Artigos de revistas sobre o tema "Galactose oxidase like complexes"
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Wang, Yadong, e T. D. P. Stack. "Galactose Oxidase Model Complexes: Catalytic Reactivities". Journal of the American Chemical Society 118, n.º 51 (janeiro de 1996): 13097–98. http://dx.doi.org/10.1021/ja9621354.
Texto completo da fonteChudin, A. A., e E. V. Kudryashova. "Impact of lipid matrix composition on the activity of membranotropic enzymes galactonolactone oxidase from Trypanosoma cruzi and L-galactono-1,4-lactone dehydrogenase from <i>Arabidopsis thaliana</i> in the system of reverse micelles". Биохимия 88, n.º 12 (15 de dezembro de 2023): 2457–68. http://dx.doi.org/10.31857/s0320972523120096.
Texto completo da fonteBreza, Martin, e Stanislav Biskupič. "N-Salicylideneaminoacidato copper(II) complexes as galactose oxidase model compounds". Journal of Molecular Structure: THEOCHEM 760, n.º 1-3 (fevereiro de 2006): 141–45. http://dx.doi.org/10.1016/j.theochem.2005.12.005.
Texto completo da fonteVaidyanathan, M., K. R. Justin Thomas e M. Palaniandavar. "Models for galactose oxidase: Copper(II) complexes with axial phenolate". Journal of Inorganic Biochemistry 59, n.º 2-3 (agosto de 1995): 686. http://dx.doi.org/10.1016/0162-0134(95)97774-k.
Texto completo da fonteOshita, Hiromi, e Yuichi Shimazaki. "π–π Stacking Interaction of Metal Phenoxyl Radical Complexes". Molecules 27, n.º 3 (8 de fevereiro de 2022): 1135. http://dx.doi.org/10.3390/molecules27031135.
Texto completo da fonteVerma, P., R. C. Pratt, T. Storr, E. C. Wasinger e T. D. P. Stack. "Sulfanyl stabilization of copper-bonded phenoxyls in model complexes and galactose oxidase". Proceedings of the National Academy of Sciences 108, n.º 46 (7 de novembro de 2011): 18600–18605. http://dx.doi.org/10.1073/pnas.1109931108.
Texto completo da fonteSokolowski, Achim, Heiko Leutbecher, Thomas Weyhermüller, Robert Schnepf, Eberhard Bothe, Eckhard Bill, Peter Hildebrandt e K. Wieghardt. "Phenoxyl-copper(II) complexes: models for the active site of galactose oxidase". JBIC Journal of Biological Inorganic Chemistry 2, n.º 4 (agosto de 1997): 444–53. http://dx.doi.org/10.1007/s007750050155.
Texto completo da fontePratt, Russell C., e T. Daniel P. Stack. "Intramolecular Charge Transfer and Biomimetic Reaction Kinetics in Galactose Oxidase Model Complexes". Journal of the American Chemical Society 125, n.º 29 (julho de 2003): 8716–17. http://dx.doi.org/10.1021/ja035837j.
Texto completo da fonteFigueiredo, Carina, Carolin Psotta, Kavita Jayakumar, Anna Lielpetere, Tanushree Mandal, Wolfgang Schuhmann, Dónal Leech et al. "Effect of Protection Polymer Coatings on the Performance of an Amperometric Galactose Biosensor in Human Plasma". Biosensors 14, n.º 4 (30 de março de 2024): 167. http://dx.doi.org/10.3390/bios14040167.
Texto completo da fonteKruse, Tobias, Thomas Weyhermüller e Karl Wieghardt. "Mono- and dinuclear (o-thioetherphenolato)-copper(II) complexes. Structural models for galactose oxidase". Inorganica Chimica Acta 331, n.º 1 (março de 2002): 81–89. http://dx.doi.org/10.1016/s0020-1693(01)00756-3.
Texto completo da fonteShi, Huatian, e Yegao Yin. "Catalytic performance and mechanism of Cu(II)-hydrazone complexes as models of galactose oxidase". Inorganica Chimica Acta 421 (setembro de 2014): 446–50. http://dx.doi.org/10.1016/j.ica.2014.06.031.
