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10 publications
Sort by Titlearrow_drop_down Datearrow_drop_down Journalarrow_drop_downA 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 Heme Enzyme for Cyclopropanation Reactions
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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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Beyond Iron: Iridium-Containing P450 Enzymes for Selective Cyclopropanations of Structurally Diverse Alkenes
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Selectivity for cis product (cis/trans = 90:1)
Capture and Characterization of a Reactive Haem– Carbenoid Complex in an Artificial Metalloenzyme
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Structure of the Mb*(NMH) haem-iron complex
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Structure of the Mb*(NMH) haem-iron–carbenoid complex
Catalytic Cyclopropanation by Myoglobin Reconstituted with Iron Porphycene: Acceleration of Catalysis due to Rapid Formation of the Carbene Species
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Cyclopropanation of styrene with ethyl diazoacetate: kcat/KM = 1.3 mM-1 * s-1, trans/cis = 99:1
Engineering a Dirhodium Artificial Metalloenzyme for Selective Olefin Cyclopropanation
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Enzyme stabilization via computationally guided protein stapling
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Stapling of protein via thioether bond formation between the noncanonical amino acid O-2-bromoethyl tyrosine and cysteine
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
Orthogonal Expression of an Artificial Metalloenzyme for Abiotic Catalysis
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Reaction of styrene with ethyl diazoacetate, cis:trans = 29:71