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A Supramolecular Enzyme Mimic That Catalyzes the 15,15′ Double Bond Scission of β , β ‐Carotene
Author(s) -
French Richard R.,
Holzer Philipp,
Leuenberger Michele G.,
Woggon WolfD.
Publication year - 2000
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/(sici)1521-3773(20000403)39:7<1267::aid-anie1267>3.0.co;2-7
Subject(s) - bond cleavage , cleavage (geology) , supramolecular chemistry , chemistry , stereochemistry , porphyrin , double bond , conjugated system , enzyme , carotene , cyclodextrin , crystallography , photochemistry , biochemistry , catalysis , polymer chemistry , crystal structure , organic chemistry , materials science , polymer , fracture (geology) , composite material
Two Ru‐porphyrin‐linked β ‐cyclodextrin units form the supramolecular system, which as an enzyme mimic for β , β ‐carotene 15,15′‐dioxgenase binds two substrates of the enzyme with K a >10 6 M −1 and selectively catalyzes the cleavage of the central carotinoid bond in the presence of tert ‐butylhydroperoxide (see picture). Mechanistic aspects of this unusual cleavage of E ‐configured, conjugated double bonds are discussed.