ReviewJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2017
Spectroscopic analyses of 2-oxoglutarate-dependent oxygenases: TauD as a case study.
Review in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 34 citations in OpenAlex.
- Structural basis of the promiscuity of the unusual Fe(II) and 2-oxoglutarate dependent human aspartate/asparagine-β-hydroxylase.Nature communications · 2026Article
- Revealing the catalytic mechanism of the Fe(II)/2-oxoglutarate-dependent human epigenetic modifying enzyme ALKBH5.Cell reports. Physical science · 2025Article
- Ancestral Sequence Reconstruction of the Ethylene-Forming Enzyme.Biochemistry · 2025Article
- Exploring the Ascorbate Requirement of the 2-Oxoglutarate-Dependent Dioxygenases.Journal of medicinal chemistry · 2025Review
- Article
- New Frontiers in Nonheme Enzymatic Oxyferryl Species.Chembiochem : a European journal of chemical biology · 2024Review
- Mössbauer-based molecular-level decomposition of the Saccharomyces cerevisiae ironome, and preliminary characterization of isolated nuclei.Metallomics : integrated biometal science · 2022Article
- An Unusual Oxidative Rearrangement Catalyzed by a Divergent Member of the 2-Oxoglutarate-Dependent Dioxygenase Superfamily during Biosynthesis of Dehydrofosmidomycin.Angewandte Chemie (International ed. in English) · 2022Article
- Spectroscopic and in vitro Investigations of FeChembiochem : a European journal of chemical biology · 2022Review
- Strongly Coupled Redox-Linked Conformational Switching at the Active Site of the Non-Heme Iron-Dependent Dioxygenase, TauD.The journal of physical chemistry. B · 2019Article
- Unleashing the Synthetic Power of Plant Oxygenases: From Mechanism to Application.Plant physiology · 2019Review
- Electron Paramagnetic Resonance Signature of Tetragonal Low Spin Iron(V)-Nitrido and -Oxo Complexes Derived from the Electronic Structure Analysis of Heme and Non-Heme Archetypes.Journal of the American Chemical Society · 2019Article
- Glutarate L-2-hydroxylase (CsiD/GlaH) is an archetype Fe(II)/2-oxoglutarate-dependent dioxygenase.Advances in protein chemistry and structural biology · 2019Review
- Understanding Biological Hydrogen Transfer Through the Lens of Temperature Dependent Kinetic Isotope Effects.Accounts of chemical research · 2018Review
- Amazing Diversity in Biochemical Roles of Fe(II)/2-Oxoglutarate Oxygenases.Trends in biochemical sciences · 2018Review
- Dioxygen Activation and O-O Bond Formation Reactions by Manganese Corroles.Journal of the American Chemical Society · 2017Article
- Manganese complex-catalyzed oxidation and oxidative kinetic resolution of secondary alcohols by hydrogen peroxide.Chemical science · 2017Article
- Achieving One-Electron Oxidation of a Mononuclear Nonheme Iron(V)-Imido Complex.Journal of the American Chemical Society · 2017Article
- Visualizing the Reaction Cycle in an Iron(II)- and 2-(Oxo)-glutarate-Dependent Hydroxylase.Journal of the American Chemical Society · 2017Article
- Dioxygen activation by nonheme iron enzymes with the 2-His-1-carboxylate facial triad that generate high-valent oxoiron oxidants.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2017Review
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
A wide range of spectroscopic approaches have been used to interrogate the mononuclear iron metallocenter in 2-oxoglutarate (2OG)-dependent oxygenases. The results from these spectroscopic studies have provided valuable insights into the structural changes at the active site during substrate binding and catalysis, thus providing critical information that complements investigations of these enzymes by X-ray crystallography, biochemical, and computational approaches. This mini-review highlights taurine hydroxylase (taurine:2OG dioxygenase, TauD) as a case study to illustrate the wealth of knowledge that can be generated by applying a diverse array of spectroscopic investigations to a single enzyme. In particular, electronic absorption, circular dichroism, magnetic circular dichroism, conventional and pulse electron paramagnetic, Mössbauer, X-ray absorption, and resonance Raman methods have been exploited to uncover the properties of the metal site in TauD.
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