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 Ka>106 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.
We report on the synthesis of a receptor 4 for b,P-carotene (l), and on the binding interaction between the two which yields inclusion complex 5. The cyclodextrin 'dimer' 4 was obtained via condensation of the corresponding 4,4-(porphyrin-5,15-diyl)bis phenol 8 with 6A-dcoxy-6A-iodo-~-cyclodextrin (6) in the presence of Cs,CO,.
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