3886-69-9Relevant articles and documents
Synthesis and reactivity towards carbon monoxide of an optically active endo five-membered ortho-cyclopalladated imine: X-ray molecular structure of trans-(μ-Cl)2[Pd(κ2-C,N-(R)-C6H4-CH{double bond, long}N-CHMe-Ph)]2
Albert, Joan,D'Andrea, Luci?a,Granell, Jaume,Tavera, Raquel,Font-Bardia, Mercè,Solans, Xavier
, p. 3070 - 3080 (2007)
(R)-1-Phenylethyl-benzylidene-amine (1) reacted with Pd(OAc)2 in acetic acid at 60 °C under nitrogen affording the acetato-bridged dinuclear endo five-membered ortho-cyclopalladated compound (μ-OAc)2[Pd(κ2-C,N-(R)-C6H4-CH{double bond, long}N-CHMe-Ph)]2 (2) in 65% yield. Compound 2 was converted by a metathesis reaction with LiCl into the corresponding chloro-bridged dinuclear cyclopalladated compound (μ-Cl)2[Pd(κ2-C,N-(R)-C6H4-CH{double bond, long}N-CHMe-Ph)]2 (3). 1H NMR of CDCl3 solutions of compounds 2 and 3 treated separately with py-d5, (R)-1-phenylethylamine and racemic 1-phenylethylamine were consistent with the endo cyclopalladated structure and the R absolute configuration of the chiral carbon atoms of compounds 2 and 3. Compounds 2 and 3 reacted with carbon monoxide in methanol affording, as major compounds, methyl 2-formylbenzoate (91% chemical yield) and the epimers of 3-methoxy-2-[(R)-1-phenylethyl]isoindolin-1-one (64% chemical yield) in ca. 20% diastereomeric excess, respectively. The trans isomer of compound 3 crystallized in the P21 monoclinic space group with a = 10.430(4) A?, b = 12.082(8) A?, c = 11.168(4) A? and β = 95.20(3)° and presented C-H?Cl intramolecular and C-H?Pd intermolecular non-conventional hydrogen bonds.
Determination of absolute configurations of amines and amino acids using nonchiral derivatizing agents (NCDA) and deuterium NMR.
Chalard,Bertrand,Canet,Thery,Remuson,Jeminet
, p. 2431 - 2434 (2000)
Enantiomeric analysis and empirical determination of the absolute configuration of amines and amino acids can be easily performed using acetyl-d(3) chloride as a nonchiral derivatizing agent (deuterium probe) and deuterium NMR in a chiral solvent (Courtieu's method). In the case of amino acids, derivatization to amido esters, performed with methanol-d(4) and acetyl-d(3) chloride, gives a double opportunity for enantiomeric analysis.
Artificial plant cell walls as multi-catalyst systems for enzymatic cooperative asymmetric catalysis in non-aqueous media
B?ckvall, Jan-E.,Córdova, Armando,Deiana, Luca,Naidu, Veluru Ramesh,Rafi, Abdolrahim A.,Tai, Cheuk-Wai
supporting information, p. 8814 - 8817 (2021/09/07)
The assembly of cellulose-based artificial plant cell wall (APCW) structures that contain different types of catalysts is a powerful strategy for the development of cascade reactions. Here we disclose an APCW catalytic system containing a lipase enzyme and nanopalladium particles that transform a racemic amine into the corresponding enantiomerically pure amide in high yieldviaa dynamic kinetic resolution.
Biochemical and Structural Characterization of an (R)-Selective Transaminase in the Asymmetric Synthesis of Chiral Hydroxy Amines
Li, Fulong,Liang, Youxiang,Wei, Yuwen,Zheng, Yukun,Du, Yan,Yu, Huimin
supporting information, p. 4582 - 4589 (2021/08/07)
An (R)-selective transaminase RbTA with excellent stereoselectivity (>99% ee) in the asymmetric amination of hydroxy ketones was identified. Biochemical characterization showed that RbTA exhibited the highest activity toward 4-hydroxy-2-butanone among reported enzymes, and that it has broad substrate specificity, including for aliphatic, aromatic, and alicyclic ketones. Crystallization of RbTA were performed, as were molecular docking and mutagenesis studies. Residue Tyr125 plays a key role in substrate recognition by forming a hydrogen bond with hydroxy ketone. The applicability of the enzyme was determined in preparative-scale synthesis of (R)-3-amino-1-butanol, demonstrating the potential of RbTA as a green biocatalyst for production of value-added chiral hydroxy amines. This study provides an efficient tool for enzymatic synthesis of chiral hydroxy amines, as well as structural insight into substrate recognition by transaminases in the asymmetric amination of hydroxy ketones. (Figure presented.).