Texto completo da fonteLI, Chunmin, Nobuko KANEHISA, Yasushi KAI, Shinobu ITOH, Akihiro FURUTA, Toshihiko KONDO, Mitsuo KOMATSU e Yoshiki OHSHIRO. "Synthesis and structural properties of copper complexes toward the active center model of galactose oxidase". Nihon Kessho Gakkaishi 36, Supplement (1994): 166. http://dx.doi.org/10.5940/jcrsj.36.supplement_166.
Texto completo da fonteZurita, Dacil, Corinne Scheer, Jean-Louis Pierre e Eric Saint-Aman. "Solution studies of copper(II) complexes as models for the active site in galactose oxidase". Journal of the Chemical Society, Dalton Transactions, n.º 23 (1996): 4331. http://dx.doi.org/10.1039/dt9960004331.
Texto completo da fonteLanza, Valeria, e Graziella Vecchio. "New Glycosalen–Manganese(III) Complexes and RCA120 Hybrid Systems as Superoxide Dismutase/Catalase Mimetics". Biomimetics 8, n.º 5 (21 de setembro de 2023): 447. http://dx.doi.org/10.3390/biomimetics8050447.
Texto completo da fonteDimeska, Roza, Jan Wikaira, Garry M. Mockler e Ray J. Butcher. "The crystal and molecular structures of three copper-containing complexes and their activities in mimicking galactose oxidase". Acta Crystallographica Section C Structural Chemistry 75, n.º 5 (10 de abril de 2019): 538–44. http://dx.doi.org/10.1107/s2053229619003267.
Texto completo da fontePratt, Russell C., Christopher T. Lyons, Erik C. Wasinger e T. Daniel P. Stack. "Electrochemical and Spectroscopic Effects of Mixed Substituents in Bis(phenolate)–Copper(II) Galactose Oxidase Model Complexes". Journal of the American Chemical Society 134, n.º 17 (23 de abril de 2012): 7367–77. http://dx.doi.org/10.1021/ja211247f.
Texto completo da fonteTaki, Masayasu, Haruna Hattori, Takao Osako, Shigenori Nagatomo, Motoo Shiro, Teizo Kitagawa e Shinobu Itoh. "Model complexes of the active site of galactose oxidase. Effects of the metal ion binding sites". Inorganica Chimica Acta 357, n.º 11 (agosto de 2004): 3369–81. http://dx.doi.org/10.1016/j.ica.2004.04.008.
Texto completo da fonteLyons, Christopher T., e T. Daniel P. Stack. "Recent advances in phenoxyl radical complexes of salen-type ligands as mixed-valent galactose oxidase models". Coordination Chemistry Reviews 257, n.º 2 (janeiro de 2013): 528–40. http://dx.doi.org/10.1016/j.ccr.2012.06.003.
Texto completo da fonteItoh, Shinobu, Masayasu Taki, Hideyuki Kumei, Shigehisa Takayama, Shigenori Nagatomo, Teizo Kitagawa, Norio Sakurada, Ryuichi Arakawa e Shunichi Fukuzumi. "Model Complexes for the Active Form of Galactose Oxidase. Physicochemical Properties of Cu(II)− and Zn(II)−Phenoxyl Radical Complexes". Inorganic Chemistry 39, n.º 16 (agosto de 2000): 3708–11. http://dx.doi.org/10.1021/ic9910211.
Texto completo da fonteSarkar, Nandita, Klaus Harms, Antonio Frontera e Shouvik Chattopadhyay. "Importance of C–H⋯π interactions in stabilizing the syn/anti arrangement of pendant alkoxy side arms in two manganese(iv) Schiff base complexes: exploration of catechol oxidase and phenoxazinone synthase like activities". New Journal of Chemistry 41, n.º 16 (2017): 8053–65. http://dx.doi.org/10.1039/c7nj00766c.
Texto completo da fonteAdams, Harry, Neil A. Bailey, Cecilia O. Rodriguez de Barbarin, David E. Fenton e Qing-Yu He. "Heteroleptic tripodal complexes of copper(II): towards a synthetic model for the active site in galactose oxidase". Journal of the Chemical Society, Dalton Transactions, n.º 14 (1995): 2323. http://dx.doi.org/10.1039/dt9950002323.
Texto completo da fonteSaysell, Colin G., Christopher D. Borman, Andrew J. Baron, Michael J. McPherson e A. Geoffrey Sykes. "Kinetic Studies on the Redox Interconversion of GOasesemiand GOaseoxForms of Galactose Oxidase with Inorganic Complexes as Redox Partners". Inorganic Chemistry 36, n.º 20 (setembro de 1997): 4520–25. http://dx.doi.org/10.1021/ic970255m.
