2 publications
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Artificial Diels–Alderase based on the Transmembrane Protein FhuA
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Beilstein J. Org. Chem. 2016, 12, 1314-1321, 10.3762/bjoc.12.124
Copper(I) and copper(II) complexes were covalently linked to an engineered variant of the transmembrane protein Ferric hydroxamate uptake protein component A (FhuA ΔCVFtev). Copper(I) was incorporated using an N-heterocyclic carbene (NHC) ligand equipped with a maleimide group on the side arm at the imidazole nitrogen. Copper(II) was attached by coordination to a terpyridyl ligand. The spacer length was varied in the back of the ligand framework. These biohybrid catalysts were shown to be active in the Diels–Alder reaction of a chalcone derivative with cyclopentadiene to preferentially give the endo product.
Metal: CuLigand type: TerpyridineHost protein: Ferric hydroxamate uptake protein component: A (FhuA)Anchoring strategy: Cystein-maleimideOptimization: ChemicalNotes: ---
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Generation of a Hybrid Sequence-Specific Single Stranded Deoxyribonuclease
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Science 1987, 238, 1401-1403, 10.1126/science.3685986
The relatively nonspecific single-stranded deoxyribonuclease, staphylococcal nuclease, was selectively fused to an oligonucleotide binding site of defined sequence to generate a hybrid enzyme. A cysteine was substituted for Lys116 in the enzyme by oligonucleotide-directed mutagenesis and coupled to an oligonucleotide that contained a 3'-thiol. The resulting hybrid enzyme cleaved single-stranded DNA at sites adjacent to the oligonucleotide binding site.
Metal: CaLigand type: UndefinedHost protein: Staphylococcal nucleaseAnchoring strategy: ---Optimization: ---Notes: Engineered sequence specificity