92998-95-3

Upstream product

• 705-60-2 (2-nitroprop-1-enyl)benzene 
• 100-52-7 benzaldehyde 
• 705-60-2 1-phenyl-2-nitroprop-1-ene 

Downstream Products

• 51-64-9 dexamfetamine 
• 156-34-3 l-amphetamine 

Relevant academic research and scientific papers

Enantioselective hydrogenation of α,β-disubstituted nitroalkenes

The first highly chemo- and enantioselective hydrogenation of α,β-disubstituted nitroalkenes was accomplished with rhodium/JosiPhos-J2 as a catalyst, with the yield and enantioselectivity of up to 95% and 94%, respectively. The α-chiral nitroalkanes will provide an entry to valuable chiral amphetamines which are otherwise not so easily accessed. This journal is the Partner Organisations 2014.

Highly enantioselective reduction of β,β-disubstituted aromatic nitroalkenes catalyzed by Clostridium sporogenes

(Chemical Equation Presented) This is the first report of the use of Clostridium sporogenes extracts for enantioselective reduction of C=C double bonds of β,β-disubstituted (1) and α,β-disubstituted nitroalkenes (3). Crude enzyme preparations reduced aryl derivatives 1a-e and 1h, in 35-86% yield with ≥97% ee. Reduction of (E)- and (Z)-isomers of 1c gave the same enantiomer of 2c (≥99% ee). In contrast, α,β- disubstituted nitroalkene 3a was a poor substrate, yielding (S)-4a in low yield (10-20%), and the ee (30-70% ee) depended on NADH concentration. An efficient synthesis of a library of nitroalkenes 1 is described.

Structure-based insight into the asymmetric bioreduction of the C=C double bond of α,β-unsaturated nitroalkenes by pentaerythritol tetranitrate reductase

Biocatalytic reduction of α- or β-alkyl-barylnitroalkenes provides a convenient and efficient method to prepare chiral substituted nitroalkanes. Pentaerythritol tetranitrate reductase (PETN reductase) from Enterobacter cloacae st. PB2 catalyses the reduction of nitroolefins such as 1-nitrocyclohexene (1) with steady state and rapid reaction kinetics comparable to other old yellow enzyme homologues. Furthermore, it reduces 2-aryl-1-nitropropenes (4a-d) to their equivalent (S)-nitropropanes 9a-d. The enzyme shows a preference for the (Z)-isomer of substrates 4a-d, providing almost pure enantiomeric products 9a-d (ees up to > 99%) in quantitative yield, whereas the respective (E)-isomers are reduced with lower enantioselectivity (63-89% ee) and lower product yields. 1-Aryl-2-nitropropenes (5a, b) are also reduced efficiently, but the products (R)-10 have lower optical purities. The structure of the enzyme complex with 1-nitrocyclohexene (1) was determined by X-ray crystallography, revealing two substrate-binding modes, with only one compatible with hydride transfer. Models of nitropropenes 4 and 5 in the active site of PETN reductase predicted that the enantioselectivity of the reaction was dependent on the orientation of binding of the (E)- and (Z)- substrates. This work provides a structural basis for understanding the mechanism of asymmetric bioreduction of nitroalkenes by PETN reductase.

Microbial Hydrogenation of Nitroolefins

Micriorganisms which hydrogenate 2-nitro-1-phenyl-1-propene were screend in type cultures and soil samples.Some actinomycetes belonging to Rhodococcus, Nocardia and Mycobacterium asymmetrically reduced the substrate and gave optically active 2-nitro-1-phenylpropane.Among them, Rhodococcus rhodochrous IFO 3338 gave the best results.The satureted compound was obtained quantitatively, when cultivation was carried out for 3 days at 30 oC with a substrate concentration of 0.4percent.The optical purity of the product was seriously affected by the pH of the medium.The more acidic the medium, the higher the enantiomeric excess.The results suggested that non-enzymatic racemization of the product take place even under neutral conditions.Other substrates, such as 2-nitro-1-propene were also converted to optically active 2-nitro-1-substituted propane.