Tau D

Dew D

Of Proto-Norse *dauði Cognates include Old Icelandic dauði ("death, deadly epidemic"), Swedish död and Finnish tauti. Intial D (Tau man ji D). Theatre, Action & Adventure, Mystery & Suspense; Director: In Theatres: THE MARCHÉS D'ALIMENTS NATURALS TAU. Summary: We present an equilibrium H/D exchange experiment for measuring the exchange rates of unstable amide protons in intrinsically developed proteins.

Mechanisms of taurine: ??Ketoglutarate-Ketoglutarate-Ketoglutarate-Ketoglutarate-Ketoglutarate-Ketoglutarate-Ketoglutarate-Ketoglutarate-Ketoglutarate-ketoglutarate dioxygenase (TauD) by Escherichia Coli Mechanisms of taurine: ??Ketoglutarate-Ketoglutarate-Ketoglutarate-Ketoglutarate-Ketoglutarate-Ketoglutarate-Ketoglutarate-Ketoglutarate-Ketoglutarate-Ketoglutarate-ketoglutarate dioxygenase (TauD) by Escherichia Coriol Mechanisms of taurine: ??Ketoglutarate-Ketoglutarate-Ketoglutarate-Ketoglutarate-Ketoglutarate-Ketoglutarate-Ketoglutarate-Ketoglutarate-Ketoglutarate-Ketoglutarate-ketoglutarate dioxygenase (TauD) by Escherichia-Chemistry Mechanisms of taurine: ??Ketoglutarate-Ketoglutarate-Ketoglutarate-Ketoglutarate-Ketoglutarate-Ketoglutarate-Ketoglutarate-Ketoglutarate-Ketoglutarate-Ketoglutarate-ketoglutarate dioxygenase (TauD) by Escherichia ketogate Mechanisms of taurine: ??Ketoglutarate-Ketoglutarate-Ketoglutarate-Ketoglutarate-Ketoglutarate-Ketoglutarate-Ketoglutarate-Ketoglutarate-Ketoglutarate-Ketoglutarate-ketoglutarate dioxygenase (TauD) by Escherichia-C Mechanisms of taurine: ??Ketoglutarate-Ketoglutarate-Ketoglutarate-Ketoglutarate-Ketoglutarate-Ketoglutarate-Ketoglutarate-Ketoglutarate-Ketoglutarate-Ketoglutarate-ketoglutarate dioxygenase (TauD) by Escherichia por))

For Xudan Song, Jiarui Lu and Wenzhen Lai, mechanistic insight into O2 activity, O2 replacement and subsoil eoxidation by means of AsqJ-Dioxygenase from quanta mechanical/molecular mechanic computations, Physical Chemistry Chemical Physics, 10. 1039/C7CP02687K, 19, 30, (20188-20197), (2017). To Faponle and Sam P. de Visser, The Role of Nonheme Transition Metal-Oxo, -Peroxo, and -Superoxo Intermediates in enzyme catalysis and bioinspired complex reaction, Inorganic reaction mechanisms, 10.1016/bs.adioch.2017.01.002, (167-194), (2017).

Timmins Amy, Maud Saint-André et Sam P. de Visser, Understanding How Prolyl-4-hydroxylase Structure Steers a Ferryl Oxidant towards Scission of a Strong C-H Bond, Journal of the American Chemical Society, 10.1021/jacs. Wei-Min Ching, Ang Zhou, Johannes E. M. N. Klein, Ruixi Fan, Gerald Knizia, Christopher J. Cramer, Yisong Guo and Lawrence Que, characterization of the volatile Hydroxoiron(III) complex of the pentadentate TMC-py ligand, inorganic chemistry, 10.1021/acs.inorgchem.

and Sumin Park, VTST/MT Trials on the catalysis of C-H activity by Cu2 (C-H-O2)],[Fe2(C-H-O2)] and Fe(IV)-O nuclei in transition metals using DFT as the basis for possible power surface, JBIC Journal of Biological Inorganic Chemistry, 10. 1007/s00775-017-1441-8, 22, 2-3, (321-338), (2017). Martin, Scott J. Eron and Michael J. Knapp, The Face Threefold in the ?-ketoglutarate-dependent BOHF: The Oxygenase:

Inorganic Biochemistry, Journal of Inorganic Biochemistry, 10.1016/j.jinorgbio.2016.10. Theoretical study on the DFT potential energy surfaces, inorganic chemistry, 10.1021/acs.inorgchem. Zekai Lin, Teng Zhang, James Gilhula, Carter W. Abney und Wenbin Lin, Robust and Porous ?-Diketiminate-Functionalized Metal-Organic Frameworks for Earth-Abundant-Metal-Catalyzed C-H Amination and Hydrogenation, Journal of the American Chemical Society, 10.1021/jacs.

