1.14.11.17 698476 18O kinetic isotope effects in non-heme iron enzymes: probing the nature of Fe/O2 intermediates J. Am. Chem. Soc. 130 8122-8123 2008 Bacteria https://pubmed.ncbi.nlm.nih.gov/18540575/ 1.14.11.17 723940 A simple assay of taurine concentrations in food and biological samples using taurine dioxygenase Anal. Biochem. 427 121-123 2012 Escherichia coli https://pubmed.ncbi.nlm.nih.gov/22595347/ 1.14.11.17 742292 alpha-Hydroxylation of carboxylic acids catalyzed by taurine dioxygenase ChemCatChem 8 1361-1366 2016 Escherichia coli - 1.14.11.17 671301 An assay for Fe(II)/2-oxoglutarate-dependent dioxygenases by enzyme-coupled detection of succinate formation Anal. Biochem. 353 69-74 2006 Escherichia coli https://pubmed.ncbi.nlm.nih.gov/16643838/ 1.14.11.17 743152 Atom tunneling in the hydroxylation process of taurine/alpha-ketoglutarate dioxygenase identified by quantum mechanics/molecular mechanics simulations J. Phys. Chem. B 121 5347-5354 2017 Escherichia coli https://pubmed.ncbi.nlm.nih.gov/28490178/ 1.14.11.17 742651 Calorimetric assessment of Fe(2+) binding to ?-ketoglutarate/taurine dioxygenase ironing out the energetics of metal coordination by the 2-His-1-carboxylate facial triad Inorg. Chem. 54 2278-2283 2015 Escherichia coli https://pubmed.ncbi.nlm.nih.gov/25668068/ 1.14.11.17 673044 Can the peroxosuccinate complex in the catalytic cycle of taurine/alpha-ketoglutarate dioxygenase (TauD) act as an alternative oxidant? Chem. Commun. (Camb. ) 2007 171-173 2007 Escherichia coli https://pubmed.ncbi.nlm.nih.gov/17180236/ 1.14.11.17 687279 CD and MCD of CytC3 and taurine dioxygenase: role of the facial triad in alpha-KG-dependent oxygenases J. Am. Chem. Soc. 129 14224-14231 2007 Escherichia coli https://pubmed.ncbi.nlm.nih.gov/17967013/ 1.14.11.17 680611 Characterization of a sulfur-regulated oxygenative alkylsulfatase from Pseudomonas putida S-313 J. Biol. Chem. 275 31661-31667 2000 Pseudomonas putida https://pubmed.ncbi.nlm.nih.gov/10913158/ 1.14.11.17 680611 Characterization of a sulfur-regulated oxygenative alkylsulfatase from Pseudomonas putida S-313 J. Biol. Chem. 275 31661-31667 2000 Pseudomonas putida S-313 https://pubmed.ncbi.nlm.nih.gov/10913158/ 1.14.11.17 285263 Characterization of alpha-ketoglutarate-dependent taurine dioxygenase from Escherichia coli J. Biol. Chem. 272 23031-23036 1997 Escherichia coli https://pubmed.ncbi.nlm.nih.gov/9287300/ 1.14.11.17 688611 Comparative quantum mechanics/molecular mechanics (QM/MM) and density functional theory calculations on the oxo-iron species of taurine/alpha-ketoglutarate dioxygenase J. Phys. Chem. A 112 2464-2468 2008 Escherichia coli https://pubmed.ncbi.nlm.nih.gov/18237159/ 1.14.11.17 687079 Cr(II) reactivity of taurine/alpha-ketoglutarate dioxygenase Inorg. Chem. 46 10087-10092 2007 Escherichia coli https://pubmed.ncbi.nlm.nih.gov/17973473/ 1.14.11.17 712249 Cryoreduction of the NO-adduct of taurine:alpha-ketoglutarate dioxygenase (TauD) yields an elusive {FeNO}(8) species J. Am. Chem. Soc. 132 4739-4751 2010 Escherichia coli https://pubmed.ncbi.nlm.nih.gov/20218714/ 1.14.11.17 658975 Direct detection of oxygen intermediates in the non-heme Fe enzyme taurine/alpha-ketoglutarate dioxygenase J. Am. Chem. Soc. 126 1022-1023 2004 Escherichia coli https://pubmed.ncbi.nlm.nih.gov/14746461/ 1.14.11.17 764499 Electrostatic