1442-11-1Relevant articles and documents
Oxidation of organoselenium compounds. A study of chemoselectivity of phenylacetone monooxygenase
Andrade, Leandro H.,Pedrozo, Eliane C.,Leite, Henrique G.,Brondani, Patricia B.
, p. 63 - 66 (2011)
Organoselenium acetophenones oxidation using enzymatic reactions has been developed and chemoselectivity of phenylacetone monooxygenase (PAMO) with selenium-containing ketones has been explored. We discovered that this biocatalyst prefers selenium oxidation, which leads to selenoxide in excellent conversion, over Baeyer-Villiger oxidation.
ω-Transaminases as efficient biocatalysts to obtain novel chiral selenium-amine ligands for Pd-catalysis
Andrade, Leandro H.,Silva, Alexandre V.,Milani, Priscila,Koszelewski, Dominik,Kroutil, Wolfgang
experimental part, p. 2043 - 2051 (2010/07/03)
ω-Transaminases have been evaluated as biocatalysts in the reductive amination of organoselenium acetophenones to the corresponding amines, and in the kinetic resolution of racemic organoselenium amines. Kinetic resolution proved to be more efficient than the asymmetric reductive amination. By using these methodologies we were able to obtain both amine enantiomers in high enantiomeric excess (up to 99%). Derivatives of the obtained optically pure o-selenium 1-phenylethyl amine were evaluated as ligands in the palladium-catalyzed asymmetric alkylation, giving the alkylated product in up to 99% ee.
First chemoenzymatic synthesis of organoselenium amines and amides
Andrade, Leandro H.,Silva, Alexandre V.
, p. 1175 - 1181 (2008/09/21)
A series of organoselenium amines have been synthesized and submitted to the enzymatic kinetic resolution by acetylation mediated by CAL-B (Novozym 435) to give the corresponding chiral amides in an enantiomerically pure form. After evaluating the appropriate lipase, solvent, temperature, and lipase/substrate ratio in the kinetic resolution, the chiral organoselenium amides were obtained with enantiomeric excess of up to 99%.
