ArticleBeilstein journal of organic chemistry2016
Artificial Diels-Alderase based on the transmembrane protein FhuA.
Article in Beilstein journal of organic chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Using BpyAla to generate copper artificial metalloenzymes: a catalytic and structural study.Catalysis science & technology · 2024Article
- Designing Artificial Metalloenzymes by Tuning of the Environment beyond the Primary Coordination Sphere.Chemical reviews · 2022Review
- Artificial Metalloenzymes: From Selective Chemical Transformations to Biochemical Applications.Molecules (Basel, Switzerland) · 2020Review
- 2-Methyl-2,4-pentanediol (MPD) boosts as detergent-substitute the performance of ß-barrel hybrid catalyst for phenylacetylene polymerization.Beilstein journal of organic chemistry · 2017Article
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Authors and funding
10 authors.
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Abstract
Copper(I) and copper(II) complexes were covalently linked to an engineered variant of the transmembrane protein Ferric hydroxamate uptake protein component A (FhuA ΔCVF(tev)). 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.
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