140-75-0Relevant articles and documents
Synthesis method of p-fluorobenzylamine
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Paragraph 0006; 0013; 0016-0018; 0021-0023; 0026-0027, (2021/06/13)
The invention discloses a synthesis method of p-fluorobenzylamine, wherein the synthesis method specifically comprises the following steps: smoothly and sequentially adding methanol, p-fluorobenzaldehyde, sodium carbonate and hydroxylamine hydrochloride into a reaction kettle, and continuously stirring until the materials are uniformly mixed; and after uniformly mixing, stirring for 2.0 hours at the temperature of 30 DEG C, fully reacting to obtain an intermediate I, and carrying out hydrogenation reduction on the intermediate I to obtain a finished product p-fluorobenzylamine. In conclusion, the total yield of the finished product p-fluorobenzylamine prepared by the method is not lower than 90%, and the purity is not lower than 99.5%; therefore, compared with the prior art, the method has the following beneficial effects that the process is simple, the raw materials are easy to obtain, the reaction yield is high, the product purity is high, generation of dimer and generation of defluorination impurity benzylamine are avoided, generation of three wastes, especially generation of waste gas ammonia gas, is greatly reduced, and the method is clean and environmentally friendly.
Zirconium-hydride-catalyzed site-selective hydroboration of amides for the synthesis of amines: Mechanism, scope, and application
Han, Bo,Jiao, Haijun,Wu, Lipeng,Zhang, Jiong
, p. 2059 - 2067 (2021/09/02)
Developing mild and efficient catalytic methods for the selective synthesis of amines is a longstanding research objective. In this respect, catalytic deoxygenative amide reduction has proven to be promising but challenging, as this approach necessitates selective C–O bond cleavage. Herein, we report the selective hydroboration of primary, secondary, and tertiary amides at room temperature catalyzed by an earth-abundant-metal catalyst, Zr-H, for accessing diverse amines. Various readily reducible functional groups, such as esters, alkynes, and alkenes, were well tolerated. Furthermore, the methodology was extended to the synthesis of bio- and drug-derived amines. Detailed mechanistic studies revealed a reaction pathway entailing aldehyde and amido complex formation via an unusual C–N bond cleavage-reformation process, followed by C–O bond cleavage.
Generation of Oxidoreductases with Dual Alcohol Dehydrogenase and Amine Dehydrogenase Activity
Tseliou, Vasilis,Schilder, Don,Masman, Marcelo F.,Knaus, Tanja,Mutti, Francesco G.
supporting information, p. 3315 - 3325 (2020/12/11)
The l-lysine-?-dehydrogenase (LysEDH) from Geobacillus stearothermophilus naturally catalyzes the oxidative deamination of the ?-amino group of l-lysine. We previously engineered this enzyme to create amine dehydrogenase (AmDH) variants that possess a new hydrophobic cavity in their active site such that aromatic ketones can bind and be converted into α-chiral amines with excellent enantioselectivity. We also recently observed that LysEDH was capable of reducing aromatic aldehydes into primary alcohols. Herein, we harnessed the promiscuous alcohol dehydrogenase (ADH) activity of LysEDH to create new variants that exhibited enhanced catalytic activity for the reduction of substituted benzaldehydes and arylaliphatic aldehydes to primary alcohols. Notably, these novel engineered dehydrogenases also catalyzed the reductive amination of a variety of aldehydes and ketones with excellent enantioselectivity, thus exhibiting a dual AmDH/ADH activity. We envisioned that the catalytic bi-functionality of these enzymes could be applied for the direct conversion of alcohols into amines. As a proof-of-principle, we performed an unprecedented one-pot “hydrogen-borrowing” cascade to convert benzyl alcohol to benzylamine using a single enzyme. Conducting the same biocatalytic cascade in the presence of cofactor recycling enzymes (i.e., NADH-oxidase and formate dehydrogenase) increased the reaction yields. In summary, this work provides the first examples of enzymes showing “alcohol aminase” activity.