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Artificial Metalloenzymes for Enantioselective Catalysis Based on the Noncovalent Incorporation of Organometallic Moieties in a Host Protein by Thomas R. Ward is a Chemistry article available to read on EtoBox.
What is Artificial Metalloenzymes for Enantioselective Catalysis Based on the Noncovalent Incorporation of Organometallic Moieties in a Host Protein about?
## Abstract Enzymatic and homogeneous catalysis offer complementary means to produce enantiopure products. Incorporation of achiral, biotinylated aminodiphosphine–rhodium complexes in (strept)avidin affords enantioselective hydrogenation catalysts. A combined chemogenetic procedure allows the optimization of the activity and the selectivity of such artificial metalloenzymes: the reduction of acetamidoacrylate proceeds to produce __N__‐acetamidoalanine in either 96 % __ee__ (__R__) or 80 % __ee__ (__S__). In addition to providing a chiral second coordination sphere and, thus, selectivity to the catalyst, the phenomenon of protein‐accelerated catalysis (e.g., increased activity) was unraveled. Such artificial metalloenzymes based on the biotin–avidin technology display features that are reminiscent of both homogeneous and of enzymatic catalysis.
Who reads Artificial Metalloenzymes for Enantioselective Catalysis Based on the Noncovalent Incorporation of Organometallic Moieties in a Host Protein?
It is typically read by researchers, students, and practitioners in Chemistry.
- Author
- Thomas R. Ward
- Publisher
- John Wiley and Sons; Wiley (John Wiley & Sons); John Wiley & Sons Ltd.; Wiley (ISSN 0947-6539)
- Published
- 2005
- Language
- EN
- Field
- Chemistry (Physical Sciences)