1.14.11.17 18O kinetic isotope effects in non-heme iron enzymes: probing the nature of Fe/O2 intermediates Bacteria 1.14.11.17 A simple assay of taurine concentrations in food and biological samples using taurine dioxygenase Escherichia coli 1.14.11.17 alpha-Hydroxylation of carboxylic acids catalyzed by taurine dioxygenase Escherichia coli 1.14.11.17 An assay for Fe(II)/2-oxoglutarate-dependent dioxygenases by enzyme-coupled detection of succinate formation Escherichia coli 1.14.11.17 Atom tunneling in the hydroxylation process of taurine/alpha-ketoglutarate dioxygenase identified by quantum mechanics/molecular mechanics simulations Escherichia coli 1.14.11.17 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 Escherichia coli 1.14.11.17 Can the peroxosuccinate complex in the catalytic cycle of taurine/alpha-ketoglutarate dioxygenase (TauD) act as an alternative oxidant? Escherichia coli 1.14.11.17 CD and MCD of CytC3 and taurine dioxygenase: role of the facial triad in alpha-KG-dependent oxygenases Escherichia coli 1.14.11.17 Characterization of a sulfur-regulated oxygenative alkylsulfatase from Pseudomonas putida S-313 Pseudomonas putida 1.14.11.17 Characterization of a sulfur-regulated oxygenative alkylsulfatase from Pseudomonas putida S-313 Pseudomonas putida S-313 1.14.11.17 Characterization of alpha-ketoglutarate-dependent taurine dioxygenase from Escherichia coli Escherichia coli 1.14.11.17 Comparative quantum mechanics/molecular mechanics (QM/MM) and density functional theory calculations on the oxo-iron species of taurine/alpha-ketoglutarate dioxygenase Escherichia coli 1.14.11.17 Cr(II) reactivity of taurine/alpha-ketoglutarate dioxygenase Escherichia coli 1.14.11.17 Cryoreduction of the NO-adduct of taurine:alpha-ketoglutarate dioxygenase (TauD) yields an elusive {FeNO}(8) species Escherichia coli 1.14.11.17 Direct detection of oxygen intermediates in the non-heme Fe enzyme taurine/alpha-ketoglutarate dioxygenase Escherichia coli 1.14.11.17 Electrostatic perturbations in the substrate-binding pocket of taurine/alpha-ketoglutarate dioxygenase determine its selectivity Escherichia coli 1.14.11.17 Electrostatic perturbations in the substrate-binding pocket of taurine/alpha-ketoglutarate dioxygenase determine its selectivity Escherichia coli K12 1.14.11.17 Elucidating enzyme mechanism and intrinsic chemical properties of short-lived intermediates in the catalytic cycles of cysteine dioxygenase and taurine/alpha-ketoglutarate dioxygenase Homo sapiens 1.14.11.17 EXAFS spectroscopic evidence for an Fe:O Unit in the Fe(IV) intermediate observed during oxygen activation by taurine:alpha-ketoglutarate dioxygenase Escherichia coli 1.14.11.17 Facile synthesis of 1,1-[2H2]-2-methylaminoethane-1-sulfonic acid as a substrate for taurine a ketoglutarate dioxygenase (TauD) Escherichia coli 1.14.11.17 Kinetic and spectroscopic investigation of CoII, NiII, and N-oxalylglycine inhibition of the FeII/alpha-ketoglutarate dioxygenase, TauD Escherichia coli 1.14.11.17 Kinetic dissection of the catalytic mechanism of taurine:alpha-ketoglutarate dioxygenase (TauD) from Escherichia coli Escherichia coli 1.14.11.17 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 Escherichia coli 1.14.11.17 Mechanism of taurine: alpha-ketoglutarate dioxygenase (TauD) from Escherichia coli Escherichia coli 1.14.11.17 Metal ligand substitution and evidence for quinone formation in taurine/alpha-ketoglutarate dioxygenase Escherichia coli 1.14.11.17 Modular behavior of tauD provides insight into the origin of specificity in alpha-ketoglutarate-dependent nonheme iron oxygenases Escherichia coli 1.14.11.17 Probing the iron-substrate orientation for taurine/alpha-ketoglutarate dioxygenase using deuterium electron spin echo envelope modulation spectroscopy Escherichia coli 1.14.11.17 Quantum chemical studies of C-H activation reactions by high-valent nonheme iron centers Escherichia coli 1.14.11.17 Self-hydroxylation of taurine/alpha-ketoglutarate dioxygenase: evidence for more than one oxygen activation mechanism Escherichia coli 1.14.11.17 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 Escherichia coli 1.14.11.17 Strongly coupled redox-linked conformational switching at the active site of the non-heme iron-dependent dioxygenase, TauD Escherichia coli 1.14.11.17 Strongly coupled redox-linked conformational switching at the active site of the non-heme iron-dependent dioxygenase, TauD Escherichia coli K12 1.14.11.17 Structural origin of the large redox-linked reorganization in the 2-oxoglutarate dependent oxygenase, TauD Escherichia coli 1.14.11.17 Structural origin of the large redox-linked reorganization in the 2-oxoglutarate dependent oxygenase, TauD Escherichia coli K12 1.14.11.17 Structure of a ferryl mimic in the archetypal iron(II)- and 2-(oxo)-glutarate-dependent dioxygenase, TauD Escherichia coli 1.14.11.17 Structure of a ferryl mimic in the archetypal iron(II)- and 2-(oxo)-glutarate-dependent dioxygenase, TauD Escherichia coli K12 1.14.11.17 Substrate-induced conformational changes in Escherichia coli taurine/alpha-ketoglutarate dioxygenase and insight into the oligomeric structure Escherichia coli 1.14.11.17 The Fe(II)/alpha-ketoglutarate-dependent taurine dioxygenases from Pseudomonas putida and Escherichia coli are tetramers Pseudomonas putida 1.14.11.17 The Fe(II)/alpha-ketoglutarate-dependent taurine dioxygenases from Pseudomonas putida and Escherichia coli are tetramers Escherichia coli 1.14.11.17 The Fe(II)/alpha-ketoglutarate-dependent taurine dioxygenases from Pseudomonas putida and Escherichia coli are tetramers Pseudomonas putida KT 2240 1.14.11.17 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) Escherichia coli 1.14.11.17 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) Escherichia coli K12 1.14.11.17 X-ray crystal structure of Escherichia coli taurine/alpha-ketoglutarate dioxygenase complexed to ferrous iron and substrates Escherichia coli