Designed evolution of artificial metalloenzymes: protein catalysts made to order.
Artificial metalloenzymes based on biotin-streptavidin technology, a "fusion" of chemistry and biology, illustrate how asymmetric catalysts can be improved and evolved using chemogenetic approaches.
Creus
Marc
M
Department of Cellular and Molecular Biology, University of Neuchâtel, Rue Emile-Argand 11, C.P. 158, Neuchâtel, CH-2009, Switzerland. marc.creus@unine.ch
Ward
Thomas R
TR
D001665:Binding Sites; D032701:Biomimetics; D001710:Biotin / Q000737:chemistry* / Q000235:genetics; D002384:Catalysis; D006864:Hydrogenase / Q000138:chemical synthesis / Q000737:chemistry / Q000235:genetics; D008024:Ligands; D008958:Models, Molecular; D016296:Mutagenesis; D009942:Organometallic Compounds / Q000138:chemical synthesis / Q000737:chemistry; D015202:Protein Engineering; D011993:Recombinant Fusion Proteins / Q000737:chemistry* / Q000235:genetics; D012238:Rhodium / Q000737:chemistry*; D013237:Stereoisomerism; D019809:Streptavidin / Q000737:chemistry* / Q000235:genetics
D008024:Ligands; D009942:Organometallic Compounds; D011993:Recombinant Fusion Proteins; D001710:Biotin; D019809:Streptavidin; D012238:Rhodium; D006864:Hydrogenase