apparent Km for salicylate of 1.1 +/- 0.2 microM. The hydroxylase exhibited similar activity levels with methylsalicylates and low activity with salicylate analogues bearing additional hydroxyl or electron-withdrawing substituents. PhnII converted anthranilate to 2-aminophenol and exhibited a relatively low affinity for this substrate (Km, 28 +/- 6 microM). 1-Hydroxy-2-naphthoate, which is an intermediate in phenanthrene degradation, was not hydroxylated by PhnII, but it induced a high rate of uncoupled oxidation of NADH. It also exerted strong competitive inhibition of salicylate hydroxylation, with a Ki of 0.68 microM. The properties of this three-component hydroxylase are compared with those of analogous bacterial hydroxylases and are discussed in light of our current knowledge of PAH degradation by sphingomonads.
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