Chemical Breakthroughs and Chemical Breakthroughs - A European Journal, 22, 8, (2562-2581), (2015). Richmond, Miquel Costas and Ebbe Nordlander, Nonheme Fe(IV) oxo complexes of two new pentadentate ligands and their hydrogen atom and oxygen atom transfer reactions, Inorganic chemistry, 10. 1021/ic5029564, 54, 15, (7152-7164), (2015). Salytta Martinez and Robert P. Hausinger, Catalysis of Fe(II) and 2-oxoglutarate-dependent oxygenases, Journal of Biological Chemistry, 10.1074/jbc.R115.

Hannah Tarhonskaya, Adam P. Hardy, Emily A. Howe, Nikita D. Loik, Holger B. Kramer, James S. O. McCullagh, Christopher J. Schofield und Emily Flashman, Kinetic Investigations of the Role of Factor Inhibiting Hypoxia-inducible Factor (FIH) as an Oxygen Sensor, Journal of Biological Chemistry, 10.1074/jbc.M115. TAKAZHI Ogura and MASATATSU Suzuki, oxidation reactivity of a structurally and spectroscopically well-defined mononuclear peroxocarbonato iron(III) complex, letters of chemistry, 10.

Insight into reducing activations of oxygen in Fe( ii) centres, Chemical Science, 10. 1039/C4SC01891E, 6, 1, (639-647), (2015). Constantin P. Bryliakov and Evgenii P. Talsi, Aktive Stellen und Mechanismen der bioinspirierten Oxidation mit H2O2, catalysed by non-Häm-Fe und verwandte Mn-Komplexe, Coordination Chemistry Reviews, 10.1016/j.ccr.2014.06.

Chang, Y. Guo, C. Wang, S. E. Butch, A. C. Rosenzweig, A. K. Boal, C. Krebs and J. M. Bollinger, Mechanism of the C5 stereoinversion reaction in the bio-synthesis of carbapenem antibiotics, science, 10,1126/science. Yui Morishima, Shoko Soma, Robert K. Szilagyi and Kiyoshi Fujisawa, conversion of carbon dioxide to oxalate by ?-ketocarboxylatocopper(II) complexes, inorganic chemistry, 10. 1021/ic5006242, 53, 16, (8191-8193), (2014).

Mary E. Pandelia, Ning Li, Hanne Nørgaard, Douglas M. Warui, Lauren J. Rajakovich, Wei-chen Chang, Squire J. Booker, Karsten Krebs and J. Bollinger, Substrate triggers addition of dioxygen to the diferrous cofactor of aldehyde-deformylating Oxygenase to produce a diferric-peroxide intermediate, Journal of the American Chemical Society, 10. 1021/ja405047b, 135, 42, (15801-15812), (2013).

The New Approach to the Storage of Oxygen-containing Intermediate Products at Multimillimolar Levels, Laura M.K. Dassama, Megan L. Matthews, Wei Jiang, John C. Price, Victoria Korboukh, Ning Li and J. Martin Bollinger, Coordination Chemistry Reviews, 10.1016/j.ccr.2012.06. Chemistry Reviews Coordination, 10.1016/j.ccr.2012.08. Richard L. Lord und G. Andrés Cisneros, Ab Initio QM/MM Berechnungen zeigen einen Intersystem Crossing im Hydrogen Abstraction Step in Decalkylation Catalysé par AlkB, The Journal of Physical Chemistry B, 10. 1021/jp403116e, 117, 21, (6410-6420), (2013).

S. P. de Visser, Oxygen Atom Transfer, Comprehensive Inorganic Chemistry II, 10.1016/B978-0-08-097774-4. J. Lloret-Fillol et M. Costas, Small Molecule Models for Nonporphyrinic Iron and Mangan Oxygenases, Comprehensive Inorganic Chemistry II, 10.1016/B978-0-08-097774-4. Spectroscopy, Thomas M. Casey, Piotr K. Grzyska, Robert P. Hausinger and John McCracken, Measurement of the active site of non-Heme Fe(II)/?-ketoglutarate-dependent Taurin hydroxylase (TauD) by electron spin-echo envelope modulation (ESEEM), The Journal of Physical Chemistry B, 10. 1021/jp404743d, 117, 36, (10384-10394), (2013)

SYNGFA Ye, Christoph Riplinger, Andreas Hansen, Charles Krebs, J. Martin Bollinger and Frank Neese, Electronic structural analysis of the oxygen activation mechanism by FeII- and -ketoglutarate (?KG)-dependent dioxygenase, Chemie - A European Journal, 18, 21, (6555-6567), (2012). Tetramere, The FEBS Journal, 279, 5, (816-831), (2012) are Stefan H. Knauer, Olivia Hartl-Spiegelhauer, Stephan Schwarzinger, Petra Hänzelmann and Holger Dobbek, The Fe(II)/-dependent-ketoglutarate-dependent taurel oxygenases from -dependent and Escherichiae.

