32231-50-8Relevant articles and documents
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Poethke
, p. 357,367, 571, 586 (1937)
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Asymmetric hydrogenation of an α-unsaturated carboxylic acid catalyzed by intact chiral transition metal carbonyl clusters-diastereomeric control of enantioselectivity
Abdel-Magied, Ahmed F.,Doverbratt, Isa,Haukka, Matti,Nordlander, Ebbe,Raha, Arun K.,Rahaman, Ahibur,Richmond, Michael G.,Singh, Amrendra K.,Theibich, Yusuf
, p. 4244 - 4256 (2020/04/17)
Twenty clusters of the general formula [(μ-H)2Ru3(μ3-S)(CO)7(μ-P-P?)] (P-P? = chiral diphosphine of the ferrocene-based Walphos or Josiphos families) have been synthesised and characterised. The clusters have be
Effect of particle restructuring during reduction processes over polydopamine-supported Pd nanoparticles
Gazdag, Tamás,Baróthi, ádám,Juhász, Koppány Levente,Kunfi, Attila,Németh, Péter,Sápi, András,Kukovecz, ákos,Kónya, Zoltán,Szori, Kornél,London, Gábor
, p. 484 - 491 (2018/12/13)
The effect of catalyst restructuring on the polydopamine-supported Pd catalyzed transfer hydrogenation of ethyl 4-nitrobenzoate and the catalytic hydrogenation of (E)-2-methyl-2-butenoic acid is reported. Transmission electron microscopy investigation of different catalyst pre-treatment and reaction conditions revealed high catalytic activity in both reactions unless drastic aggregation of the active metal occurred. In the transfer hydrogenation reaction aggregation was primarily dependent on the H-source used, while in the catalytic hydrogenation additives in combination with the reductive environment led to extensive Pd aggregation and thus decreased catalytic activity. The enantioselective hydrogenation of (E)-2-methyl-2-butenoic acid showed increased enantioselectivity and decreased conversion with increased particle size.
Chemoenzymatic Cascade Synthesis of Optically Pure Alkanoic Acids by Using Engineered Arylmalonate Decarboxylase Variants
Enoki, Junichi,Mügge, Carolin,Tischler, Dirk,Miyamoto, Kenji,Kourist, Robert
, p. 5071 - 5076 (2019/03/17)
Arylmalonate decarboxylase (AMDase) catalyzes the cofactor-free asymmetric decarboxylation of prochiral arylmalonic acids and produces the corresponding monoacids with rigorous R selectivity. Alteration of catalytic cysteine residues and of the hydrophobic environment in the active site by protein engineering has previously resulted in the generation of variants with opposite enantioselectivity and improved catalytic performance. The substrate spectrum of AMDase allows it to catalyze the asymmetric decarboxylation of small methylvinylmalonic acid derivatives, implying the possibility to produce short-chain 2-methylalkanoic acids with high optical purity after reduction of the nonactivated C=C double bond. Use of diimide as the reductant proved to be a simple strategy to avoid racemization of the stereocenter during reduction. The developed chemoenzymatic sequential cascade with use of R- and S-selective AMDase variants produced optically pure short-chain 2-methylalkanoic acids in moderate to full conversion and gave both enantiomers in excellent enantiopurity (up to 83 % isolated yield and 98 % ee).