Literatura académica sobre el tema "Complexes de type galactose oxydase"
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Artículos de revistas sobre el tema "Complexes de type galactose oxydase":
Ramkumar, R., A. Surolia y S. K. Podder. "Energetics of carbohydrate binding by a 14 kDa S-type mammalian lectin". Biochemical Journal 308, n.º 1 (15 de mayo de 1995): 237–41. http://dx.doi.org/10.1042/bj3080237.
Hatakeyama, Tomomitsu, Takuro Kamiya, Masami Kusunoki, Sachiko Nakamura-Tsuruta, Jun Hirabayashi, Shuichiro Goda y Hideaki Unno. "Galactose Recognition by a Tetrameric C-type Lectin, CEL-IV, Containing the EPN Carbohydrate Recognition Motif". Journal of Biological Chemistry 286, n.º 12 (19 de enero de 2011): 10305–15. http://dx.doi.org/10.1074/jbc.m110.200576.
Holzer, Isabelle, Oksana Desiatkina, Nicoleta Anghel, Serena K. Johns, Ghalia Boubaker, Andrew Hemphill, Julien Furrer y Emilia Păunescu. "Synthesis and Antiparasitic Activity of New Trithiolato-Bridged Dinuclear Ruthenium(II)-arene-carbohydrate Conjugates". Molecules 28, n.º 2 (16 de enero de 2023): 902. http://dx.doi.org/10.3390/molecules28020902.
Lyons, Christopher T. y 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 (enero de 2013): 528–40. http://dx.doi.org/10.1016/j.ccr.2012.06.003.
Shimazaki, 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 febrero de 2014): 163–72. http://dx.doi.org/10.1515/pac-2014-5022.
Kovalchuk, Svetlana, Nina Buinovskaya, Galina Likhatskaya, Valery Rasskazov, Oksana Son, Liudmila Tekutyeva y Larissa Balabanova. "Mutagenesis Studies and Structure-function Relationships for GalNAc/Gal-Specific Lectin from the Sea Mussel Crenomytilus grayanus". Marine Drugs 16, n.º 12 (27 de noviembre de 2018): 471. http://dx.doi.org/10.3390/md16120471.
Wold, J. K., H. S. Slayter, J. F. Codington y R. W. Jeanloz. "Location of an epitopic site on epiglycanin by molecular immunoelectron microscopy". Biochemical Journal 227, n.º 1 (1 de abril de 1985): 231–37. http://dx.doi.org/10.1042/bj2270231.
Mimuro, J., RR Schleef y DJ Loskutoff. "Extracellular matrix of cultured bovine aortic endothelial cells contains functionally active type 1 plasminogen activator inhibitor". Blood 70, n.º 3 (1 de septiembre de 1987): 721–28. http://dx.doi.org/10.1182/blood.v70.3.721.721.
Mimuro, J., RR Schleef y DJ Loskutoff. "Extracellular matrix of cultured bovine aortic endothelial cells contains functionally active type 1 plasminogen activator inhibitor". Blood 70, n.º 3 (1 de septiembre de 1987): 721–28. http://dx.doi.org/10.1182/blood.v70.3.721.bloodjournal703721.
Rossi, J. M. y S. Lindquist. "The intracellular location of yeast heat-shock protein 26 varies with metabolism." Journal of Cell Biology 108, n.º 2 (1 de febrero de 1989): 425–39. http://dx.doi.org/10.1083/jcb.108.2.425.
Tesis sobre el tema "Complexes de type galactose oxydase":
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
Pawlik, Grzegorz. "Assembly and maturation of cbb3-type cytochrome c oxidase in Rhodobacter capsulatus". Thesis, Strasbourg, 2012. http://www.theses.fr/2012STRAF070.
In this thesis, the assembly and maturation process of the cbb3-type cytochrome c oxidase (cbb3-Cox) was studied in the purple-non-sulphur phototrophic α-proteobacterium Rhodobacter capsulatus. R. capsulatus contains a highly branched electron-transfer chain and is a well studied model organism for investigating respiratory and photosynthetic processes.The bacteria-specific cbb3-Coxs represent the second most abundant class of cytochrome c oxidases after the aa3-type Cox, but have so far not been investigated in much detail. Recently, the first crystal structure of cbb3-Cox from P. stutzeri was obtained, providing a major breakthrough and inviting detailed studies on the catalytic mechanism and the assembly process. Studies on the assembly and maturation processes are of wide significance due to the fact that many human pathogens like Helicobacter pylori, Neisseria meningitides or Campylobacter jejuni use this type of Cox and it therefore might develop into an attractive drug-target. cbb3-Cox in R. capsulatus is encoded by the ccoNOQP gene operon which codes for four membrane proteins constituting cbb3-Cox. CcoP and CcoO are c-type cytochromes, containing periplasmic heme-binding motifs. CcoN is the central catalytic subunit which contains two b-type hemes and a copper ion. Investigating the delivery of Cu to the CcoN subunit and the assembly of all four subunits into the active cbb3-Cox complex were the main topics of this work. Here the role of the putative assembly factor CcoH, its structure and interaction with cbb3-Cox was investigated in detail. CcoH is a small membrane protein encoded in the ccoGHIS gene cluster located adjacent to the genes coding for cbb3-Cox. In vivo analysis of cbb3-Cox formation in a strain lacking ccoH showed the total absence of cbb3-Cox. Likewise, the stability of CcoH was drastically impaired in a ccoNOQP deletion strain. The mutual dependency of both proteins suggested their direct interaction, which was confirmed by site-directed photocrosslinking of CcoH to the CcoN subunit, by immunodetection of CcoH in cbb3-Cox complexes on Blue Native gels, by CcoH-cbb3-Cox co-purification and by in vitro labelling of cbb3-Cox complexes with radioactively labelled CcoH.[...]
Actas de conferencias sobre el tema "Complexes de type galactose oxydase":
Mimuro, Jun, Raymond R. Schleef y David J. Loskutoff. "THE EXTRACELLULAR MATRIX (ECM) OF CULTURED BOVINE AORTIC ENDOTHELIAL CELLS (BAEs) CONTAINS FUNCTIONALLY ACTIVE TYPE I PLASMINOGEN ACTIVATOR INHIBITOR (PAI-1)". En XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644438.