10202-87-6

Upstream product

• 99-03-6 1-(3-aminophenyl)ethanone 
• 7463-31-2 3-Acetamidoacetophenone 
• 92642-18-7 N-(3-acetyl-2-nitrophenyl)acetamide 

Downstream Products

• 92642-20-1 2-nitro-3-(trifluoroacetamido)acetophenone 
• 1438559-38-6 phenyl(quinoxalin-5-yl)methanone 
• 89334-34-9 1-(quinoxalin-5-yl)ethanone 
• 1125484-40-3 1-{2-[4-(4-isopropyl-phenyl)-6-prop-2-ynyloxy-quinazolin-2-yl]-3H-benzoimidazol-4-yl}-ethanone 
• 159724-51-3 1-(1H-benzoimidazol-4-yl)-ethanone 
• 159724-48-8 3-Acetyl-1,2-phenylendiamine hydrochloride 
• 92642-21-2 3-(methylamino)-2-nitroacetophenone 
• 1455-88-5 <3-Azido-2-nitro-phenyl>-aethanon 
• 159724-49-9 monoacetylphenylenediamine 
• 56759-31-0 1-(3-bromo-2-nitrophenyl)ethanone 
• 7137-38-4 1-(3-chloro-2-nitrophenyl)ethan-1-one 

Relevant academic research and scientific papers

Site-specific labelling of caged ATP with deuterium or 18oxygen

[3-D]2-Nitroacetophenone and [alcohol-18O]-1-(2-nitrophenyl)ethyl alcohol were prepared and used to synthesise labelled P3-1-(2-nitrophenyl)ethyl esters of ATP ('caged ATP') with isotope present either as deuterium on the 3-position of the nitrosubstituted ring or as 18oxygen in the bridging position between the terminal phosphate and the nitrophenylethyl group. The availability of the deuterated compounds enabled complete assignment of their 1H NMR spectra.

Direct exchange of a ketone methyl or aryl group to another aryl group through ciC bond activation assisted by rhodium chelation

Swapped: Commercially available quinolinone derivatives (1 or 2, see scheme) were reacted with arylboronic acids in the presence of a RhI complex to give aryl(quinolin-8-yl)methanone products 3 in medium to good yields. A mechanism that involves the in situ oxidation of RhI to RhIII by O2 in the presence of CuI was proposed. Copyright

Semisynthetic Enzymes: Characterization of Isomeric Flavopapains with Widely Different Catalytic Efficiencies

Flavopapain 6 has been prepared by alkylation of the active site cysteine-25 of papain with 8α-(bromoacetyl)-10-methylisoalloxazine.This semisynthetic enzyme was shown to serve as a catalyst for the oxidation of dihydronicotinamides, exhibiting saturation kinetics and up to 600-fold rate accelerations relative to a model flavin.This is contrasted to the behavior of flavopapain 9, the product of the modification of papain with 6α-(bromoacetyl)-10-methylisoalloxazine.In this case no catalytic rate enhancement compared to the behavior of a model compound is observed.Since the two isoalloxazines are isomeric, the differences in the activities of the semisynthetic enzymes are interpreted in terms of differences in the geometry of the flavin at the active site.It is also noted that flavopapain 6 can exhibit some chiral discrimination toward optically active dihydronicotinamides.