Low catalytic activity of the Cu()-binding motif (Xxx-Zzz-His; ATCUN) in reactive oxygen species production and inhibition by the Cu()-chelator BCS

The catalytic redox activity of Cu( ii ) bound to the motif NH 2 -Xxx-Zzz-His (ATCUN) with ascorbate and H 2 O 2 /O 2 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 C...

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Bibliographic Details
Published in:Chemical communications (Cambridge, England) England), 2018-10, Vol.54 (84), p.11945-11948
Main Authors: Santoro, Alice, Walke, Gulshan, Vileno, Bertrand, Kulkarni, Prasad P, Raibaut, Laurent, Faller, Peter
Format: Article
Language:English
Subjects:
Biochemistry, Molecular Biology
Biomolecules
Catalysis
Catalytic activity
Chelation
Chemical Sciences
Hydrogen peroxide
Inorganic chemistry
Life Sciences
Molecular biology
Oxidation
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Summary:The catalytic redox activity of Cu( ii ) bound to the motif NH 2 -Xxx-Zzz-His (ATCUN) with ascorbate and H 2 O 2 /O 2 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. The application of Cu( ii )-Xxx-Zzz-His (ATCUN-peptides) as artificial metalloenzymes is limited by their low catalytic-redox activity and disruption by Cu( i )-chelators.
ISSN:1359-7345
1364-548X
DOI:10.1039/c8cc06040a