Texto completo da fonteShimazaki, Yuichi, Stefan Huth, Shun Hirota e Osamu Yamauchi. "Studies on galactose oxidase active site model complexes: effects of ring substituents on Cu(II)-phenoxyl radical formation". Inorganica Chimica Acta 331, n.º 1 (março de 2002): 168–77. http://dx.doi.org/10.1016/s0020-1693(01)00781-2.
Texto completo da fonteShimazaki, Yuichi. "Properties of the one-electron oxidized copper(II) salen-type complexes: relationship between electronic structures and reactivities". Pure and Applied Chemistry 86, n.º 2 (1 de fevereiro de 2014): 163–72. http://dx.doi.org/10.1515/pac-2014-5022.
Texto completo da fonteAhamad, M. Naqi, Manjeet Kumar, Azaj Ansari, Mantasha I., Musheer Ahmad e M. Shahid. "Synthesis, characterization, theoretical studies and catecholase like activities of [MO6] type complexes". New Journal of Chemistry 43, n.º 35 (2019): 14074–83. http://dx.doi.org/10.1039/c9nj03729b.
Texto completo da fonteAuernik, Kathryne S., e Robert M. Kelly. "Identification of Components of Electron Transport Chains in the Extremely Thermoacidophilic Crenarchaeon Metallosphaera sedula through Iron and Sulfur Compound Oxidation Transcriptomes". Applied and Environmental Microbiology 74, n.º 24 (17 de outubro de 2008): 7723–32. http://dx.doi.org/10.1128/aem.01545-08.
Texto completo da fonteRomanowski, Stela Maris de M., Francielen Tormena, Viviane A. dos Santos, Monique de F. Hermann e Antonio S. Mangrich. "Solution studies of copper(II) complexes as a contribution to the study of the active site of galactose oxidase". Journal of the Brazilian Chemical Society 15, n.º 6 (dezembro de 2004): 897–903. http://dx.doi.org/10.1590/s0103-50532004000600017.
Texto completo da fonteJazdzewski, Brian A., Anne M. Reynolds, Patrick L. Holland, Victor G. Young, Susan Kaderli, Andreas D. Zuberbühler e William B. Tolman. "Copper(I)-phenolate complexes as models of the reduced active site of galactose oxidase: synthesis, characterization, and O2 reactivity". JBIC Journal of Biological Inorganic Chemistry 8, n.º 4 (18 de fevereiro de 2003): 381–93. http://dx.doi.org/10.1007/s00775-002-0420-9.
Texto completo da fonteLiman, Recep, Paul D. Facey, Geertje van Keulen, Paul J. Dyson e Ricardo Del Sol. "A Laterally Acquired Galactose Oxidase-Like Gene Is Required for Aerial Development during Osmotic Stress in Streptomyces coelicolor". PLoS ONE 8, n.º 1 (11 de janeiro de 2013): e54112. http://dx.doi.org/10.1371/journal.pone.0054112.
Texto completo da fonteAlaji, Zahra, Elham Safaei, Hong Yi, Hengjiang Cong, Andrzej Wojtczak e Aiwen Lei. "Redox active ligand and metal cooperation for C(sp2)–H oxidation: extension of the galactose oxidase mechanism in water-mediated amide formation". Dalton Transactions 47, n.º 43 (2018): 15293–97. http://dx.doi.org/10.1039/c8dt03477j.
Texto completo da fonteClark, Kimber, James E. Penner-Hahn, Mei M. Whittaker e James W. Whittaker. "Oxidation-state assignments for galactose oxidase complexes from x-ray absorption spectroscopy. Evidence for copper(II) in the active enzyme". Journal of the American Chemical Society 112, n.º 17 (agosto de 1990): 6433–34. http://dx.doi.org/10.1021/ja00173a061.
Texto completo da fonteTaki, Masayasu, Hideyuki Kumei, Shinobu Itoh* e Shunichi Fukuzumi*. "Hydrogen atom abstraction by Cu(II)- and Zn(II)-phenoxyl radical complexes, models for the active form of galactose oxidase". Journal of Inorganic Biochemistry 78, n.º 1 (janeiro de 2000): 1–5. http://dx.doi.org/10.1016/s0162-0134(99)00198-1.
