124779-08-4Relevant academic research and scientific papers
Asymmetric synthesis of 2-alkyl-3-phosphonopropanoic acid derivatives via Rh-catalyzed asymmetric hydrogenation
Luo, Li-Bin,Wang, Dao-Yong,Zhou, Xiao-Mao,Zheng, Zhuo,Hu, Xiang-Ping
, p. 2117 - 2123 (2012/03/27)
The commercially available ferrocene-based diphosphine ligand (S c,SFc)-TaniaPhos was found to be highly effective in the Rh-catalyzed asymmetric hydrogenation of 3-aryl-2-(phosphonomethyl)propenates. Excellent enantioselectivity (90
Enantioselective Rh-catalyzed hydrogenation of 3-aryl- 2phosphonomethylpropenoates by a new class of chiral ferrocenyl diphosphine ligands
Wang, Dao-Yong,Hu, Xiang-Ping,Hou, Chuan-Jin,Deng, Jun,Yu, Sai-Bo,Duan, Zheng-Chao,Huang, Jia-Di,Zheng, Zhuo
supporting information; experimental part, p. 3226 - 3229 (2009/12/09)
A new class of chiral ferrocenyl diphosphine ligands with an imidazole ring, (Rc,SFc,)-ImiFerroPhos, has been prepared from acylferrocenes through a five-step transformation and successfully applied in the Rh-catalyzed asymmetric hyd
Potential Inhibitors of Phosphoenolpyruvate Carboxylase. II. Phosphonic Acid Substrate Analogues Derived from Reactions of Trialkyl Phosphites with Halomethacrylates
McFadden, Helen G.,Harris, Roger L. N.,Jenkins, Colin L. D.
, p. 301 - 314 (2007/10/02)
Analogues of phosphoenolpyruvate (PEP), the substrate of PEP carboxylase, were synthesized as potential inhibitors of the enzyme.Esterified analogue precursors were obtained by nucleophilic substitution of various halomethacrylate derivatives with trialkyl phosphites.Substitution of the halomethacrylates can occur either α to the leaving halogen or in the γ position with subsequent allylic shift of the double bond.The course of the reaction was influenced both by reaction conditions and the nature of the substituents on the reactants.The phosphonomethacrylates obtained were hydrolysed to PEP analogues that were found to be moderate to good inhibitors of PEP carboxylase.Phosphonomethacrylic acid derivatives bearing two halogen substituents in the γ position were found to be the most potent inhibitors of this enzyme.
