ArticleNature communications2022
Design principles for site-selective hydroxylation by a Rieske oxygenase.
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed.
- Emerging classes of copper enzymes.Current opinion in chemical biology · 2026Review
- Robots and Minimal, Physics-Informed Features: A Hybrid Framework for Enzyme Catalysis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Utility-Scale Quantum Computational Chemistry.The journal of physical chemistry letters · 2026Review
- High-Valent Late Transition Metal-Oxo Complexes: Breaking Boundaries at the Oxo Wall and Beyond.Chemical reviews · 2026Review
- Regioselective Sesquiterpene Hydroxylation Directed by Tunnel Remodeling in Rieske Oxygenases.JACS Au · 2026Article
- Structure-guided engineering of an aromatic ring-hydroxylating dioxygenase for broad-spectrum phthalate degradation.Journal of bacteriology · 2025Article
- Rieske Oxygenases: Powerful Models for Understanding Nature's Orchestration of Electron Transfer and Oxidative Chemistry.Biochemistry · 2025Review
- The Role of the Unusual 2-Tyr-1-carboxylate Non-heme Iron Motif in the Mechanism of N,N-Dimethylformamidase.ACS catalysis · 2025Article
- Three distinct strategies lead to programmable aliphatic C-H oxidation in bicyclomycin biosynthesis.Nature communications · 2025Article
- Biosynthesis of guanidine-containing natural products in cyanobacteria.Journal of industrial microbiology & biotechnology · 2024Review
- Advances, opportunities, and challenges in methods for interrogating the structure activity relationships of natural products.Natural product reports · 2024Review
- Elucidating the Role of OACS environmental Au · 2024Article
- Semi-rational design of nitroarene dioxygenase for catalytic ability toward 2,4-dichloronitrobenzene.Applied and environmental microbiology · 2024Article
- 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
- Functional and spectroscopic approaches to determining thermal limitations of Rieske oxygenases.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
- Biocatalytic control of site-selectivity and chain length-selectivity in radical amino acid halogenases.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- A structure-function analysis of chlorophyllase reveals a mechanism for activity regulation dependent on disulfide bonds.The Journal of biological chemistry · 2023Article
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7 authors.
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Abstract
Rieske oxygenases exploit the reactivity of iron to perform chemically challenging C-H bond functionalization reactions. Thus far, only a handful of Rieske oxygenases have been structurally characterized and remarkably little information exists regarding how these enzymes use a common architecture and set of metallocenters to facilitate a diverse range of reactions. Herein, we detail how two Rieske oxygenases SxtT and GxtA use different protein regions to influence the site-selectivity of their catalyzed monohydroxylation reactions. We present high resolution crystal structures of SxtT and GxtA with the native β-saxitoxinol and saxitoxin substrates bound in addition to a Xenon-pressurized structure of GxtA that reveals the location of a substrate access tunnel to the active site. Ultimately, this structural information allowed for the identification of six residues distributed between three regions of SxtT that together control the selectivity of the C-H hydroxylation event. Substitution of these residues produces a SxtT variant that is fully adapted to exhibit the non-native site-selectivity and substrate scope of GxtA. Importantly, we also found that these selectivity regions are conserved in other structurally characterized Rieske oxygenases, providing a framework for predictively repurposing and manipulating Rieske oxygenases as biocatalysts.
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