Zeitschriftenartikel zum Thema „Galactose oxidase like complexes“
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Wang, Yadong, und T. D. P. Stack. „Galactose Oxidase Model Complexes: Catalytic Reactivities“. Journal of the American Chemical Society 118, Nr. 51 (Januar 1996): 13097–98. http://dx.doi.org/10.1021/ja9621354.
Chudin, A. A., und 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, Nr. 12 (15.12.2023): 2457–68. http://dx.doi.org/10.31857/s0320972523120096.
Breza, Martin, und Stanislav Biskupič. „N-Salicylideneaminoacidato copper(II) complexes as galactose oxidase model compounds“. Journal of Molecular Structure: THEOCHEM 760, Nr. 1-3 (Februar 2006): 141–45. http://dx.doi.org/10.1016/j.theochem.2005.12.005.
Vaidyanathan, M., K. R. Justin Thomas und M. Palaniandavar. „Models for galactose oxidase: Copper(II) complexes with axial phenolate“. Journal of Inorganic Biochemistry 59, Nr. 2-3 (August 1995): 686. http://dx.doi.org/10.1016/0162-0134(95)97774-k.
Oshita, Hiromi, und Yuichi Shimazaki. „π–π Stacking Interaction of Metal Phenoxyl Radical Complexes“. Molecules 27, Nr. 3 (08.02.2022): 1135. http://dx.doi.org/10.3390/molecules27031135.
Verma, P., R. C. Pratt, T. Storr, E. C. Wasinger und T. D. P. Stack. „Sulfanyl stabilization of copper-bonded phenoxyls in model complexes and galactose oxidase“. Proceedings of the National Academy of Sciences 108, Nr. 46 (07.11.2011): 18600–18605. http://dx.doi.org/10.1073/pnas.1109931108.
Sokolowski, Achim, Heiko Leutbecher, Thomas Weyhermüller, Robert Schnepf, Eberhard Bothe, Eckhard Bill, Peter Hildebrandt und K. Wieghardt. „Phenoxyl-copper(II) complexes: models for the active site of galactose oxidase“. JBIC Journal of Biological Inorganic Chemistry 2, Nr. 4 (August 1997): 444–53. http://dx.doi.org/10.1007/s007750050155.
Pratt, Russell C., und T. Daniel P. Stack. „Intramolecular Charge Transfer and Biomimetic Reaction Kinetics in Galactose Oxidase Model Complexes“. Journal of the American Chemical Society 125, Nr. 29 (Juli 2003): 8716–17. http://dx.doi.org/10.1021/ja035837j.
Figueiredo, 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, Nr. 4 (30.03.2024): 167. http://dx.doi.org/10.3390/bios14040167.
Kruse, Tobias, Thomas Weyhermüller und Karl Wieghardt. „Mono- and dinuclear (o-thioetherphenolato)-copper(II) complexes. Structural models for galactose oxidase“. Inorganica Chimica Acta 331, Nr. 1 (März 2002): 81–89. http://dx.doi.org/10.1016/s0020-1693(01)00756-3.
Shi, Huatian, und Yegao Yin. „Catalytic performance and mechanism of Cu(II)-hydrazone complexes as models of galactose oxidase“. Inorganica Chimica Acta 421 (September 2014): 446–50. http://dx.doi.org/10.1016/j.ica.2014.06.031.
LI, Chunmin, Nobuko KANEHISA, Yasushi KAI, Shinobu ITOH, Akihiro FURUTA, Toshihiko KONDO, Mitsuo KOMATSU und 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.
Zurita, Dacil, Corinne Scheer, Jean-Louis Pierre und 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, Nr. 23 (1996): 4331. http://dx.doi.org/10.1039/dt9960004331.
Lanza, Valeria, und Graziella Vecchio. „New Glycosalen–Manganese(III) Complexes and RCA120 Hybrid Systems as Superoxide Dismutase/Catalase Mimetics“. Biomimetics 8, Nr. 5 (21.09.2023): 447. http://dx.doi.org/10.3390/biomimetics8050447.
Dimeska, Roza, Jan Wikaira, Garry M. Mockler und 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, Nr. 5 (10.04.2019): 538–44. http://dx.doi.org/10.1107/s2053229619003267.
Pratt, Russell C., Christopher T. Lyons, Erik C. Wasinger und 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, Nr. 17 (23.04.2012): 7367–77. http://dx.doi.org/10.1021/ja211247f.
Taki, Masayasu, Haruna Hattori, Takao Osako, Shigenori Nagatomo, Motoo Shiro, Teizo Kitagawa und Shinobu Itoh. „Model complexes of the active site of galactose oxidase. Effects of the metal ion binding sites“. Inorganica Chimica Acta 357, Nr. 11 (August 2004): 3369–81. http://dx.doi.org/10.1016/j.ica.2004.04.008.
