ArticleBiochemistry2023
Leveraging a Structural Blueprint to Rationally Engineer the Rieske Oxygenase TsaM.
Article in Biochemistry, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 20 citations in OpenAlex.
- Rieske Oxygenases: Powerful Models for Understanding Nature's Orchestration of Electron Transfer and Oxidative Chemistry.Biochemistry · 2025Review
- Machine Learning Guided Rational Design of a Non-Heme Iron-Based Lysine Dioxygenase Improves its Total Turnover Number.Chembiochem : a European journal of chemical biology · 2024Article
- Elucidating the Role of OACS environmental Au · 2024Article
- Machine learning guided rational design of a non-heme iron-based lysine dioxygenase improves its total turnover number.bioRxiv : the preprint server for biology · 2024Article
- The catabolism of lignin-derivedApplied 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
- 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
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Rieske nonheme iron oxygenases use two metallocenters, a Rieske-type [2Fe-2S] cluster and a mononuclear iron center, to catalyze oxidation reactions on a broad range of substrates. These enzymes are widely used by microorganisms to degrade environmental pollutants and to build complexity in a myriad of biosynthetic pathways that are industrially interesting. However, despite the value of this chemistry, there is a dearth of understanding regarding the structure-function relationships in this enzyme class, which limits our ability to rationally redesign, optimize, and ultimately exploit the chemistry of these enzymes. Therefore, in this work, by leveraging a combination of available structural information and state-of-the-art protein modeling tools, we show that three "hotspot" regions can be targeted to alter the site selectivity, substrate preference, and substrate scope of the Rieske oxygenase
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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.