An Artificial Metalloenzyme: Creation of a Designed Copper Binding Site in a Thermostable Protein
Guided by nature: A designed binding site comprising the His/His/Asp motif for CuII complexation has been constructed in a robust protein by site‐specific mutagenesis (see picture). The artificial metalloenzyme catalyzes an enantioselective Diels–Alder reaction.
Artificial Copper Enzymes for Asymmetric Diels–AlderReactions
Artificial Diels–Alderase based on the Transmembrane Protein FhuA
Artificial Metalloenzymes with the Neocarzinostatin Scaffold: Toward a Biocatalyst for the Diels–Alder Reaction
Bimetallic Copper-Heme-Protein-DNA Hybrid Catalyst for Diels Alder Reaction
Construction of a Hybrid Biocatalyst Containing a Covalently-Linked Terpyridine Metal Complex within a Cavity of Aponitrobindin
Copper–Phthalocyanine Conjugates of Serum Albumins as Enantioselective Catalysts in Diels–Alder Reactions
Enantioselective Artificial Metalloenzymes by Creation of a Novel Active Site at the Protein Dimer Interface
(η6-Arene) Ruthenium(II) Complexes and Metallo-Papain Hybrid as Lewis Acid Catalysts of Diels–Alder Reaction in Water
Covalent embedding of a (η6-arene) ruthenium(II) complex into the protein papain gives rise to a metalloenzyme displaying a catalytic efficiency for a Lewis acid-mediated catalysed Diels–Alder reaction enhanced by two orders of magnitude in water.