ArticleActa crystallographica. Section D, Biological crystallography2009
Structures of the multicomponent Rieske non-heme iron toluene 2,3-dioxygenase enzyme system.
Article in Acta crystallographica. Section D, Biological crystallography, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
29 citing papers in PubMed, 74 citations in OpenAlex.
- Regioselective Sesquiterpene Hydroxylation Directed by Tunnel Remodeling in Rieske Oxygenases.JACS Au · 2026Article
- Metabolic engineering of doxorubicin biosynthesis through P450-redox partner optimization and structural analysis of DoxA.Nature communications · 2026Article
- Rieske Oxygenases: Powerful Models for Understanding Nature's Orchestration of Electron Transfer and Oxidative Chemistry.Biochemistry · 2025Review
- Study and Modification of the Polycyclic Aromatic Hydrocarbon Degradation Gene Cluster inMicroorganisms · 2025Article
- Toluene Toxicity in the Brain: From Cellular Targets to Molecular Mechanisms.Annual review of pharmacology and toxicology · 2025Review
- Photo-reduction facilitated stachydrine oxidative N-demethylation reaction: A case study of Rieske non-heme iron oxygenase Stc2 from Sinorhizobium meliloti.Methods in enzymology · 2024Article
- Purification and characterization of a Rieske oxygenase and its NADH-regenerating partner proteins.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
- Contrasting Mechanisms of Aromatic and Aryl-Methyl Substituent Hydroxylation by the Rieske Monooxygenase Salicylate 5-Hydroxylase.Biochemistry · 2023Article
- Light-driven Oxidative Demethylation Reaction Catalyzed by a Rieske-type Non-heme Iron Enzyme Stc2.ACS catalysis · 2022Article
- Fluoro-recognition: New in vivo fluorescent assay for toluene dioxygenase probing induction by and metabolism of polyfluorinated compounds.Environmental microbiology · 2022Article
- The α- and β-Subunit Boundary at the Stem of the Mushroom-Like αApplied and environmental microbiology · 2022Article
- Monooxygenase- and Dioxygenase-Catalyzed Oxidative Dearomatization of Thiophenes by Sulfoxidation,International journal of molecular sciences · 2022Review
- Design principles for site-selective hydroxylation by a Rieske oxygenase.Nature communications · 2022Article
- Customized exogenous ferredoxin functions as an efficient electron carrier.Bioresources and bioprocessing · 2021Article
- Active-site loop variations adjust activity and selectivity of the cumene dioxygenase.Nature communications · 2021Article
- Evaluation of aromatic hydrocarbon decomposition catalyzed by the dioxygenase system and substitution of ferredoxin and ferredoxin reductase.Environmental science and pollution research international · 2019Article
- NRVS Studies of the Peroxide Shunt Intermediate in a Rieske Dioxygenase and Its Relation to the Native FeJournal of the American Chemical Society · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 2 institutions in 3 countries.
Funding
Abstract
Bacterial Rieske non-heme iron oxygenases catalyze the initial hydroxylation of aromatic hydrocarbon substrates. The structures of all three components of one such system, the toluene 2,3-dioxygenase system, have now been determined. This system consists of a reductase, a ferredoxin and a terminal dioxygenase. The dioxygenase, which was cocrystallized with toluene, is a heterohexamer containing a catalytic and a structural subunit. The catalytic subunit contains a Rieske [2Fe-2S] cluster and mononuclear iron at the active site. This iron is not strongly bound and is easily removed during enzyme purification. The structures of the enzyme with and without mononuclear iron demonstrate that part of the structure is flexible in the absence of iron. The orientation of the toluene substrate in the active site is consistent with the regiospecificity of oxygen incorporation seen in the product formed. The ferredoxin is Rieske type and contains a [2Fe-2S] cluster close to the protein surface. The reductase belongs to the glutathione reductase family of flavoenzymes and consists of three domains: an FAD-binding domain, an NADH-binding domain and a C-terminal domain. A model for electron transfer from NADH via FAD in the reductase and the ferredoxin to the terminal active-site mononuclear iron of the dioxygenase is proposed.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.