Issue 5, 2012
From the journal:

Organic & Biomolecular Chemistry

Triazacyclophane (TAC)-scaffolded histidine and aspartic acid residues as mimics of non-heme metalloenzyme active sites†

H. Bauke Albada,‡a   Fouad Soulimani,b   Hans J. F. Jacobs,a   Cees Versluis,c   Bert M. Weckhuysenb  and  Rob M. J. Liskamp*a  

* Corresponding authors

a Utrecht Institute for Pharmaceutical Sciences, Medicinal Chemistry & Chemical Biology, Faculty of Science, University of Utrecht, Universiteitsweg 99, Utrecht, The Netherlands
E-mail: r.m.j.liskamp@uu.nl
Fax: +31-30-2536655
Tel: +31-30-2537396

b Inorganic Chemistry and Catalysis group, Department of Chemistry, Faculty of Science, University of Utrecht, Universiteitsweg 99, Utrecht, The Netherlands

c Biomolecular Mass Spectrometry and Proteomics Group, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Faculty of Science, University of Utrecht, Universiteitsweg 99, Utrecht, The Netherlands

Abstract

We describe the synthesis and coordination behaviour to copper(II) of two close structural triazacyclophane-based mimics of two often encountered aspartic acid and histidine containing metalloenzyme active sites. Coordination of these mimics to copper(I) and their reaction with molecular oxygen leads to the formation of dimeric bis(μ-hydroxo) dicopper(II) complexes.

Graphical abstract: Triazacyclophane (TAC)-scaffolded histidine and aspartic acid residues as mimics of non-heme metalloenzyme active sites

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Article information

DOI
https://doi.org/10.1039/C1OB06806G
Article type
Paper
Submitted
19 Aug 2011
Accepted
09 Nov 2011
First published
16 Nov 2011

Org. Biomol. Chem., 2012,10, 1088-1092

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Triazacyclophane (TAC)-scaffolded histidine and aspartic acid residues as mimics of non-heme metalloenzyme active sites

H. B. Albada, F. Soulimani, H. J. F. Jacobs, C. Versluis, B. M. Weckhuysen and R. M. J. Liskamp, Org. Biomol. Chem., 2012, 10, 1088 DOI: 10.1039/C1OB06806G

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