Abstract
The catalytic redox activity of Cu(ii) bound to the motif NH2-Xxx-Zzz-His (ATCUN) with ascorbate and H2O2/O2 is very low and can be stopped via Cu(i)-chelation. This impacts its application as an artificial Cu-enzyme to degrade biomolecules via production of reactive oxygen species in a Cu(i)-chelator rich environment like the cytosol.
Original language | English |
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Pages (from-to) | 11945-11948 |
Number of pages | 4 |
Journal | Chemical Communications |
Volume | 54 |
Issue number | 84 |
DOIs | |
State | Published - 18 Oct 2018 |
Bibliographical note
Publisher Copyright:© 2018 The Royal Society of Chemistry.
Funding
A. S. and G. W were supported by the IDEX PhD program (University of Strasbourg) and an EMBO short-term fellowship (ASTF 505-2016), respectively. The Frontier Research in Chemistry Foundation of Strasbourg (P. F.), the University of Strasbourg Institute for Advanced Study (USIAS) (P. F.), IDEX attractivity program of the University of Strasbourg (L. R.) and the Reseau NAtional de Rpe interDisciplinaire (RENARD, Fédération IR-RPE CNRS #3443) are acknowledged. P. F. would like to thank Dr C. Hureau (LCC, Toulouse) for helpful discussions. P. K. would like to acknowledge funds from the Department of Science and Technology, India (EMR/2014/001235). We would like to thank Dr Romain Ruppert (UMR7177 - Institut de Chimie, Strasbourg) for the gift of the Phen and DmBipy compound.
Funders | Funder number |
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European Molecular Biology Organization | ASTF 505-2016 |