Artificial transfer hydrogenases for the enantioselective reduction of cyclic imines

Autor:	Malcolm Jeremy Zimbron, Tilman Schirmer, Tillmann Heinisch, Livia Knörr, Julien Pierron, Yvonne M. Wilson, Elisa S. Nogueira, Thibaud Rossel, Annette Mutschler, Karoline Kersten, Thomas R. Ward, Marc Dürrenberger
Rok vydání:	2010
Předmět:	Streptavidin Models Molecular Stereochemistry Imine chemistry.chemical_element Reductase 010402 general chemistry Transfer hydrogenation Crystallography X-Ray 01 natural sciences Catalysis chemistry.chemical_compound Hydrogenase Iridium Saturated mutagenesis Molecular Structure 010405 organic chemistry Enantioselective synthesis Stereoisomerism General Medicine General Chemistry 0104 chemical sciences 3. Good health chemistry Cyclization Biotinylation Imines Oxidation-Reduction
Zdroj:	Angewandte Chemie (International ed. in English). 50(13)
ISSN:	1521-3773
Popis:	Man-made activity: Introduction of a biotinylated iridium piano stool complex within streptavidin affords an artificial imine reductase (see scheme). Saturation mutagenesis allowed optimization of the activity and the enantioselectivity of this metalloenzyme, and its X-ray structure suggests that a nearby lysine residue acts as a proton source during the transfer hydrogenation.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1abbde3601357d9fcabb50bc50fec6ac https://pubmed.ncbi.nlm.nih.gov/21404391 Zobrazit plný text záznamu Plný text