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 Functional, Semisynthetic [FeFe]-Hydrogenase in a Photosynthetic Microorganism
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Energy Environ. Sci. 2018, 11, 3163-3167, 10.1039/C8EE01975D
[FeFe]-Hydrogenases are hydrogen producing metalloenzymes with excellent catalytic capacities, highly relevant in the context of a future hydrogen economy. Here we demonstrate the synthetic activation of a heterologously expressed [FeFe]-hydrogenase in living cells of Synechocystis PCC 6803, a photoautotrophic microbial chassis with high potential for biotechnological energy applications. H2-Evolution assays clearly show that the non-native, semi-synthetic enzyme links to the native metabolism in living cells.
Metal: FeHost protein: HydA1 ([FeFe]-hydrogenase) from C. reinhardtiiAnchoring strategy: ReconstitutionOptimization: Chemical & geneticNotes: ---