Low catalytic activity of the Cu(ii)-binding motif (Xxx-Zzz-His; ATCUN) in reactive oxygen species production and inhibition by the Cu(i)-chelator BCS. Issue 84 (5th October 2018)

• Record Type: Journal Article
• Authors: Santoro, Alice; Walke, Gulshan; Vileno, Bertrand; Kulkarni, Prasad P.; Raibaut, Laurent; Faller, Peter
• Is Part Of: Chemical communications. Volume 54:Issue 84(2018)
• Page Start: 11945
• Page End: 11948
• Publication Date: 2018-10-05
• Subjects: Chemistry -- Periodicals; 540
• DOI: 10.1039/c8cc06040a
• Languages: English
• ISSNs: 1359-7345

Abstract

Abstract : 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. Abstract : The catalytic redox activity of Cu(ii ) bound to the motif NH2 –Xxx-Zzz-His (ATCUN) with ascorbate and H2 O2 /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.