Literatura científica selecionada sobre o tema "[Cp*Ir(bpy-OMe)H]+"
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Artigos de revistas sobre o assunto "[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.º 46 (2014): 17366–74. http://dx.doi.org/10.1039/c4dt02744b.
Texto completo da fonteAbramov, 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.º 24 (2016): 20240–46. http://dx.doi.org/10.1039/c5ra23918d.
Texto completo da fonteDeguire, Suzanne, e François Brisse. "The effect of substitution on the conformation in para-substituted ethylene glycol dibenzoate molecules". Canadian Journal of Chemistry 66, n.º 10 (1 de outubro de 1988): 2545–52. http://dx.doi.org/10.1139/v88-399.
Texto completo da fonteRöllig, 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.
Texto completo da fonteTeses / dissertações sobre o assunto "[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.
Texto completo da fonteThe 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