20570-67-6Relevant academic research and scientific papers
Asymmetric synthesis of highly substituted β-nitro alcohols and enantiomerically enriched 4,4,5-trisubstituted oxazolidinones
Crich, David,Ranganathan, Krishnakumar,Rumthao, Sochanchingwung,Shirai, Michio
, p. 2034 - 2037 (2007/10/03)
It is demonstrated that α,α-disubstituted-α-nitroketones are reduced to the corresponding trisubstituted nitro alcohols in good to excellent yield and enantiomeric excess by borane-dimethyl sulfide in the presence of a chiral oxazaborolidine catalyst. Red
Reactions of nitrogen dioxide with hexenes. The mechanistic and structural factors controlling the product composition
Golding, Peter,Powell, Joy L.,Ridd, John H.
, p. 813 - 820 (2007/10/03)
The reaction of nitrogen dioxide with a number of hexenes has been investigated using several solvents and the major products have been identified.The heterolytic reaction path has been effectively eliminated by the use of hexane as solvent.The mechanism of the heterolytic reaction path is discussed with the aid of ab initio molecular orbital calculations on possible nitrosating agents with particular reference to the syn and anti forms of nitrosyl nitrate.A new mechanism is proposed for the formation of certain trisubstituted derivatives.
Specific Inhibitors in Vitamin Biosynthesis. Part 7. Syntheses of Blocked 7,8-Dihydropteridines via &α-Amino Ketones
Al-Hassan, Saiba S.,Cameron, Robert J.,Curran, Adrian W. C.,Lyall, William J. S.,Nicholson, Sydney H.,et al.
, p. 1645 - 1660 (2007/10/02)
The synthesis of 15 blocked 7,8-dihydropteridines is described in which the pyrazine ring is built from a derivative of an α-amino ketone.Three routes to the amino ketones based upon amino acids, nitrosyl chloride addition to alkenes, and nitro alcohols are discussed.The compounds synthesised are inhibitors of 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase , an enzyme in the pathway leading to dihydrofolate, and the inhibitory potencies of the compounds are discussed in the light of a hypothetical active site model for the enzyme.