Lyons, Christopher T., und T. Daniel P. Stack. „Recent advances in phenoxyl radical complexes of salen-type ligands as mixed-valent galactose oxidase models“. Coordination Chemistry Reviews 257, Nr. 2 (Januar 2013): 528–40. http://dx.doi.org/10.1016/j.ccr.2012.06.003.
Itoh, Shinobu, Masayasu Taki, Hideyuki Kumei, Shigehisa Takayama, Shigenori Nagatomo, Teizo Kitagawa, Norio Sakurada, Ryuichi Arakawa und 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, Nr. 16 (August 2000): 3708–11. http://dx.doi.org/10.1021/ic9910211.
Sarkar, Nandita, Klaus Harms, Antonio Frontera und 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, Nr. 16 (2017): 8053–65. http://dx.doi.org/10.1039/c7nj00766c.
Adams, Harry, Neil A. Bailey, Cecilia O. Rodriguez de Barbarin, David E. Fenton und 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, Nr. 14 (1995): 2323. http://dx.doi.org/10.1039/dt9950002323.
Saysell, Colin G., Christopher D. Borman, Andrew J. Baron, Michael J. McPherson und A. Geoffrey Sykes. „Kinetic Studies on the Redox Interconversion of GOasesemiand GOaseoxForms of Galactose Oxidase with Inorganic Complexes as Redox Partners“. Inorganic Chemistry 36, Nr. 20 (September 1997): 4520–25. http://dx.doi.org/10.1021/ic970255m.
Shimazaki, Yuichi, Stefan Huth, Shun Hirota und Osamu Yamauchi. „Studies on galactose oxidase active site model complexes: effects of ring substituents on Cu(II)-phenoxyl radical formation“. Inorganica Chimica Acta 331, Nr. 1 (März 2002): 168–77. http://dx.doi.org/10.1016/s0020-1693(01)00781-2.
Shimazaki, Yuichi. „Properties of the one-electron oxidized copper(II) salen-type complexes: relationship between electronic structures and reactivities“. Pure and Applied Chemistry 86, Nr. 2 (01.02.2014): 163–72. http://dx.doi.org/10.1515/pac-2014-5022.
Ahamad, M. Naqi, Manjeet Kumar, Azaj Ansari, Mantasha I., Musheer Ahmad und M. Shahid. „Synthesis, characterization, theoretical studies and catecholase like activities of [MO6] type complexes“. New Journal of Chemistry 43, Nr. 35 (2019): 14074–83. http://dx.doi.org/10.1039/c9nj03729b.
Auernik, Kathryne S., und 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, Nr. 24 (17.10.2008): 7723–32. http://dx.doi.org/10.1128/aem.01545-08.
Romanowski, Stela Maris de M., Francielen Tormena, Viviane A. dos Santos, Monique de F. Hermann und 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, Nr. 6 (Dezember 2004): 897–903. http://dx.doi.org/10.1590/s0103-50532004000600017.
Jazdzewski, Brian A., Anne M. Reynolds, Patrick L. Holland, Victor G. Young, Susan Kaderli, Andreas D. Zuberbühler und 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, Nr. 4 (18.02.2003): 381–93. http://dx.doi.org/10.1007/s00775-002-0420-9.
Liman, Recep, Paul D. Facey, Geertje van Keulen, Paul J. Dyson und Ricardo Del Sol. „A Laterally Acquired Galactose Oxidase-Like Gene Is Required for Aerial Development during Osmotic Stress in Streptomyces coelicolor“. PLoS ONE 8, Nr. 1 (11.01.2013): e54112. http://dx.doi.org/10.1371/journal.pone.0054112.
Alaji, Zahra, Elham Safaei, Hong Yi, Hengjiang Cong, Andrzej Wojtczak und 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, Nr. 43 (2018): 15293–97. http://dx.doi.org/10.1039/c8dt03477j.
Clark, Kimber, James E. Penner-Hahn, Mei M. Whittaker und 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, Nr. 17 (August 1990): 6433–34. http://dx.doi.org/10.1021/ja00173a061.
Taki, Masayasu, Hideyuki Kumei, Shinobu Itoh* und 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, Nr. 1 (Januar 2000): 1–5. http://dx.doi.org/10.1016/s0162-0134(99)00198-1.
Vaidyanathan, Mathrubootham, und 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, Nr. 3 (Juni 2000): 223–38. http://dx.doi.org/10.1007/bf02706175.
Anjos, Ademir dos, Adailton J. Bortoluzzi, Renata E. H. M. B. Osório, Rosely A. Peralta, Geraldo R. Friedermann, Antonio S. Mangrich und 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, Nr. 3 (März 2005): 249–53. http://dx.doi.org/10.1016/j.inoche.2004.12.022.