Jörg Sutter, Haobin Wang, Karsten Meyer und Ranko P. Bontchev, N-O Bond Homolyse of an Iron(II) TEMPO Complex Yields an Iron(III) Oxo Intermediate, Journal of the American Chemical Society, 10. 1021/ja211882e, 134, 15, (6516-6519), (2012). Chemistry - A European Journal, 18, 37, (11747-11760), (2012).

Nad Sørensen Vad, Anders Lennartson, Anne Nielsen, Jeffrey Harmer, John E. McGrady, Cathrine Frandsen, Steen Mørup and Christine J. McKenzie, An aquous Fe(iv)oxo compound with a base group in the second co-ordination area, Chemical Communications, 10. 1039/c2cc35746a, 48, 88, (10880), (2012). The Subrata Kundu, Eduard Matito, Stephan Walleck, Florian F. Pfaff, Florian Heims, Battist Rábay, Josep M. Luis, Anna Company, Beatrice Braun, Thorsten Glaser und Kallol Ray, OO Bond Formation Mediatated by a Hexanuclear Iron Supported on a Stannoxane Core, Chemistry - A European Journal, 18, 10, (2787-2791), (2012), (2012).

Kyung-Bin Cho, Eun Jeong Kim, Mi Sook Seo, Sason Shaik and Wonwoo Nam, Correlation of DFT-calculated energy barriers to experiments in non-thematic octahedral FeIVO species, Chemie - A European Journal, 18, 33, (10444-10453), (2012). Comma J. Christian, Shengfa Ye and Frank Neese, oxygen reactivation in extradiol-catecholate oxygenases - a chemical science functionally close spaced trial, 10. 1039/c2sc00754a, 3, 5, (1600), (2012).

Aidsan R. McDonald, Yisong Guo, Van V. Vu, Emile L. Bominaar, Eckard Münck and Lawrence Que, A single-core, carboxylate-rich oxoiron(iv) complex: a textural and fuctional facial expression of the T&D intermediate'J', Chemical Science, 10. 1039/c2sc01044e, 3, 5, (1680), (2012). Substitution of water and oxidation reactivity of a non-heme-iron(IV) oxo compound with a tripodal tetradentate ligand, Chemistry - A European Journal, 17, 5, (1622-1634), (2011).

Joel Panay, Michael Lee, Carsten Krebs, J. Martin Bollinger and Paul F. Fitzpatrick, Residence for a High-Spin Fe(IV) type in the catalysis of a bacterial phenylalanine hydroxylase, biochemistry, 10. 1021/bi1019868, 50, 11, (1928-1933), (2011).

Émily Flashman, Lee M. Hoffart, Refaat B. Hamed, J. Martin Bollinger Jr, J. Christopher J. Schofield and Christopher J. Krebs, evidence for the gradual response of hypoxia-inducible hypoxia inducible factors with prolysis, The FEBS Journal, 277, 19, (4089-4099), (2010). Ketoglutarate et Judith P. Klinman, An Active-Site Phenylalanine Directs Substrate Binding and C-H Cleavage in the ?-Ketoglutarate-Dependent Dioxygenase TauD, Journal of the American Chemical Society, 10. 1021/ja909416z, 132, 14, (5114-5120), (2010), (2010).

Cryoreduction of the NO-Adduct of Taurine:?-Ketoglutarate Dioxygenase (TauD) Ye yields an Elusive {FeNO} 8 Species, Journal of the American Chemical Society, 10. 1021/ja909715g, 132, 13, (4739-4751), (2010). de?Visser, Origin of the correlation of the rate constant of substrate hydroxideation by non-heme iron (IV) oxo complexes with the bond dissociation energy of the CH bond of the substrate, Chemie ? A European Journal, 15, 27, (6651-6662), (2009).

Cancer and J. Martin Bollinger, Freeze-quench 57Fe-Mössbauer Spectroscopy: Capturing of reaction intermediate products, photosynthesis research, 10. 1007/s11120-009-9406-6, 102, 2-3, (295-304), (2009). Kristian Koski, Reija Hieta, Maija Hirsilä, Anna Rönkä, Johanna Myllyharju et Rik K. Wierenga, The Crystal Structure of an Algal Prolyl 4-Hydroxylase Complexed mit Proline-rich Peptide Reveals a Novel Buried Binding Motif, Journal of Biological Chemistry, 10.1074/jbc.M109.

Jens Müller and Martin Bröring, Iron Catalysis in Biological and Biomimetic Reactions, Iron Catalysis in Organic Chemistry, (29-72), (2008). Chemistry - A European Journal, 14, 15, (4533-4541), (2008). Fujimori and Christopher T. Walsh, Halogenation Strategies in Natural Product Biosynthesis, Chemistry & Biology, 10.1016/j.chembiol.2008.01.

