ArticleThe Journal of biological chemistry2010
Characterization of chlorophenol 4-monooxygenase (TftD) and NADH:FAD oxidoreductase (TftC) of Burkholderia cepacia AC1100.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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33 citing papers in PubMed, 84 citations in OpenAlex.
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- Catabolism of acetosyringone and co-metabolic transformation of 2,4,6-trichlorophenol by a novel FAD-dependent monooxygenase.mSystems · 2026Article
- Flavin affinity for the reductase HpaC differentially sensitizes Neisseria gonorrhoeae during Type IV pilus-dependent killing.PLoS pathogens · 2025Article
- A review of enhancement of chlorophenol bioremediation using synergistic effects between zero-valent iron and microorganisms.Biodegradation · 2025Review
- Unifying and versatile features of flavin-dependent monooxygenases: Diverse catalysis by a common C4a-(hydro)peroxyflavin.The Journal of biological chemistry · 2023Review
- Optimal evaluation of energy yield and driving force in microbial metabolic pathway variants.PLoS computational biology · 2023Article
- Mechanisms of aerobic dechlorination of hexachlorobenzene and pentachlorophenol byJournal of pesticide science · 2021Article
- Single-Component and Two-ComponentApplied and environmental microbiology · 2021Article
- Biochemical characterization of NADH:FMN oxidoreductase HcbA3 fromJournal of pesticide science · 2020Article
- Tuning of pThe Journal of biological chemistry · 2020Article
- Microbial degradation of halogenated aromatics: molecular mechanisms and enzymatic reactions.Microbial biotechnology · 2020Review
- Monooxygenation of aromatic compounds by flavin-dependent monooxygenases.Protein science : a publication of the Protein Society · 2019Review
- 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
- Identification of the novelJournal of pesticide science · 2018Article
- Kinetic Mechanism of the Dechlorinating Flavin-dependent Monooxygenase HadA.The Journal of biological chemistry · 2017Article
- Initial investigations of C4a-(hydro)peroxyflavin intermediate formation by dibenzothiophene monooxygenase.Biochemical and biophysical research communications · 2016Article
- Article
- Characterizations of Two Bacterial Persulfide Dioxygenases of the Metallo-β-lactamase Superfamily.The Journal of biological chemistry · 2015Article
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9 authors at 1 institution in 1 country.
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Abstract
Burkholderia cepacia AC1100 completely degrades 2,4,5-trichlorophenol, in which an FADH(2)-dependent monooxygenase (TftD) and an NADH:FAD oxidoreductase (TftC) catalyze the initial steps. TftD oxidizes 2,4,5-trichlorophenol (2,4,5-TCP) to 2,5-dichloro-p-benzoquinone, which is chemically reduced to 2,5-dichloro-p-hydroquinone (2,5-DiCHQ). Then, TftD oxidizes the latter to 5-chloro-2-hydroxy-p-benzoquinone. In those processes, TftC provides all the required FADH(2). We have determined the crystal structures of dimeric TftC and tetrameric TftD at 2.0 and 2.5 A resolution, respectively. The structure of TftC was similar to those of related flavin reductases. The stacked nicotinamide:isoalloxazine rings in TftC and sequential reaction kinetics suggest that the reduced FAD leaves TftC after NADH oxidation. The structure of TftD was also similar to the known structures of FADH(2)-dependent monooxygenases. Its His-289 residue in the re-side of the isoalloxazine ring is within hydrogen bonding distance with a hydroxyl group of 2,5-DiCHQ. An H289A mutation resulted in the complete loss of activity toward 2,5-DiCHQ and a significant decrease in catalytic efficiency toward 2,4,5-TCP. Thus, His-289 plays different roles in the catalysis of 2,4,5-TCP and 2,5-DiCHQ. The results support that free FADH(2) is generated by TftC, and TftD uses FADH(2) to separately transform 2,4,5-TCP and 2,5-DiCHQ. Additional experimental data also support the diffusion of FADH(2) between TftC and TftD without direct physical interaction between the two enzymes.
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