Letteratura scientifica selezionata sul tema "[Cp*Ir(bpy-OMe)H]+"
Cita una fonte nei formati APA, MLA, Chicago, Harvard e in molti altri stili
Consulta la lista di attuali articoli, libri, tesi, atti di convegni e altre fonti scientifiche attinenti al tema "[Cp*Ir(bpy-OMe)H]+".
Accanto a ogni fonte nell'elenco di riferimenti c'è un pulsante "Aggiungi alla bibliografia". Premilo e genereremo automaticamente la citazione bibliografica dell'opera scelta nello stile citazionale di cui hai bisogno: APA, MLA, Harvard, Chicago, Vancouver ecc.
Puoi anche scaricare il testo completo della pubblicazione scientifica nel formato .pdf e leggere online l'abstract (il sommario) dell'opera se è presente nei metadati.
Articoli di riviste sul tema "[Cp*Ir(bpy-OMe)H]+":
Talavera, M., J. Bravo, J. Castro, S. García-Fontán, J. M. Hermida-Ramón e S. Bolaño. "Electronic effects of substituents on the stability of the iridanaphthalene compound [IrCp*{C(OMe)CHC(o-C6H4)(Ph)}(PMe3)]PF6". Dalton Trans. 43, n. 46 (2014): 17366–74. http://dx.doi.org/10.1039/c4dt02744b.
Abramov, P. A., C. Vicent, N. B. Kompankov, J. A. Laricheva e M. N. Sokolov. "Unique solubility of polyoxoniobate salts in methanol: coordination to cations and POM methylation". RSC Advances 6, n. 24 (2016): 20240–46. http://dx.doi.org/10.1039/c5ra23918d.
Deguire, Suzanne, e François Brisse. "The effect of substitution on the conformation in para-substituted ethylene glycol dibenzoate molecules". Canadian Journal of Chemistry 66, n. 10 (1 ottobre 1988): 2545–52. http://dx.doi.org/10.1139/v88-399.
Röllig, Robert, Caroline Emilie Paul, Pierre Rousselot-Pailley, Selin Kara e Véronique Alphand. "Hybrid catalysis for enantioselective Baeyer-Villiger oxidation and epoxidation: A Cp*Ir complex to fuel FMN and FAD reduction for flavoprotein monooxygenase modules." Reaction Chemistry & Engineering, 2023. http://dx.doi.org/10.1039/d3re00411b.
Tesi sul tema "[Cp*Ir(bpy-OMe)H]+":
Röllig, Robert. "Chemical hydride transfer for flavin dependent monooxygenases of two-component systems". Electronic Thesis or Diss., Aix-Marseille, 2021. http://www.theses.fr/2021AIXM0436.
The term flavoprotein monooxygenases (FPMO) covers two different types of flavoenzymes: single and two component oxygenases. Two component FPMOs consist of a reductase and an oxygenating enzyme. The functional independence of the oxygenase part of 2,5-diketocamphane 1,2-monooxygenase I (2,5 DKCMO), an FMN dependent type II Baeyer-Villiger monooxygenase, from the reductase counterpart, as well as the mechanism of flavin transfer by free diffusion, was investigated in a reductase-free reaction, using synthetic nicotinamide biomimetics (NCBs) for the reduction of FMN. The balance of flavin reduction and enzymatic (re)oxidation was identified as the bottleneck of the system. Aiming for potentially cost efficient hydride donors for enzymatic redox reactions, nicotinamide coenzyme and nicotinamide biomimetic independent flavin reduction strategies were investigated. The capability of the pH and oxygen robust iridium III complex [Cp*Ir(bpy-OMe)H]+ (Ir* (H+)) to transfer hydrides for flavin reduction for the enzymatic reaction of respectively FMNH2 and FADH2 dependent monooxygenases, 2,5 DKCMO and styrene monooxygenase from Sphingopyxis fribergensis Kp.5.2 (SfStyA) was exploited. The Ir* (H+)/SfStyA approach outperformed the state of the art system by six-fold in terms of turn over number of the metal catalyst. Nevertheless, the robustness of the system remains challenging, and improvements are required to establish the approach as an efficient and versatile platform technology for flavoenzymes