NON-hae isen mononuclear non-haem ferrous Enzyme with the 2-His-1-carboxylate face triad: New Evolutions in Enzymmology and Modelling Research, Chemical Society Reviews, 10. 1039/b707179p, 37, 12, (2716), (2008). Martin Bollinger and Cancer, Enzzymatic C-H activity by metal-superoxo intermediate products, Current statement in chemical biology, 10.1016/j.cbpa.2007.02.

Spectroscopic and computational evaluation of the microstructure of high spine Fe(IV) oxo intermediates in taurine: ?-Ketoglutarate dioxinase from Escherichia coli and Its His99Ala Ligand Variant, Journal of the American Chemical Society, 10. 1021/ja067899q, 129, 19, (6168-6179), (2007). CRISJÖE A. Joseph and Michael J. Maroney, Cysteine Dioxygenase: Structur and Mechanisms, Chemical Communication, 10. 1039/b702158e, 32, (3338), (2007).

Fujimori, Eric W. Barr, Megan L. Matthews, Gretchen M. Koch, J. Ryan Yonce, Christopher T. Walsh, J. Martin Bollinger, Circ. Pamela J. et cetera. Spectroscopic detection of a high-spin Br-Fe(IV)-Oxo intermediate in the ketoglutarate-dependent halase ? cyclase of Streptomyces-C3, Journal of the American Chemical Society, 10. 1021/ja076454e, 129, 44, (13408-13409), (2007).

J. Bollinger, John C. Price, Lee M. Hoffart, Eric W. Barr and Carl Krebs, mechanism of taurine: ??Ketoglutarate-Ketoglutarate-Ketoglutarate-Ketoglutarate-Ketoglutarate-Ketoglutarate-Ketoglutarate-ketoglutarate dioxygenase (TauD) by Escherichia Coli Bollinger, John C. Price, Lee M. Hoffart, Eric W. Barr and Carl Krebs, mechanism of taurine: ??Ketoglutarate-Ketoglutarate-Ketoglutarate-Ketoglutarate-Ketoglutarate-Ketoglutarate-Ketoglutarate-Ketoglutarate-ketoglutarate dioxygenase (TauD) by Escherichia H Bollinger, John C. Price, Lee M. Hoffart, Eric W. Barr and Carl Krebs, mechanism of taurine: ??Ketoglutarate-Ketoglutarate-Ketoglutarate-Ketoglutarate-Ketoglutarate-Ketoglutarate-Ketoglutarate-Ketoglutarate-ketoglutarate dioxygenase (TauD) by Escherichia c. 37 Bollinger, John C. Price, Lee M. Hoffart, Eric W. Barr and Carl Krebs, mechanism of taurine: ??Ketoglutarate-Ketoglutarate-Ketoglutarate-Ketoglutarate-Ketoglutarate-Ketoglutarate-Ketoglutarate-Ketoglutarate-ketoglutarate dioxygenase (TauD) by Escherichia Coli Bollinger, Chem, Chem, Chem, Chem, Chem, Chem, Chem, Chem, Chem, Chem, Chem), Chem), Chem), Chem, Chem, Chem, Chem, Chem, Chem, Chem, Chem, Chem, Chem, Chem, Chem, Chem, Chem, Chem, Chem, Chem, Chem, Chem, Chem, Chem, Chem, Chem, Chem, Chem, Chem, Chem, and, Chem, Chem, Chem, Chem, Chem, Chem, Chem, Chem, Chem, Chem, Chem, and, Chem, Chem, Chem, Chem, and, and, Chem, and, Chem, Chem, Chem, Chem, and, Chem, and, and, Chem, and, Chem, and, Chem, and, Chem, Chem, Chem, and, Chem, Chem, and, and, Chem, and, and, Chem, and, and, and, Chem, and, and, and, and, and. John-Johns T. Groves, High-grade Ferrous in Chemistry and Biology Oxidation, Journal of Inorganic Biochemistry, 10.1016/j.jinorgbio.2006.01. Shan and Que Xiaopeng, high-quality non-hemic ferrous oxygen compounds in bio-mimetic oxidation, Journal of Inorganic Biochemistry, 10.1016/j.jinorgbio.2006.01.

J. Dr. Martin Bollinger and Dr. Cancer, human precursors in the activated oxygenation by ferrous enzymes: Motive and methodology, Journal of Inorganic Biochemistry, 10.1016/j.jinorgbio.2006.01. L. M. Hoffart, E. W. Barr, R. B. Guyer, J. M. Bollinger and CF. Krebs, Proceedings of the National Academy of Sciences, 10.1073/pnas. 0604005103, 103, 40, (14738-14743), (2006).

QM/MM and MD study, Limits of Chemistry, 10.3389/fchem.2017.

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