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  • Title: Heme-protein active site models via self-assembly in water.
    Author: Fiammengo R, Wojciechowski K, Crego-Calama M, Timmerman P, Figoli A, Wessling M, Reinhoudt DN.
    Journal: Org Lett; 2003 Sep 18; 5(19):3367-70. PubMed ID: 12967276.
    Abstract:
    [structure: see text] Water-soluble models of heme-protein active sites are obtained via the self-assembly of cationic porphyrins 1 and tetrasulfonato calix[4]arene 2 (K(1.2)() = 10(5) 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 Assemblies Co-1.2, in which the Zn porphyrin moiety has been replaced by a Co(II) porphyrin, can act as O(2) carriers.
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