ArticleAnalytical biochemistry2010
Metal and substrate binding to an Fe(II) dioxygenase resolved by UV spectroscopy with global regression analysis.
Article in Analytical biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Designing a Whole-Cell Biosensor for Detection of Toxic Metals Using Intein Splicing Inhibition ofACS omega · 2026Article
- Association between human paraoxonase 2 protein and efficacy of acetylcholinesterase inhibiting drugs used against Alzheimer's disease.PloS one · 2021Article
- The oxidation of cyclo-olefin by the S = 2 ground-state complex [FeJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2020Article
- Structural Origin of the Large Redox-Linked Reorganization in the 2-Oxoglutarate Dependent Oxygenase, TauD.Journal of the American Chemical Society · 2019Article
- 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
- Comparative analysis of the metal-dependent structural and functional properties of mouse and human SMP30.PloS one · 2019Article
- Global stability of an α-ketoglutarate-dependent dioxygenase (TauD) and its related complexes.Biochimica et biophysica acta. General subjects · 2017Article
- Spectroscopic analyses of 2-oxoglutarate-dependent oxygenases: TauD as a case study.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2017Review
- Calorimetric assessment of Fe(2+) binding to α-ketoglutarate/taurine dioxygenase: ironing out the energetics of metal coordination by the 2-His-1-carboxylate facial triad.Inorganic chemistry · 2015Article
- Equilibrium and kinetic behavior of Fe(CN)6(3-/4-) and cytochrome c in direct electrochemistry using a film electrode thin-layer transmission cell.Analytical chemistry · 2011Article
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3 authors.
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Abstract
The addition of divalent metal ions or substrate taurine to TauD, an alpha-ketoglutarate-dependent dioxygenase, alters its UV absorption, as clearly observed by monitoring the protein's difference spectra. Binding of metal ions leads to a decrease in absorption at approximately 297 nm and modulation of other features. A separate signature with enhanced absorption at approximately 295 nm is identified for binding of taurine. These narrow ( approximately 700 cm(-1)) and intense ( approximately 0.5mM(-1) cm(-1)) spectral changes are attributed to ligand-induced protein conformational changes affecting the environment of aromatic residues. The changes in the UV difference spectra were exploited to assess directly the thermodynamics and kinetics of ligand interactions in wild-type TauD and selected variants. This approach holds promise as a new tool to probe ligand-induced conformational changes in a wide range of other proteins. Experimental and quantification approaches for a reliable analysis of protein absorption below 320 nm are presented.
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