Auswahl der wissenschaftlichen Literatur zum Thema „Galactose oxidase like complexes“
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Zeitschriftenartikel zum Thema "Galactose oxidase like complexes":
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.
Dissertationen zum Thema "Galactose oxidase like complexes":
Wang, Guanqi. „Etat d'oxydation élevé des complexes de cuivre de type galactose oxydase pour l'oxydation biomimétique de l'alcool“. Electronic Thesis or Diss., Université Grenoble Alpes, 2023. http://www.theses.fr/2023GRALV106.
Galactose Oxidase (GOase), a copper-containing metallo-enzyme, is one of the most studied biocatalysts for the enzymatic oxidation of carbohydrates. The consensus mechanism involves the key oxidized form (GOaseox), in which an the carbohydrate substrate (galactose unit) binds to the equatorial (free) site and is subsequently deprotonated. It undergoes hydrogen atom abstraction by the radical and further electron transfer to give the final product aldehyde and the reduced form of the GOase. Due to the potential for highly selective catalytic oxidations, the development of small-molecular models of the GOase active site has been carried out. Notably, sterically hindered schiff bases, which stand as one of the most representative mimics, have garnered significant attention. This biomimetic approach has extended to encompass other strategies. Within this framework, a range of Cu(II)-phenol complexes, serving as pre-catalysts, have been synthesized, subsequently undergoing one-electron oxidation to yield the "active" catalyst form. A central question then arises: What factors determine whether the oxidation pathway proceeds toward the ligand, resulting in the formation of Cu(II)-phenoxyl radicals, or toward the metal, giving rise to the Cu(III)-phenolate species? Despite substantial efforts, a definitive answer to this question has yet to be obtained.The aim of this thesis is to develop redox-active ligands aimed at understanding the factors affecting the oxidation state of copper, able to catalyze the oxidation of an alcohol into an aldehyde. The strategy is to include chemical functions that can stabilize either valence tautomer (Cu(II)-phenoxyl radical and Cu(III)-phenolate) and study their effect. For that purpose, several complexes were synthesized and characterized by different ways to understand their properties. The catalytic activities were also tested against different families of substrates comprising hydroxyl functions. Finally, quantum chemistry (DFT) calculations have been carried to help understand the characteristics of different complexes and elucidate of the catalytic mechanisms at work
Marshall, George. „Transition metal diphenolate and dithiophenolate complexes as synthetic analogues of the active sites of nickel superoxide dismutase and galactose oxidase“. Thesis, University of Nottingham, 2016. http://eprints.nottingham.ac.uk/36240/.
„Syntheses and structures of copper and zinc complexes with N₃O donor ligands“. 2001. http://library.cuhk.edu.hk/record=b5895872.
Thesis (M.Phil.)--Chinese University of Hong Kong, 2001.
Includes bibliographical references.
Abstracts in English and Chinese.
ABSTRACT --- p.i
摘要 --- p.ii
ACKNOWLEDGMENT --- p.iii
CONTENTS --- p.iv
ABBREVIATIONS --- p.vi
Chapter CHAPTER 1 --- General Introduction
Chapter 1-A. --- Role of Copper in Biology --- p.1
Chapter 1-B. --- A Brief Review on Radical Copper Proteins --- p.4
Chapter 1-C. --- Objectives of This Work --- p.12
Chapter 1-D. --- References --- p.13
Chapter CHAPTER 2 --- Copper(II) and Zinc(II) Complexes containing N3O Tetradentate Ligands
Chapter 2-A. --- Introduction Results and Discussion --- p.14
Chapter 2-B. --- Preparation of Tetradentate Ligands and Complexes --- p.27
Chapter 2-C. --- Characterization --- p.36
Chapter 2-D. --- Generation of Metal Phenoxyl Radical Species --- p.51
Chapter 2-E. --- Summary --- p.57
Chapter 2-F. --- References --- p.59
Chapter CHAPTER 3 --- Copper(I) Complexes with N30 Tetradentate Ligands
Chapter 3-A. --- Introduction Results and Discussion --- p.62
Chapter 3-B. --- Preparation of Copper(I) Complexes with N30 Tetradentate Ligands --- p.75
Chapter 3-C. --- Characterization --- p.79
Chapter 3-D. --- Reactivities of 86,87 and 88 toward Dioxygen --- p.88
Chapter 3-E. --- Summary --- p.93
Chapter 3-F. --- References --- p.94
Chapter CHAPTER 4 --- Experimental Sections
Chapter 4-A. --- General Preparations and Physical Measurements --- p.97
Chapter 4-B. --- Compounds Described in Chapter2 --- p.99
Chapter 4-C. --- Compounds Described in Chapter3 --- p.113
Chapter 4-D. --- Oxo-Transfer to Triphenylphosphine as Described in Chapter3 --- p.117
Chapter 4-E. --- References --- p.119
Chapter APPENDIX A --- 1H and13 C̐ưث1H ̐ưحNMR Spectra
Chapter A-1. --- Compounds Described in Chapter2 --- p.120
Chapter A-2. --- Compounds Described in Chapter3 --- p.127
Chapter APPENDIX B --- Crystallographic Data
Chapter B-1. --- X-ray Crystal Structure Data for Complexes in Chapter2 --- p.131
Chapter B-2. --- X-ray Crystal Structure Data for Complexes in Chapter3 --- p.133
Chapter APPENDIX C --- GC-MS Spectra
Chapter C-1. --- GC-MS Spectra for Standard Samples --- p.134
Chapter C-2. --- GC-MS Spectra for the Reactions with Triphenylphosphine Described in Chapter3 --- p.136
Buchteile zum Thema "Galactose oxidase like complexes":
Schmitt, Mark E., und Bernard L. Trumpower. „A Calmodulin-Like Protein in the Cytochrome bc1 Complex Required for Synthesis of both Cytochrome bc1 and Cytochrome c Oxidase Complexes in Yeast Mitochondria“. In Cytochrome Systems, 177–87. Boston, MA: Springer US, 1987. http://dx.doi.org/10.1007/978-1-4613-1941-2_25.