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Burkhard König
Researcher at University of Regensburg
Publications - 568
Citations - 27308
Burkhard König is an academic researcher from University of Regensburg. The author has contributed to research in topics: Catalysis & Photoredox catalysis. The author has an hindex of 73, co-authored 562 publications receiving 22098 citations. Previous affiliations of Burkhard König include University of Bordeaux & University of Kansas.
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Visible-Light-Mediated Radical Arylation of Anilines with Acceptor-Substituted (Hetero)aryl Halides
TL;DR: A visible-light-mediated, catalyst-free, direct (hetero)arylation of anilines with mild reaction conditions has been developed and the donor-acceptor complex formation between aniline and aryl halide is confirmed.
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Synthetic receptors for the differentiation of phosphorylated peptides with nanomolar affinities.
TL;DR: The synthetic receptors show the highest binding affinities to phosphorylated peptides under physiological conditions (HEPES, pH 7.5, 154 mM NaCl) reported thus far for artificial systems.
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Photoinitiated carbonyl-metathesis: deoxygenative reductive olefination of aromatic aldehydes via photoredox catalysis
TL;DR: Carbonyl–carbonyl olefination, known as McMurry reaction, represents a powerful strategy for the construction of oleFins.
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Visible-Light-Accelerated C-H Sulfinylation of Heteroarenes.
TL;DR: A metal-free visible-light-accelerated synthesis of heteroaromatic sulfoxides from sulfinamides and peroxodisulfate is reported and an electrophilic aromatic substitution mechanism is proposed based on the substrate scope, substitution selectivity, and competition experiments with different nucleophiles.
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Molecular analysis of the interaction of Bordetella pertussis adenylyl cyclase with fluorescent nucleotides.
Martin Göttle,Stefan Dove,Phillip Steindel,Yuequan Shen,Wei-Jen Tang,Jens Geduhn,Burkhard König,Roland Seifert +7 more
TL;DR: It is concluded that the catalytic site of CyaA possesses substantial conformational freedom to accommodate structurally diverse ligands and that certain ligands bind to CyaB even in the absence of CaM, facilitating future inhibitor design.