Abstract
Abstract An artificial enzyme was constructed with a combination of the single-walled vesicle of N,N-dihexadecyl-Nα-[6-(trimethylammonio)hexanoyl]-l-alaninamide bromide (N+C5Ala2C16) and a simple vitamin Bi12 model; (11-hydroxyimino-4,10-dipropyl-5,9-diazatrideca-4,9-dien-3-one oximato)cobalt, [Co(C2C3)(DO)(DOH)pn], or [N-(2-hydroxyiminocyclohexylidene)-N′-(cyclohexyliden-2-one oximato)-1,3-diaminopropane]cobalt, [Co(ch)(DO)(DOH)pn]. Carbon-skeleton rearrangement reactions of alkyl ligands bound to the cobalt complex were markedly favored in the single-walled vesicle, relative to the reactions in methanol and benzene, under anaerobic photolysis conditions at ordinary temperatures. The cobalt complex incorporated into the intramembrane domain is subjected to significant repression of its molecular motion and to desolvation as confirmed by fluorescence and fluorescence polarization measurements. The 1,2-migration of cyano and carboxylic ester groups involved in the alkyl ligands is plausibly enhanced by such effects.
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