perturbations in the substrate-binding pocket of taurine/alpha-ketoglutarate dioxygenase determine its selectivity Chemistry 28 e202104167 2022 Escherichia coli https://pubmed.ncbi.nlm.nih.gov/34967481/ 1.14.11.17 764499 Electrostatic perturbations in the substrate-binding pocket of taurine/alpha-ketoglutarate dioxygenase determine its selectivity Chemistry 28 e202104167 2022 Escherichia coli K12 https://pubmed.ncbi.nlm.nih.gov/34967481/ 1.14.11.17 697475 Elucidating enzyme mechanism and intrinsic chemical properties of short-lived intermediates in the catalytic cycles of cysteine dioxygenase and taurine/alpha-ketoglutarate dioxygenase Coord. Chem. Rev. 253 754-768 2009 Homo sapiens - 1.14.11.17 658984 EXAFS spectroscopic evidence for an Fe:O Unit in the Fe(IV) intermediate observed during oxygen activation by taurine:alpha-ketoglutarate dioxygenase J. Am. Chem. Soc. 126 8108-8109 2004 Escherichia coli https://pubmed.ncbi.nlm.nih.gov/15225039/ 1.14.11.17 701264 Facile synthesis of 1,1-[2H2]-2-methylaminoethane-1-sulfonic acid as a substrate for taurine a ketoglutarate dioxygenase (TauD) Tetrahedron Lett. 50 611-613 2009 Escherichia coli - 1.14.11.17 671717 Kinetic and spectroscopic investigation of CoII, NiII, and N-oxalylglycine inhibition of the FeII/alpha-ketoglutarate dioxygenase, TauD Biochem. Biophys. Res. Commun. 338 191-197 2005 Escherichia coli https://pubmed.ncbi.nlm.nih.gov/16165092/ 1.14.11.17 658130 Kinetic dissection of the catalytic mechanism of taurine:alpha-ketoglutarate dioxygenase (TauD) from Escherichia coli Biochemistry 44 8138-8147 2005 Escherichia coli https://pubmed.ncbi.nlm.nih.gov/15924433/ 1.14.11.17 725787 Measuring the orientation of taurine in the active site of the non-heme Fe(II)/alpha-ketoglutarate-dependent taurine hydroxylase (TauD) using electron spin echo envelope modulation (ESEEM) spectroscopy J. Phys. Chem. B 117 10384-10394 2013 Escherichia coli https://pubmed.ncbi.nlm.nih.gov/23937570/ 1.14.11.17 673443 Mechanism of taurine: alpha-ketoglutarate dioxygenase (TauD) from Escherichia coli Eur. J. Inorg. Chem. 2005 4245-4254 2005 Escherichia coli - 1.14.11.17 688192 Metal ligand substitution and evidence for quinone formation in taurine/alpha-ketoglutarate dioxygenase J. Inorg. Biochem. 101 797-808 2007 Escherichia coli https://pubmed.ncbi.nlm.nih.gov/17350690/ 1.14.11.17 701001 Modular behavior of tauD provides insight into the origin of specificity in alpha-ketoglutarate-dependent nonheme iron oxygenases Proc. Natl. Acad. Sci. USA 106 19791-19795 2009 Escherichia coli https://pubmed.ncbi.nlm.nih.gov/19892731/ 1.14.11.17 685159 Probing the iron-substrate orientation for taurine/alpha-ketoglutarate dioxygenase using deuterium electron spin echo envelope modulation spectroscopy Biochemistry 46 5951-5959 2007 Escherichia coli https://pubmed.ncbi.nlm.nih.gov/17469855/ 1.14.11.17 697518 Quantum chemical studies of C-H activation reactions by high-valent nonheme iron centers Curr. Opin. Chem. Biol. 13 89-98 2009 Escherichia coli https://pubmed.ncbi.nlm.nih.gov/19272830/ 1.14.11.17 674930 Self-hydroxylation of taurine/alpha-ketoglutarate dioxygenase: evidence for more than one oxygen activation mechanism J. Biol. Inorg. Chem. 11 63-72 2006 Escherichia coli https://pubmed.ncbi.nlm.nih.gov/16320009/ 1.14.11.17 687288 Spectroscopic and computational evaluation