Texto completo da fonteVaidyanathan, Mathrubootham, e Mallayan Palaniandavar. "Models for the active site in galactose oxidase: Structure, spectra and redox of copper(II) complexes of certain phenolate ligands". Journal of Chemical Sciences 112, n.º 3 (junho de 2000): 223–38. http://dx.doi.org/10.1007/bf02706175.
Texto completo da fonteAnjos, Ademir dos, Adailton J. Bortoluzzi, Renata E. H. M. B. Osório, Rosely A. Peralta, Geraldo R. Friedermann, Antonio S. Mangrich e Ademir Neves. "New mononuclear CuII and ZnII complexes capable of stabilizing phenoxyl radicals as models for the active form of galactose oxidase". Inorganic Chemistry Communications 8, n.º 3 (março de 2005): 249–53. http://dx.doi.org/10.1016/j.inoche.2004.12.022.
Texto completo da fonteOrio, Maylis, Olivier Jarjayes, Hussein Kanso, Christian Philouze, Frank Neese e Fabrice Thomas. "X-Ray Structures of Copper(II) and Nickel(II) Radical Salen Complexes: The Preference of Galactose Oxidase for Copper(II)". Angewandte Chemie International Edition 49, n.º 29 (23 de abril de 2010): 4989–92. http://dx.doi.org/10.1002/anie.201001040.
Texto completo da fonteOrio, Maylis, Olivier Jarjayes, Hussein Kanso, Christian Philouze, Frank Neese e Fabrice Thomas. "X-Ray Structures of Copper(II) and Nickel(II) Radical Salen Complexes: The Preference of Galactose Oxidase for Copper(II)". Angewandte Chemie 122, n.º 29 (23 de abril de 2010): 5109–12. http://dx.doi.org/10.1002/ange.201001040.
Texto completo da fonteKERN, Renée, Abderrahim MALKI, Arne HOLMGREN e Gilbert RICHARME. "Chaperone properties of Escherichia coli thioredoxin and thioredoxin reductase". Biochemical Journal 371, n.º 3 (1 de maio de 2003): 965–72. http://dx.doi.org/10.1042/bj20030093.
Texto completo da fonteKrichevsky, Alexander, Stanislav V. Kozlovsky, Helen Gutgarts e Vitaly Citovsky. "Arabidopsis Co-Repressor Complexes Containing Polyamine Oxidase-Like Proteins and Plant-Specific Histone Methyltransferases". Plant Signaling & Behavior 2, n.º 3 (maio de 2007): 174–77. http://dx.doi.org/10.4161/psb.2.3.3726.
Texto completo da fonteBarrio, Daniel A., Elizabeth R. Cattáneo, María C. Apezteguía e Susana B. Etcheverry. "Vanadyl(IV) complexes with saccharides. Bioactivity in osteoblast-like cells in cultureThis paper is one of a selection of papers published in this Special issue, enititled Second Messengers and Phosphoproteins—12th International Conference." Canadian Journal of Physiology and Pharmacology 84, n.º 7 (julho de 2006): 765–75. http://dx.doi.org/10.1139/y06-021.
Texto completo da fonteSingha Mahapatra, Tufan, Dipmalya Basak, Santanu Chand, Jeff Lengyel, Michael Shatruk, Valerio Bertolasi e Debashis Ray. "Competitive coordination aggregation for V-shaped [Co3] and disc-like [Co7] complexes: synthesis, magnetic properties and catechol oxidase activity". Dalton Transactions 45, n.º 34 (2016): 13576–89. http://dx.doi.org/10.1039/c6dt02494g.
Texto completo da fonteItoh, Shinobu, Masayasu Taki, Shigehisa Takayama, Shigenori Nagatomo, Teizo Kitagawa, Norio Sakurada, Ryuichi Arakawa e Shunichi Fukuzumi. "Oxidation of Benzyl Alcohol with CuII and ZnII Complexes of the Phenoxyl Radical as a Model of the Reaction of Galactose Oxidase". Angewandte Chemie International Edition 38, n.º 18 (17 de setembro de 1999): 2774–76. http://dx.doi.org/10.1002/(sici)1521-3773(19990917)38:18<2774::aid-anie2774>3.0.co;2-e.
