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

doi:10.1021/ol030053w

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

Research output: Contribution to journal › Article › Academic › peer-review

34 Citations (Scopus)

Abstract

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 Assemblies Co-1·2, in which the Zn porphyrin moiety has been replaced by a CoII porphyrin, can act as O2 carriers.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 language	Undefined
Pages (from-to)	3367-3370
Number of pages	4
Journal	Organic letters
Volume	5
Issue number	19
DOIs	https://doi.org/10.1021/ol030053w
Publication status	Published - 2003

Keywords

IR-40758
METIS-214472

Access to Document

10.1021/ol030053w

Cite this

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title = "Heme-Protein Active Site Models via Self-Assembly in Water",

abstract = "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 Assemblies Co-1·2, in which the Zn porphyrin moiety has been replaced by a CoII porphyrin, can act as O2 carriers.",

keywords = "IR-40758, METIS-214472",

author = "R. Fiammengo and Kamil Wojciechowski and {Crego Calama}, Mercedes and A. Figoli and Matthias Wessling and David Reinhoudt and P. Timmerman",

year = "2003",

doi = "10.1021/ol030053w",

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journal = "Organic letters",

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TY - JOUR

T1 - Heme-Protein Active Site Models via Self-Assembly in Water

AU - Fiammengo, R.

AU - Wojciechowski, Kamil

AU - Crego Calama, Mercedes

AU - Figoli, A.

AU - Wessling, Matthias

AU - Reinhoudt, David

AU - Timmerman, P.

PY - 2003

Y1 - 2003

N2 - 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.

AB - 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.

KW - IR-40758

KW - METIS-214472

U2 - 10.1021/ol030053w

DO - 10.1021/ol030053w

M3 - Article

SN - 1523-7060

VL - 5

SP - 3367

EP - 3370

JO - Organic letters

JF - Organic letters

IS - 19

ER -