of the structure of the high-spin Fe(IV)-oxo intermediates in taurine: alpha-ketoglutarate dioxygenase from Escherichia coli and its His99Ala ligand variant J. Am. Chem. Soc. 129 6168-6179 2007 Escherichia coli https://pubmed.ncbi.nlm.nih.gov/17451240/ 1.14.11.17 765270 Strongly coupled redox-linked conformational switching at the active site of the non-heme iron-dependent dioxygenase, TauD J. Phys. Chem. B 123 7785-7793 2019 Escherichia coli https://pubmed.ncbi.nlm.nih.gov/31433947/ 1.14.11.17 765270 Strongly coupled redox-linked conformational switching at the active site of the non-heme iron-dependent dioxygenase, TauD J. Phys. Chem. B 123 7785-7793 2019 Escherichia coli K12 https://pubmed.ncbi.nlm.nih.gov/31433947/ 1.14.11.17 764972 Structural origin of the large redox-linked reorganization in the 2-oxoglutarate dependent oxygenase, TauD J. Am. Chem. Soc. 141 15318-15326 2019 Escherichia coli https://pubmed.ncbi.nlm.nih.gov/31475523/ 1.14.11.17 764972 Structural origin of the large redox-linked reorganization in the 2-oxoglutarate dependent oxygenase, TauD J. Am. Chem. Soc. 141 15318-15326 2019 Escherichia coli K12 https://pubmed.ncbi.nlm.nih.gov/31475523/ 1.14.11.17 764167 Structure of a ferryl mimic in the archetypal iron(II)- and 2-(oxo)-glutarate-dependent dioxygenase, TauD Biochemistry 58 4218-4223 2019 Escherichia coli https://pubmed.ncbi.nlm.nih.gov/31503454/ 1.14.11.17 764167 Structure of a ferryl mimic in the archetypal iron(II)- and 2-(oxo)-glutarate-dependent dioxygenase, TauD Biochemistry 58 4218-4223 2019 Escherichia coli K12 https://pubmed.ncbi.nlm.nih.gov/31503454/ 1.14.11.17 657996 Substrate-induced conformational changes in Escherichia coli taurine/alpha-ketoglutarate dioxygenase and insight into the oligomeric structure Biochemistry 42 5547-5554 2003 Escherichia coli https://pubmed.ncbi.nlm.nih.gov/12741810/ 1.14.11.17 724974 The Fe(II)/alpha-ketoglutarate-dependent taurine dioxygenases from Pseudomonas putida and Escherichia coli are tetramers FEBS J. 279 816-831 2012 Pseudomonas putida https://pubmed.ncbi.nlm.nih.gov/22221834/ 1.14.11.17 724974 The Fe(II)/alpha-ketoglutarate-dependent taurine dioxygenases from Pseudomonas putida and Escherichia coli are tetramers FEBS J. 279 816-831 2012 Escherichia coli https://pubmed.ncbi.nlm.nih.gov/22221834/ 1.14.11.17 724974 The Fe(II)/alpha-ketoglutarate-dependent taurine dioxygenases from Pseudomonas putida and Escherichia coli are tetramers FEBS J. 279 816-831 2012 Pseudomonas putida KT 2240 https://pubmed.ncbi.nlm.nih.gov/22221834/ 1.14.11.17 765089 The Irving-Williams series and the 2-His-1-carboxylate facial triad a thermodynamic study of Mn2+, Fe2+, and Co2+ binding to taurine/?-ketoglutarate dioxygenase (TauD) J. Biol. Inorg. Chem. 23 785-793 2018 Escherichia coli https://pubmed.ncbi.nlm.nih.gov/29923040/ 1.14.11.17 765089 The Irving-Williams series and the 2-His-1-carboxylate facial triad a thermodynamic study of Mn2+, Fe2+, and Co2+ binding to taurine/?-ketoglutarate dioxygenase (TauD) J. Biol. Inorg. Chem. 23 785-793 2018 Escherichia coli K12 https://pubmed.ncbi.nlm.nih.gov/29923040/ 1.14.11.17 657933 X-ray crystal structure of Escherichia coli taurine/alpha-ketoglutarate dioxygenase complexed to ferrous iron and substrates Biochemistry 41 5185-5192 2002 Escherichia coli https://pubmed.ncbi.nlm.nih.gov/11955067/