Artificial metalloenzymes for enantioselective catalysis : the phenomenon of protein accelerated catalysis
JournalArticle (Originalarbeit in einer wissenschaftlichen Zeitschrift)
 
ID 116723
Author(s) Collot, Jerome; Humbert, Nicolas; Skander, Myriem; Klein, Gerard; Ward, Thomas R.
Author(s) at UniBasel Ward, Thomas R.
Year 2004
Title Artificial metalloenzymes for enantioselective catalysis : the phenomenon of protein accelerated catalysis
Journal Journal of Organometallic Chemistry
Volume 689
Number 25
Pages / Article-Number 4868-4871
Keywords Coenzymes Role: CAT (Catalyst use), CPS (Chemical process), PEP (Physical, engineering or chemical process), PROC (Process), USES (Uses) (artificial rhodium; phenomenon of protein accelerated catalysis of enantioselective hydrogenation by artificial rhodium coenzymes); Enzymes Role: CAT (Catalyst use), CPS (Chemical process), PEP (Physical, engineering or chemical process), PROC (Process), USES (Uses) (metallo-; phenomenon of protein accelerated catalysis of enantioselective hydrogenation by art
Abstract We report on the phenomenon of protein-accelerated catalysis in the field of artificial metalloenzymes based on the non-covalent incorporation of biotinylated rhodium–diphosphine complexes in (strept)avidin as host proteins. By incrementally varying the [Rh(COD)(Biot-1)]+ vs. (strept)avidin ratio, we show that the enantiomeric excess of the produced acetamidoalanine decreases slowly. This suggests that the catalyst inside (strept)avidin is more active than the catalyst outside the host protein. Both avidin and streptavidin display protein-accelerated catalysis as the protein embedded catalyst display 12.0- and 3.0-fold acceleration over the background reaction with a catalyst devoid of protein. Thus, these artificial metalloenzymes display an increase both in activity and in selectivity for the reduction of acetamidoacrylic acid.
Publisher Elsevier
ISSN/ISBN 0022-328X
edoc-URL http://edoc.unibas.ch/dok/A5254439
Full Text on edoc No
Digital Object Identifier DOI 10.1016/j.jorganchem.2004.09.032
 
   

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