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53 publications
Sort by Titlearrow_drop_down Datearrow_drop_down Journalarrow_drop_down8-Amino-5,6,7,8-tetrahydroquinoline in Iridium(III) Biotinylated Cp* Complex as Artificial Imine Reductase
Diamine ligands I–IV coordinated to an iridium metal complex with the biotin moiety anchored to the Cp* ring were investigated. This strategy, in contrast to the traditional biotin–streptavidin technology that uses a biotinylated ligand in the artificial imine reductase, is practical for envisaging how the enantiodiscrimination by different Streptavidin (Sav) mutants could influence the chiral environment of the metal cofactor. Only in the case of (R)-CAMPY IV did the chirality at the metal centre and the second coordination sphere environment, which was dictated by the host protein, operate in a synergistic way, producing better enantioselectivity at a S112M Sav catalyst/catalyst ratio of 1.0 : 2.5. Under these optimized conditions, the artificial imine reductase afforded a good enantiomeric excess (83%) in the asymmetric transfer hydrogenation of 6,7-dimethoxy-1-methyl-3,4-dihydroisoquinoline.
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8-Amino-5,6,7,8-tetrahydroquinoline in Iridium(III) Biotinylated Cp* Complex as Artificial Imine Reductase
Diamine ligands I–IV coordinated to an iridium metal complex with the biotin moiety anchored to the Cp* ring were investigated. This strategy, in contrast to the traditional biotin–streptavidin technology that uses a biotinylated ligand in the artificial imine reductase, is practical for envisaging how the enantiodiscrimination by different Streptavidin (Sav) mutants could influence the chiral environment of the metal cofactor. Only in the case of (R)-CAMPY IV did the chirality at the metal centre and the second coordination sphere environment, which was dictated by the host protein, operate in a synergistic way, producing better enantioselectivity at a S112M Sav catalyst/catalyst ratio of 1.0 : 2.5. Under these optimized conditions, the artificial imine reductase afforded a good enantiomeric excess (83%) in the asymmetric transfer hydrogenation of 6,7-dimethoxy-1-methyl-3,4-dihydroisoquinoline.
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A 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 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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An Artificial Imine Reductase Based on the Ribonuclease S Scaffold
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An NAD(P)H-Dependent Artificial Transfer Hydrogenase for Multienzymatic Cascades
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Aqueous Oxidation of Alcohols Catalyzed by Artificial Metalloenzymes Based on the Biotin–Avidin Technology
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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 the Diastereoselective Reduction of NAD+ to NAD2H
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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 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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Artificial Transfer Hydrogenases for the Enantioselective Reduction of Cyclic Imines
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Asymmetric δ-Lactam Synthesis with a Monomeric Streptavidin Artificial Metalloenzyme
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Biotinylated Rh(III) Complexes in Engineered Streptavidin for Accelerated Asymmetric C–H Activation
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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+
Chimeric Streptavidins as Host Proteins for Artificial Metalloenzymes
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RCM, biotinylated Hoveyda-Grubbs second generation catalyst
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No metal
Chimeric Streptavidins as Host Proteins for Artificial Metalloenzymes
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RCM, biotinylated Hoveyda-Grubbs second generation catalyst
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Computational Insights on an Artificial Imine Reductase Based on the Biotin-Streptavidin Technology
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Prediction of the enantioselectivity by computational methods.
Cross-Regulation of an Artificial Metalloenzyme
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Cross-regulated reduction of the antibiotic enrofloxacin by an ArM.
Directed Evolution of an Artificial Imine Reductase
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Salsolidine formation; Sav mutant S112A-N118P-K121A-S122M: (R)-selective
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Salsolidine formation; Sav mutant S112R-N118P-K121A-S122M-L124Y: (S)-selective
Directed Evolution of an Artificial Imine Reductase
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Salsolidine formation; Sav mutant S112A-N118P-K121A-S122M: (R)-selective
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Salsolidine formation; Sav mutant S112R-N118P-K121A-S122M-L124Y: (S)-selective
Efficient in Situ Regeneration of NADH Mimics by an Artificial Metalloenzyme
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ArM works in combination with the ene reductase (ER) of the Old Yellow Enzyme family fromThermus scotuductus (TsOYE).
Enantioselective Transfer Hydrogenation of Ketone Catalysed by Artificial Metalloenzymes Derived from Bovine β-Lactoglobulin
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Evaluation of Chemical Diversity of Biotinylated Chiral 1,3-Diamines as a Catalytic Moiety in Artificial Imine Reductase
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Expanding the Chemical Diversity in Artificial Imine Reductases Based on the Biotin–Streptavidin Technology
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Expanding the Chemical Diversity in Artificial Imine Reductases Based on the Biotin–Streptavidin Technology
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