Hydrophobie vitamin B12. Part 6. † Carbon-skeleton rearrangement via formation of Host-guest complexes derived from an 'Octopus' azaparacyclophane and hydrophobie vitamin B12 derivatives: A novel holoenzyme model system

Yukito Murakami, Yoshio Hisaeda, Jun Ichi Kikuchi, Teruhisa Ohno, Masashi Suzuki, Yoshihisa Matsuda, Takeo Matsuura

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The alkylation reactions of a hydrophobic vitamin B12 derivative with alkyl bromides in an 'octopus' azaparacyclophane having eight hydrocarbon chains have been investigated. Molecular discrimination has been shown to originate from electrostatic interaction between the octopus cyclophane and the alkyl bromides. Alkylation was enhanced by desolvation and proximity effects operating on the reacting species via formation of a ternary complex composed of the octopus cyclophane, the hydrophobic vitamin B12 derivative, and an alkyl halide. Carbon-skeleton rearrangement reactions of alkyl ligands bound to the hydrophobic vitamin B12 were found to be markedly favoured in the hydrophobic cavity provided by the octopus cyclophane, relative to the reactions in methanol and benzene, under anaerobic photolysis conditions at ordinary temperatures. The same reactions took place readily in solid benzene below 4 °C under similar conditions. The central cobalt atom of the hydrophobic vitamin B12 participates in the rearrangement reaction via formation of a tight pair with an alkyl radical species. Nonenzymic rearrangement reactions have been shown here to proceed quite efficiently by employing a relevant apoenzyme model.

Original languageEnglish
Pages (from-to)1237-1246
Number of pages10
JournalJournal of the Chemical Society, Perkin Transactions 2
Issue number7
Publication statusPublished - Jan 1 1988


All Science Journal Classification (ASJC) codes

  • Chemistry(all)

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