ArticlePloS one2017
Structural and functional studies of ferredoxin and oxygenase components of 3-nitrotoluene dioxygenase from Diaphorobacter sp. strain DS2.
Article in PloS one, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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12 citing papers in PubMed, 22 citations in OpenAlex.
- Rieske Oxygenases: Powerful Models for Understanding Nature's Orchestration of Electron Transfer and Oxidative Chemistry.Biochemistry · 2025Review
- Semi-rational design of nitroarene dioxygenase for catalytic ability toward 2,4-dichloronitrobenzene.Applied and environmental microbiology · 2024Article
- Functional and spectroscopic approaches to determining thermal limitations of Rieske oxygenases.Methods in enzymology · 2024Article
- Custom tuning of Rieske oxygenase reactivity.Nature communications · 2023Article
- Leveraging a Structural Blueprint to Rationally Engineer the Rieske Oxygenase TsaM.Biochemistry · 2023Article
- Engineering Rieske oxygenase activity one piece at a time.Current opinion in chemical biology · 2023Review
- Molecular Basis and Evolutionary Origin of 1-Nitronaphthalene Catabolism inApplied and environmental microbiology · 2023Article
- Contrasting Mechanisms of Aromatic and Aryl-Methyl Substituent Hydroxylation by the Rieske Monooxygenase Salicylate 5-Hydroxylase.Biochemistry · 2023Article
- The α- and β-Subunit Boundary at the Stem of the Mushroom-Like αApplied and environmental microbiology · 2022Article
- Design principles for site-selective hydroxylation by a Rieske oxygenase.Nature communications · 2022Article
- Article
- Structural basis for divergent C-H hydroxylation selectivity in two Rieske oxygenases.Nature communications · 2020Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
3-nitrotoluene dioxygenase (3NTDO) from Diaphorobacter sp. strain DS2 catalyses the conversion of 3-nitrotoluene (3NT) into a mixture of 3- and 4-methylcatechols with release of nitrite. We report here, X-ray crystal structures of oxygenase and ferredoxin components of 3NTDO at 2.9 Å and 2.4 Å, respectively. The residues responsible for nitrite release in 3NTDO were further probed by four single and two double mutations in the catalytic site of α-subunit of the dioxygenase. Modification of Val 350 to Phe, Ile 204 to Ala, and Asn258 to Val by site directed mutagenesis resulted in inactive enzymes revealing the importance of these residues in catalysis. Docking studies of meta nitrotoluene to the active site of 3NTDO suggested possible orientations of binding that favor the formation of 3-methylcatechol (3MC) over 4-methylcatechol energetically. The electron transfer pathway from ferredoxin subunit to the active site of the oxygenase subunit is also proposed.
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