ArticleApplied and environmental microbiology2006
Control of substrate specificity by active-site residues in nitrobenzene dioxygenase.
Article in Applied and environmental microbiology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 57 citations in OpenAlex.
- Semi-rational design of nitroarene dioxygenase for catalytic ability toward 2,4-dichloronitrobenzene.Applied and environmental microbiology · 2024Article
- Recent advances in eco-friendly technology for decontamination of pulp and paper mill industrial effluent: a review.Environmental monitoring and assessment · 2024Review
- Isolation and Characterization a Novel Catabolic Gene Cluster Involved in Chlorobenzene Degradation in HaloalkaliphilicBiology · 2022Article
- Biodegradation of 3-Chloronitrobenzene and 3-Bromonitrobenzene byApplied and environmental microbiology · 2022Article
- Structural and Biochemical Analysis Reveals a Distinct Catalytic Site of Salicylate 5-Monooxygenase NagGH from Rieske Dioxygenases.Applied and environmental microbiology · 2021Article
- A Bph-Like Nitroarene Dioxygenase Catalyzes the Conversion of 3-Nitrotoluene to 3-Methylcatechol by Rhodococcus sp. Strain ZWL3NT.Applied and environmental microbiology · 2020Article
- Article
- Enhancing Mn(II)-Binding and Manganese Peroxidase Activity in a Designed Cytochrome c Peroxidase through Fine-Tuning Secondary-Sphere Interactions.Biochemistry · 2016Article
- Selection for growth on 3-nitrotoluene by 2-nitrotoluene-utilizing Acidovorax sp. strain JS42 identifies nitroarene dioxygenases with altered specificities.Applied and environmental microbiology · 2015Article
- Molecular Dynamics Simulation of Nitrobenzene Dioxygenase Using AMBER Force Field.Journal of chemical theory and computation · 2014Article
- Structural basis of the divergent oxygenation reactions catalyzed by the rieske nonheme iron oxygenase carbazole 1,9a-dioxygenase.Applied and environmental microbiology · 2014Article
- A DFT study of the cis-dihydroxylation of nitroaromatic compounds catalyzed by nitrobenzene dioxygenase.The journal of physical chemistry. B · 2014Article
- Engineering non-heme mono- and dioxygenases for biocatalysis.Computational and structural biotechnology journal · 2012Review
- Evolution of a new bacterial pathway for 4-nitrotoluene degradation.Molecular microbiology · 2011Article
- Nitroaromatic compounds, from synthesis to biodegradation.Microbiology and molecular biology reviews : MMBR · 2010Review
- Reconstructing the evolutionary history of nitrotoluene detection in the transcriptional regulator NtdR.Molecular microbiology · 2009Article
- Application of nitroarene dioxygenases in the design of novel strains that degrade chloronitrobenzenes.Microbial biotechnology · 2009Article
- Structural basis for regioselectivity and stereoselectivity of product formation by naphthalene 1,2-dioxygenase.Journal of bacteriology · 2006Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Nitrobenzene 1,2-dioxygenase from Comamonas sp. strain JS765 catalyzes the initial reaction in nitrobenzene degradation, forming catechol and nitrite. The enzyme also oxidizes the aromatic rings of mono- and dinitrotoluenes at the nitro-substituted carbon, but the basis for this specificity is not understood. In this study, site-directed mutagenesis was used to modify the active site of nitrobenzene dioxygenase, and the contribution of specific residues in controlling substrate specificity and enzyme performance was evaluated. The activities of six mutant enzymes indicated that the residues at positions 258, 293, and 350 in the alpha subunit are important for determining regiospecificity with nitroarene substrates and enantiospecificity with naphthalene. The results provide an explanation for the characteristic specificity with nitroarene substrates. Based on the structure of nitrobenzene dioxygenase, substitution of valine for the asparagine at position 258 should eliminate a hydrogen bond between the substrate nitro group and the amino group of asparagine. Up to 99% of the mononitrotoluene oxidation products formed by the N258V mutant were nitrobenzyl alcohols rather than catechols, supporting the importance of this hydrogen bond in positioning substrates in the active site for ring oxidation. Similar results were obtained with an I350F mutant, where the formation of the hydrogen bond appeared to be prevented by steric interference. The specificity of enzymes with substitutions at position 293 varied depending on the residue present. Compared to the wild type, the F293Q mutant was 2.5 times faster at oxidizing 2,6-dinitrotoluene while retaining a similar Km for the substrate based on product formation rates and whole-cell kinetics.
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