ArticleProceedings of the National Academy of Sciences of the United States of America2010
Structural basis for cofactor-independent dioxygenation of N-heteroaromatic compounds at the alpha/beta-hydrolase fold.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 78 citations in OpenAlex.
- Bacterial Lactonases ZenA with Noncanonical Structural Features Hydrolyze the Mycotoxin Zearalenone.ACS catalysis · 2024Article
- Cofactorless oxygenases guide anthraquinone-fused enediyne biosynthesis.Nature chemical biology · 2024Article
- Evolutionary adaptation from hydrolytic to oxygenolytic catalysis at the α/β-hydrolase fold.Chemical science · 2023Article
- Crystal structures of herbicide-detoxifying esterase reveal a lid loop affecting substrate binding and activity.Nature communications · 2023Article
- Gene discovery and virus-induced gene silencing reveal branched pathways to major classes of bioactive diterpenoids inProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Innovation and tinkering in the evolution of oxidases.Protein science : a publication of the Protein Society · 2022Review
- Stabilizing AqdC, a Pseudomonas Quinolone Signal-Cleaving Dioxygenase from Mycobacteria, by FRESCO-Based Protein Engineering.Chembiochem : a European journal of chemical biology · 2021Article
- An α/β-Hydrolase Fold Subfamily ComprisingApplied and environmental microbiology · 2020Article
- Immunosuppressant mycophenolic acid biosynthesis employs a new globin-like enzyme for prenyl side chain cleavage.Acta pharmaceutica Sinica. B · 2019Article
- 3-Hydroxyflavones and 3-Hydroxy-4-oxoquinolines as Carbon Monoxide-Releasing Molecules.Molecules (Basel, Switzerland) · 2019Review
- Advances in Sustainable Catalysis: A Computational Perspective.Frontiers in chemistry · 2019Review
- Indole Biodegradation in Acinetobacter sp. Strain O153: Genetic and Biochemical Characterization.Applied and environmental microbiology · 2017Article
- The Metal Drives the Chemistry: Dual Functions of Acireductone Dioxygenase.Chemical reviews · 2017Review
- Unveiling the functional diversity of the alpha/beta hydrolase superfamily in the plant kingdom.Current opinion in structural biology · 2016Review
- Monooxygenase Substrates Mimic Flavin to Catalyze Cofactorless Oxygenations.The Journal of biological chemistry · 2016Article
- Refining the reaction mechanism of OPeerJ · 2016Article
- Endoperoxide formation by an α-ketoglutarate-dependent mononuclear non-haem iron enzyme.Nature · 2015Article
- Rhodococcus erythropolis BG43 Genes Mediating Pseudomonas aeruginosa Quinolone Signal Degradation and Virulence Factor Attenuation.Applied and environmental microbiology · 2015Article
- How the Same Core Catalytic Machinery Catalyzes 17 Different Reactions: the Serine-Histidine-Aspartate Catalytic Triad of α/β-Hydrolase Fold Enzymes.ACS catalysis · 2015Article
- Direct evidence for a peroxide intermediate and a reactive enzyme-substrate-dioxygen configuration in a cofactor-free oxidase.Angewandte Chemie (International ed. in English) · 2014Article
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Authors and funding
5 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Enzymatic catalysis of oxygenation reactions in the absence of metal or organic cofactors is a considerable biochemical challenge. The CO-forming 1-H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase (HOD) from Arthrobacter nitroguajacolicus Rü61a and 1-H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase (QDO) from Pseudomonas putida 33/1 are homologous cofactor-independent dioxygenases involved in the breakdown of N-heteroaromatic compounds. To date, they are the only dioxygenases suggested to belong to the alpha/beta-hydrolase fold superfamily. Members of this family typically catalyze hydrolytic processes rather than oxygenation reactions. We present here the crystal structures of both HOD and QDO in their native state as well as the structure of HOD in complex with its natural 1-H-3-hydroxy-4-oxoquinaldine substrate, its N-acetylanthranilate reaction product, and chloride as dioxygen mimic. HOD and QDO are structurally very similar. They possess a classical alpha/beta-hydrolase fold core domain additionally equipped with a cap domain. Organic substrates bind in a preorganized active site with an orientation ideally suited for selective deprotonation of their hydroxyl group by a His/Asp charge-relay system affording the generation of electron-donating species. The "oxyanion hole" of the alpha/beta-hydrolase fold, typically employed to stabilize the tetrahedral intermediate in ester hydrolysis reactions, is utilized here to host and control oxygen chemistry, which is proposed to involve a peroxide anion intermediate. Product release by proton back transfer from the catalytic histidine is driven by minimization of intramolecular charge repulsion. Structural and kinetic data suggest a nonnucleophilic general-base mechanism. Our analysis provides a framework to explain cofactor-independent dioxygenation within a protein architecture generally employed to catalyze hydrolytic reactions.
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