Heme-Protein Active Site Models via Self-Assembly in Water

R. Fiammengo, Kamil Wojciechowski, Mercedes Crego Calama, A. Figoli, Matthias Wessling, David Reinhoudt, P. Timmerman

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34 Citations (Scopus)


Water-soluble models of heme-protein active sites are obtained via the self-assembly of cationic porphyrins 1 and tetrasulfonato calix[4]arene 2 (K1·2 = 105 M-1). Selective binding of ligands either outside or inside the cavity of assemblies 1·2 via coordination to the zinc center has been observed. Small ligands such as 4-methylpyridine and 1-methylimidazole are encapsulated, while the bulkier caffeine is bound outside. Assemblies Co-1·2, in which the Zn porphyrin moiety has been replaced by a CoII porphyrin, can act as O2 carriers.
Original languageUndefined
Pages (from-to)3367-3370
Number of pages4
JournalOrganic letters
Issue number19
Publication statusPublished - 2003


  • IR-40758
  • METIS-214472

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