A Metal Ion Regulated Artificial Metalloenzyme
Regulation of enzyme activity is essential in living cells. The rapidly increasing number of designer enzymes with new-to-nature activities makes it necessary to develop novel strategies for controlling their catalytic activity. Here we present the development of a metal ion regulated artificial metalloenzyme created by combining two anchoring strategies, covalent and supramolecular, for introducing a regulatory and a catalytic site, respectively. This artificial metalloenzyme is activated in the presence of Fe2+ ions, but only marginally in the presence of Zn2+.
Artificial Metalloenzymes Derived from Bovine β-Lactoglobulin for the Asymmetric Transfer Hydrogenation of an Aryl Ketone – Synthesis, Characterization and Catalytic Activity
Bovine Serum Albumin-Cobalt(II) Schiff Base Complex Hybrid: An Efficient Artificial Metalloenzyme for Enantioselective Sulfoxidation using Hydrogen Peroxide
Chalcogenide Substitution in the [2Fe] Cluster of [FeFe]-Hydrogenases Conserves High Enzymatic Activity
Ferritin Encapsulation of Artificial Metalloenzymes: Engineering a Tertiary Coordination Sphere for an Artificial Transfer Hydrogenase
Neocarzinostatin-Based Hybrid Biocatalysts for Oxidation Reactions
Oxidation Catalysis via Visible-Light Water Activation of a [Ru(bpy)3]2+ Chromophore BSA–Metallocorrole Couple
Semi-Synthesis of an Artificial Scandium(III) Enzyme with a β-Helical Bio-Nanotube
Supramolecular Interactions Between Functional Metal Complexes and ProteinsReview
Synthesis of Hybrid Transition-Metalloproteins via Thiol-Selective Covalent Anchoring of Rh-Phosphine and Ru-Phenanthroline Complexes
(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.