TY  - JOUR
AU  - Paul, Melanie
AU  - Teubner, Melissa
AU  - Grimm‐Lebsanft, Benjamin
AU  - Golchert, Christiane
AU  - Meiners, Yannick
AU  - Senft, Laura
AU  - Keisers, Kristina
AU  - Liebhäuser, Patricia
AU  - Rösener, Thomas
AU  - Biebl, Florian
AU  - Buchenau, Sören
AU  - Naumova, Maria
AU  - Murzin, Vadim
AU  - Krug, Roxanne
AU  - Hoffmann, Alexander
AU  - Pietruszka, Jörg
AU  - Ivanović‐Burmazović, Ivana
AU  - Rübhausen, Michael
AU  - Herres‐Pawlis, Sonja
TI  - Exceptional Substrate Diversity in Oxygenation Reactions Catalyzed by a Bis(μ‐oxo) Copper Complex
JO  - Chemistry - a European journal
VL  - 26
IS  - 34
SN  - 1521-3765
CY  - Weinheim
PB  - Wiley-VCH
M1  - FZJ-2020-03835
SP  - 7556 - 7562
PY  - 2020
AB  - The enzyme tyrosinase contains a reactive side‐on peroxo dicopper(II) center as catalytically active species in C−H oxygenation reactions. The tyrosinase activity of the isomeric bis(μ‐oxo) dicopper(III) form has been discussed controversially. The synthesis of bis(μ‐oxo) dicopper(III) species [Cu2(μ‐O)2(L1)2](X)2 ([O1](X)2, X=PF6−, BF4−, OTf−, ClO4−), stabilized by the new hybrid guanidine ligand 2‐{2‐((dimethylamino)methyl)phenyl}‐1,1,3,3‐tetramethylguanidine (L1), and its characterization by UV/Vis, Raman, and XAS spectroscopy, as well as cryo‐UHR‐ESI mass spectrometry, is described. We highlight selective oxygenation of a plethora of phenolic substrates mediated by [O1](PF6)2, which results in mono‐ and bicyclic quinones and provides an attractive strategy for designing new phenazines. The selectivity is predicted by using the Fukui function, which is hereby introduced into tyrosinase model chemistry. Our bioinspired catalysis harnesses molecular dioxygen for organic transformations and achieves a substrate diversity reaching far beyond the scope of the enzyme.
LB  - PUB:(DE-HGF)16
C6  - pmid:32104930
UR  - <Go to ISI:>//WOS:000533570100001
DO  - DOI:10.1002/chem.202000664
UR  - https://juser.fz-juelich.de/record/885452
ER  -