Artificial metalloenzymes for enantioselective catalysis based on the noncovalent incorporation of organometallic moieties in a host protein.
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.
Ward
Thomas R
TR
Institute of Chemistry, University of Neuchâtel, Av. Bellevaux 51, CP 2, 2007 Neuchâtel, Switzerland. thomas.ward@unine.ch
D001665:Binding Sites; D032701:Biomimetics; D002384:Catalysis; D004800:Enzymes, Immobilized / Q000138:chemical synthesis* / Q000737:chemistry; D008958:Models, Molecular; D015394:Molecular Structure; D046912:Multiprotein Complexes / Q000138:chemical synthesis* / Q000737:chemistry; D009942:Organometallic Compounds / Q000737:chemistry*; D010084:Oxidation-Reduction; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry*; D012238:Rhodium / Q000737:chemistry*; D013237:Stereoisomerism; D019809:Streptavidin / Q000737:chemistry*
D004800:Enzymes, Immobilized; D046912:Multiprotein Complexes; D009942:Organometallic Compounds; D011506:Proteins; D019809:Streptavidin; D012238:Rhodium