Journal
JOURNAL OF ORGANOMETALLIC CHEMISTRY
Volume 689, Issue 25, Pages 4868-4871Publisher
ELSEVIER SCIENCE SA
DOI: 10.1016/j.jorganchem.2004.09.032
Keywords
biotin-avidin; streptavidin; enantioselective catalysis; second coordination sphere; hydrogenation; artificial metalloenzyme; bioinorganic chemistry; protein-accelerated catalysis
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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. (C) 2004 Elsevier B.V. All rights reserved.
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