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47 publications
Sort by Titlearrow_drop_down Datearrow_drop_down Journalarrow_drop_downA Dual Anchoring Strategy for the Localization and Activation of Artificial Metalloenzymes Based on the Biotin−Streptavidin Technology
Artificial metalloenzymes result from anchoring an active catalyst within a protein environment. Toward this goal, various localization strategies have been pursued: covalent, supramolecular, or dative anchoring. Herein we show that introduction of a suitably positioned histidine residue contributes to firmly anchor, via a dative bond, a biotinylated rhodium piano stool complex within streptavidin. The in silico design of the artificial metalloenzyme was confirmed by X-ray crystallography. The resulting artificial metalloenzyme displays significantly improved catalytic performance, both in terms of activity and selectivity in the transfer hydrogenation of imines. Depending on the position of the histidine residue, both enantiomers of the salsolidine product can be obtained.
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A General Method for Artificial Metalloenzyme Formationthrough Strain-Promoted Azide–Alkyne Cycloaddition
Strain‐promoted azide–alkyne cycloaddition (SPAAC) can be used to generate artificial metalloenzymes (ArMs) from scaffold proteins containing a p‐azido‐L‐phenylalanine (Az) residue and catalytically active bicyclononyne‐substituted metal complexes. The high efficiency of this reaction allows rapid ArM formation when using Az residues within the scaffold protein in the presence of cysteine residues or various reactive components of cellular lysate. In general, cofactor‐based ArM formation allows the use of any desired metal complex to build unique inorganic protein materials. SPAAC covalent linkage further decouples the native function of the scaffold from the installation process because it is not affected by native amino acid residues; as long as an Az residue can be incorporated, an ArM can be generated. We have demonstrated the scope of this method with respect to both the scaffold and cofactor components and established that the dirhodium ArMs generated can catalyze the decomposition of diazo compounds and both SiH and olefin insertion reactions involving these carbene precursors.
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An Artificial Metalloenzyme for Carbene Transfer Based on a Biotinylated Dirhodium Anchored Within Streptavidin
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Cyclopropanation reaction was also performed in the E. coli periplasm.
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A Protein-Rhodium Complex as an Efficient Catalyst for Two-Phase Olefin Hydroformylation
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Aqueous Biphasic Hydroformylation Catalysed by Protein-Rhodium Complexes
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Aqueous Oxidation of Alcohols Catalyzed by Artificial Metalloenzymes Based on the Biotin–Avidin Technology
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Aqueous Phase Transfer Hydrogenation of Aryl Ketones Catalysed by Achiral Ruthenium(II) and Rhodium(III) Complexes and their Papain Conjugates
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A Rhodium Complex-Linked β-Barrel Protein as a Hybrid Biocatalyst for Phenylacetylene Polymerization
Our group recently prepared a hybrid catalyst containing a rhodium complex, Rh(Cp)(cod), with a maleimide moiety at the peripheral position of the Cp ligand. This compound was then inserted into a β-barrel protein scaffold of a mutant of aponitrobindin (Q96C) via a covalent linkage. The hybrid protein is found to act as a polymerization catalyst and preferentially yields trans-poly(phenylacetylene) (PPA), although the rhodium complex without the protein scaffold normally produces cis PPA.
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Artificial Metalloenzymes Derived from Bovine β-Lactoglobulin for the Asymmetric Transfer Hydrogenation of an Aryl Ketone – Synthesis, Characterization and Catalytic Activity
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Artificial Metalloenzymes for Enantioselective Catalysis Based on Biotin-Avidin
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Artificial Metalloenzymes for Enantioselective Catalysis: The Phenomenon of Protein Accelerated Catalysis
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Reduction of acetamidoacrylic acid. 3.0-fold protein acceleration.
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Reduction of acetamidoacrylic acid. 12.0-fold protein acceleration.
Artificial Metalloenzymes: (Strept)avidin as Host for Enantioselective Hydrogenation by Achiral Biotinylated Rhodium-Diphosphine Complexes
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Artificial Transfer Hydrogenases Based on the Biotin-(Strept)avidin Technology: Fine Tuning the Selectivity by Saturation Mutagenesis of the Host Protein
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Artificial Transfer Hydrogenases for the Enantioselective Reduction of Cyclic Imines
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Asymmetric Hydrogenation with Antibody-Achiral Rhodium Complex
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Asymmetric δ-Lactam Synthesis with a Monomeric Streptavidin Artificial Metalloenzyme
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A Whole Cell E. coli Display Platform for Artificial Metalloenzymes: Poly(phenylacetylene) Production with a Rhodium–Nitrobindin Metalloprotein
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Calculated in vivo TON assuming 12800 metalloenzymes per E. coli cell
Biotinylated Rh(III) Complexes in Engineered Streptavidin for Accelerated Asymmetric C–H Activation
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Burkavidin: A Novel Secreted Biotin-Binding Protein from the Human Pathogen Burkholderia Pseudomallei
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Catalytic Hydrogenation of Itaconic Acid in a Biotinylated Pyrphos-Rhodium(I) System in a Protein Cavity
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Chemically Engineered Papain as Artificial Formate Dehydrogenase for NAD(P)H Regeneration
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TOF = 52.1 h-1 for NAD+
Chemical Optimization of Artificial Metalloenzymes Based on the Biotin-Avidin Technology: (S)-Selective and Solvent-Tolerant Hydrogenation Catalysts via the Introduction of Chiral Amino Acid Spacers
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Conversion of a Protein to a Homogeneous Asymmetric Hydrogenation Catalyst by Site-Specific Modification with a Diphosphinerhodium (I) Moiety
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Counter Propagation Artificial Neural Networks Modeling of an Enantioselectivity of Artificial Metalloenzymes
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Computational prediction of the enantioselectivity of the hydrogenation reaction catalysed by the ArM.
Directed Evolution of Hybrid Enzymes: Evolving Enantioselectivity of an Achiral Rh-Complex Anchored to a Protein
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Direct Hydrogenation of Carbon Dioxide by an Artificial Reductase Obtained by Substituting Rhodium for Zinc in the Carbonic Anhydrase Catalytic Center. A Mechanistic Study
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Computational study of the reaction mechanism of the formation of HCOOH from CO2
Enantioselective Transfer Hydrogenation of Ketone Catalysed by Artificial Metalloenzymes Derived from Bovine β-Lactoglobulin
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Engineering a Dirhodium Artificial Metalloenzyme for Selective Olefin Cyclopropanation
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Enzyme Activity by Design: An Artificial Rhodium Hydroformylase for Linear Aldehydes
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Selectivity for the linear product over the branched product
Evolving Artificial Metalloenzymes via Random Mutagenesis
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Mutagenesis of the ArM by error-prone PCR
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Mutagenesis of the ArM by error-prone PCR
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Mutagenesis of the ArM by error-prone PCR
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Mutagenesis of the ArM by error-prone PCR