ReviewMetallomics : integrated biometal science2013
Imposing function down a (cupin)-barrel: secondary structure and metal stereochemistry in the αKG-dependent oxygenases.
Review in Metallomics : integrated biometal science, 2013. 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, 41 citations in OpenAlex.
- A highly dynamic mononuclear non-heme iron enzyme for the two-step isonitrile biosynthesis.Nature communications · 2026Article
- 2-Oxoglutarate Analog-Based Biomolecular Tools for Exploring Structure-Activity Relationships in Nonheme Iron Enzymes.Chembiochem : a European journal of chemical biology · 2025Article
- Three distinct strategies lead to programmable aliphatic C-H oxidation in bicyclomycin biosynthesis.Nature communications · 2025Article
- Multiple Physiological and Biochemical Functions of Ascorbic Acid in Plant Growth, Development, and Abiotic Stress Response.International journal of molecular sciences · 2024Review
- Dissecting the Mechanism of the Nonheme Iron Endoperoxidase FtmOx1 Using Substrate Analogues.JACS Au · 2022Article
- Reaction pathway engineering converts a radical hydroxylase into a halogenase.Nature chemical biology · 2022Article
- Genome-Wide Identification and Expression Profiling of 2OGD Superfamily Genes from ThreeGenes · 2021Article
- Protein Flexibility of the α-Ketoglutarate-Dependent Oxygenase Factor-Inhibiting HIF-1: Implications for Substrate Binding, Catalysis, and Regulation.Biochemistry · 2019Article
- Exploiting Substrate Promiscuity of Ectoine Hydroxylase for Regio- and Stereoselective Modification of Homoectoine.Frontiers in microbiology · 2019Article
- Recent examples of α-ketoglutarate-dependent mononuclear non-haem iron enzymes in natural product biosyntheses.Natural product reports · 2018Review
- The Irving-Williams series and the 2-His-1-carboxylate facial triad: a thermodynamic study of MnJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2018Article
- Global stability of an α-ketoglutarate-dependent dioxygenase (TauD) and its related complexes.Biochimica et biophysica acta. General subjects · 2017Article
- Evidence that oxidative dephosphorylation by the nonheme Fe(II), α-ketoglutarate:UMP oxygenase occurs by stereospecific hydroxylation.FEBS letters · 2017Article
- The facial triad in the α-ketoglutarate dependent oxygenase FIH: A role for sterics in linking substrate binding to OJournal of inorganic biochemistry · 2017Article
- EctD-mediated biotransformation of the chemical chaperone ectoine into hydroxyectoine and its mechanosensitive channel-independent excretion.Microbial cell factories · 2016Article
- Substrate Promotes Productive Gas Binding in the α-Ketoglutarate-Dependent Oxygenase FIH.Biochemistry · 2016Article
- Increased Turnover at Limiting O2 Concentrations by the Thr(387) → Ala Variant of HIF-Prolyl Hydroxylase PHD2.Biochemistry · 2015Article
- Crystal structure of the ectoine hydroxylase, a snapshot of the active site.The Journal of biological chemistry · 2014Article
- Oxygen sensing strategies in mammals and bacteria.Journal of inorganic biochemistry · 2014Review
- First- and second-sphere contributions to Fe(II) site activation by cosubstrate binding in non-heme Fe enzymes.Dalton transactions (Cambridge, England : 2003) · 2014Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The Fe(ii)/αketoglutarate (αKG) dependent oxygenases catalyze a diverse range of reactions significant in biological processes such as antibiotic biosynthesis, lipid metabolism, oxygen sensing, and DNA and RNA repair. Although functionally diverse, the eight-stranded β-barrel (cupin) and HX(D/E)XnH facial triad motifs are conserved in this super-family of enzymes. Crystal structure analysis of 25 αKG oxygenases reveals two stereoisomers of the Fe cofactor, Anti and Clock, which differ in the relative position of the exchangeable ligand position and the primary substrate. Herein, we discuss the relationship between the chemical mechanism and the secondary coordination sphere of the αKG oxygenases, within the constraints of the stereochemistry of the Fe cofactor. Sequence analysis of the cupin barrel indicates that a small subset of positions constitute the second coordination sphere, which has significant ramifications for the structure of the ferryl intermediate. The competence of both Anti and Clock stereoisomers of Fe points to a ferryl intermediate that is 5 coordinate. The small number of conserved close contacts within the active sites of αKG oxygenases can be extended to chemically related enzymes, such as the αKG-dependent halogenases SyrB2 and CytC3, and the non-αKG dependent dioxygenases isopenicillin N synthase (IPNS) and cysteine dioxygenase (CDO).
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