26629-33-4Relevant articles and documents
Lipase active site covalent anchoring of Rh(NHC) catalysts: Towards chemoselective artificial metalloenzymes
Basauri-Molina,Riemersma,Würdemann,Kleijn,Klein Gebbink
supporting information, p. 6792 - 6795 (2015/04/22)
A Rh(NHC) phosphonate complex reacts with the lipases cutinase and Candida antarctica lipase B resulting in the first (soluble) artificial metalloenzymes formed by covalent active site-directed hybridization. When compared to unsupported complexes, these
Stereochemistry at carbon upon protonolysis of a late transition metal-alkyl bond: A reaction of relevance to catalytic enantioselective hydrogenation of olefins
Wiles,Bergens,Young V.G.
, p. 1019 - 1025 (2007/10/03)
Reaction of [Ru((R)-BINAP)(H)(MeCN)n (acetone)3-n](BF4) (where n = 0-3) (2) with 1 equiv of the olefin substrate methyl α-acetamidoacrylate (MAA) in acetone at room temperature immediately generated a mixture (72:28) of two diastereomers of the complex [Ru((R)-BINAP)(MeCN)(MAA(H))](BF4)(3). The olefin-hydride insertion reaction between 2 and MAA to generate 3 was regioselective, with transfer of the hydride to the β-olefinic carbon and transfer of ruthenium to the α-carbon in both diastereomers of 3. The two diastereomers of 3 differ by the absolute configuration at the α-carbon of MAA(H) ((Scα)-3 and (Rcα)-3). The absolute configuration of the major ((Scα)-3) diastereomer was determined by X-ray diffraction in conjunction with NMR spectroscopic data. Protonolysis of the ruthenium-carbon bond in 3 and in the methyl α-acetamidocinnamate (MAC) analog ([Ru((R)-BINAP)(MeCN)((S)-MAC(H))](BF4)((Scα)-4)) by addition of 2 equiv HBF4·Et2O in CH2 Cl2 at room temperature was not stereospecific and did not occur with β-hydride elimination from the methyl or benzyl groups.
