ArticleJournal of bacteriology2006
Structural basis for regioselectivity and stereoselectivity of product formation by naphthalene 1,2-dioxygenase.
Article in Journal of bacteriology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 65 citations in OpenAlex.
- The Role of Free Radicals in the Mimetic Naphthalene Dioxygenase Function ofMolecules (Basel, Switzerland) · 2026Article
- Rieske Oxygenases: Powerful Models for Understanding Nature's Orchestration of Electron Transfer and Oxidative Chemistry.Biochemistry · 2025Review
- Catalytic resilience of multicomponent aromatic ring-hydroxylating dioxygenases in Pseudomonas for degradation of polycyclic aromatic hydrocarbons.World journal of microbiology & biotechnology · 2023Review
- Molecular Basis and Evolutionary Origin of 1-Nitronaphthalene Catabolism inApplied and environmental microbiology · 2023Article
- Substrate-Specific Coupling of OACS catalysis · 2022Article
- 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
- Structural Insights into Dihydroxylation of Terephthalate, a Product of Polyethylene Terephthalate Degradation.Journal of bacteriology · 2022Article
- Binding interaction of a ring-hydroxylating dioxygenase with fluoranthene in Pseudomonas aeruginosa DN1.Scientific reports · 2021Article
- Heterologous expression of membrane-bound alcohol dehydrogenase-encoding genes for glyceric acid production using Gluconobacter sp. CHM43 and its derivatives.Applied microbiology and biotechnology · 2021Article
- Structural basis for divergent C-H hydroxylation selectivity in two Rieske oxygenases.Nature communications · 2020Article
- Article
- Formation of Developmentally Toxic Phenanthrene Metabolite Mixtures by Mycobacterium sp. ELW1.Environmental science & technology · 2017Article
- Article
- Use of silica-encapsulated Pseudomonas sp. strain NCIB 9816-4 in biodegradation of novel hydrocarbon ring structures found in hydraulic fracturing waters.Applied and environmental microbiology · 2014Article
- Theoretical approach to the innovative mutation of naphthalene 1,2-dioxygenase: a molecular dynamics and docking study.Journal of molecular modeling · 2014Article
- 3-Ketosteroid 9α-hydroxylase enzymes: Rieske non-heme monooxygenases essential for bacterial steroid degradation.Antonie van Leeuwenhoek · 2014Review
- Structural basis of the divergent oxygenation reactions catalyzed by the rieske nonheme iron oxygenase carbazole 1,9a-dioxygenase.Applied and environmental microbiology · 2014Article
- Retuning Rieske-type oxygenases to expand substrate range.The Journal of biological chemistry · 2011Article
- Article
- Near-IR MCD of the nonheme ferrous active site in naphthalene 1,2-dioxygenase: correlation to crystallography and structural insight into the mechanism of Rieske dioxygenases.Journal of the American Chemical Society · 2008Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Rieske oxygenase (RO) systems are two- and three-component enzyme systems that catalyze the formation of cis-dihydrodiols from aromatic substrates. Degradation of pollutants in contaminated soil and generation of chiral synthons have been the major foci of RO research. Substrate specificity and product regio- and stereoselectivity have been shown to vary between individual ROs. While directed evolution methods for altering RO function have been successful in the past, rational engineering of these enzymes still poses a challenge due to the lack of structural understanding. Here we examine the structural changes induced by mutation of Phe-352 in naphthalene 1,2-dioxygenase from Pseudomonas sp. strain NCIB 9816-4 (NDO-O(9816-4)). Structures of the Phe-352-Val mutant in native form and in complex with phenanthrene and anthracene, along with those of wild-type NDO-O(9816-4) in complex with phenanthrene, anthracene, and 3-nitrotoluene, are presented. Phenanthrene was shown to bind in a different orientation in the Phe-352-Val mutant active site from that in the wild type, while anthracene was found to bind in similar positions in both enzymes. Two orientations of 3-nitrotoluene were observed, i.e., a productive and a nonproductive orientation. These orientations help explain why NDO-O(9816-4) forms different products from 3-nitrotoluene than those made from nitrobenzene dioxygenase. Comparison of these structures among themselves and with other known ROs bound to substrates reveals that the orientation of substrate binding at the active site is the primary determinant of product regio- and stereoselectivity.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.