Orio, Maylis, Olivier Jarjayes, Hussein Kanso, Christian Philouze, Frank Neese und 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, Nr. 29 (23.04.2010): 4989–92. http://dx.doi.org/10.1002/anie.201001040.
Orio, Maylis, Olivier Jarjayes, Hussein Kanso, Christian Philouze, Frank Neese und 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, Nr. 29 (23.04.2010): 5109–12. http://dx.doi.org/10.1002/ange.201001040.
KERN, Renée, Abderrahim MALKI, Arne HOLMGREN und Gilbert RICHARME. „Chaperone properties of Escherichia coli thioredoxin and thioredoxin reductase“. Biochemical Journal 371, Nr. 3 (01.05.2003): 965–72. http://dx.doi.org/10.1042/bj20030093.
Krichevsky, Alexander, Stanislav V. Kozlovsky, Helen Gutgarts und Vitaly Citovsky. „Arabidopsis Co-Repressor Complexes Containing Polyamine Oxidase-Like Proteins and Plant-Specific Histone Methyltransferases“. Plant Signaling & Behavior 2, Nr. 3 (Mai 2007): 174–77. http://dx.doi.org/10.4161/psb.2.3.3726.
Barrio, Daniel A., Elizabeth R. Cattáneo, María C. Apezteguía und 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, Nr. 7 (Juli 2006): 765–75. http://dx.doi.org/10.1139/y06-021.
Singha Mahapatra, Tufan, Dipmalya Basak, Santanu Chand, Jeff Lengyel, Michael Shatruk, Valerio Bertolasi und Debashis Ray. „Competitive coordination aggregation for V-shaped [Co3] and disc-like [Co7] complexes: synthesis, magnetic properties and catechol oxidase activity“. Dalton Transactions 45, Nr. 34 (2016): 13576–89. http://dx.doi.org/10.1039/c6dt02494g.
Itoh, Shinobu, Masayasu Taki, Shigehisa Takayama, Shigenori Nagatomo, Teizo Kitagawa, Norio Sakurada, Ryuichi Arakawa und 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, Nr. 18 (17.09.1999): 2774–76. http://dx.doi.org/10.1002/(sici)1521-3773(19990917)38:18<2774::aid-anie2774>3.0.co;2-e.
Vaidyanathan, Mathrubootham, Mallayan Palaniandavar und 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, Nr. 1-2 (November 2001): 241–51. http://dx.doi.org/10.1016/s0020-1693(01)00606-5.
Matyuska, Ferenc, Nóra V. May, Attila Bényei und 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, Nr. 20 (2017): 11647–60. http://dx.doi.org/10.1039/c7nj02013a.
Yamato, 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, Nr. 4 (April 2000): 903–12. http://dx.doi.org/10.1246/bcsj.73.903.
Takahashi, Shinichiro, Shigeru Taketani, Jun-etsu Akasaka, Akira Kobayashi, Norio Hayashi, Masayuki Yamamoto und Tadashi Nagai. „Differential Regulation of Coproporphyrinogen Oxidase Gene Between Erythroid and Nonerythroid Cells“. Blood 92, Nr. 9 (01.11.1998): 3436–44. http://dx.doi.org/10.1182/blood.v92.9.3436.
Takahashi, Shinichiro, Shigeru Taketani, Jun-etsu Akasaka, Akira Kobayashi, Norio Hayashi, Masayuki Yamamoto und Tadashi Nagai. „Differential Regulation of Coproporphyrinogen Oxidase Gene Between Erythroid and Nonerythroid Cells“. Blood 92, Nr. 9 (01.11.1998): 3436–44. http://dx.doi.org/10.1182/blood.v92.9.3436.421k13_3436_3444.
Wu, Ru Feng, You Cheng Xu, Zhenyi Ma, Fiemu E. Nwariaku, George A. Sarosi und Lance S. Terada. „Subcellular targeting of oxidants during endothelial cell migration“. Journal of Cell Biology 171, Nr. 5 (05.12.2005): 893–904. http://dx.doi.org/10.1083/jcb.200507004.
Kustov, 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, Nr. 10 (10.05.2022): 5294. http://dx.doi.org/10.3390/ijms23105294.
Dancs, Ágnes, Nóra V. May, Katalin Selmeczi, Zsuzsanna Darula, Attila Szorcsik, Ferenc Matyuska, Tibor Páli und 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, Nr. 2 (2017): 808–23. http://dx.doi.org/10.1039/c6nj03126a.
Yoneda, Kazunari, Haruhiko Sakuraba, Tomohiro Araki und 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, Nr. 16 (28.02.2012): 12966–74. http://dx.doi.org/10.1074/jbc.m111.336958.