Texto completo da fonteVaidyanathan, Mathrubootham, Mallayan Palaniandavar e R. Srinivasa Gopalan. "Copper(II) complexes of sterically hindered phenolate ligands as structural models for the active site in galactose oxidase and glyoxal oxidase: X-ray crystal structure and spectral and redox properties". Inorganica Chimica Acta 324, n.º 1-2 (novembro de 2001): 241–51. http://dx.doi.org/10.1016/s0020-1693(01)00606-5.
Texto completo da fonteMatyuska, Ferenc, Nóra V. May, Attila Bényei e Tamás Gajda. "Control of structure, stability and catechol oxidase activity of copper(ii) complexes by the denticity of tripodal platforms". New Journal of Chemistry 41, n.º 20 (2017): 11647–60. http://dx.doi.org/10.1039/c7nj02013a.
Texto completo da fonteYamato, Kazuhiro, Takanori Inada, Matsumi Doe, Akio Ichimura, Takeji Takui, Yoshitane Kojima, Toshimitsu Kikunaga et al. "Preparations and Characterizations of NovelN,N′-Ethylene-Bridged-(S)-Histidyl-(S)-Tyrosine Derivatives and Their Copper(II) Complexes as Models of Galactose Oxidase". Bulletin of the Chemical Society of Japan 73, n.º 4 (abril de 2000): 903–12. http://dx.doi.org/10.1246/bcsj.73.903.
Texto completo da fonteTakahashi, Shinichiro, Shigeru Taketani, Jun-etsu Akasaka, Akira Kobayashi, Norio Hayashi, Masayuki Yamamoto e Tadashi Nagai. "Differential Regulation of Coproporphyrinogen Oxidase Gene Between Erythroid and Nonerythroid Cells". Blood 92, n.º 9 (1 de novembro de 1998): 3436–44. http://dx.doi.org/10.1182/blood.v92.9.3436.
Texto completo da fonteTakahashi, Shinichiro, Shigeru Taketani, Jun-etsu Akasaka, Akira Kobayashi, Norio Hayashi, Masayuki Yamamoto e Tadashi Nagai. "Differential Regulation of Coproporphyrinogen Oxidase Gene Between Erythroid and Nonerythroid Cells". Blood 92, n.º 9 (1 de novembro de 1998): 3436–44. http://dx.doi.org/10.1182/blood.v92.9.3436.421k13_3436_3444.
Texto completo da fonteWu, Ru Feng, You Cheng Xu, Zhenyi Ma, Fiemu E. Nwariaku, George A. Sarosi e Lance S. Terada. "Subcellular targeting of oxidants during endothelial cell migration". Journal of Cell Biology 171, n.º 5 (5 de dezembro de 2005): 893–904. http://dx.doi.org/10.1083/jcb.200507004.
Texto completo da fonteKustov, Andrey V., Philipp K. Morshnev, Natal’ya V. Kukushkina, Nataliya L. Smirnova, Dmitry B. Berezin, Dmitry R. Karimov, Olga V. Shukhto et al. "Solvation, Cancer Cell Photoinactivation and the Interaction of Chlorin Photosensitizers with a Potential Passive Carrier Non-Ionic Surfactant Tween 80". International Journal of Molecular Sciences 23, n.º 10 (10 de maio de 2022): 5294. http://dx.doi.org/10.3390/ijms23105294.
Texto completo da fonteDancs, Ágnes, Nóra V. May, Katalin Selmeczi, Zsuzsanna Darula, Attila Szorcsik, Ferenc Matyuska, Tibor Páli e Tamás Gajda. "Tuning the coordination properties of multi-histidine peptides by using a tripodal scaffold: solution chemical study and catechol oxidase mimicking". New Journal of Chemistry 41, n.º 2 (2017): 808–23. http://dx.doi.org/10.1039/c6nj03126a.
Texto completo da fonteYoneda, Kazunari, Haruhiko Sakuraba, Tomohiro Araki e Toshihisa Ohshima. "Crystal Structure of Binary and Ternary Complexes of Archaeal UDP-galactose 4-Epimerase-like l-Threonine Dehydrogenase fromThermoplasma volcanium". Journal of Biological Chemistry 287, n.º 16 (28 de fevereiro de 2012): 12966–74. http://dx.doi.org/10.1074/jbc.m111.336958.
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