Institut de Chimie, UMR 7177, CNRS-Université de Strasbourg, 4 rue Blaise Pascal, 67000, Strasbourg, France.
Chem Commun (Camb). 2018 Oct 18;54(84):11945-11948. doi: 10.1039/c8cc06040a.
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.
与抗坏血酸和 H2O2/O2 结合的 motif NH2-Xxx-Zzz-His(ATCUN)上的 Cu(ii)的催化氧化还原活性非常低,并且可以通过 Cu(i)-螯合来停止。这影响了其作为人工 Cu 酶在富含 Cu(i)-螯合剂的环境(如细胞质)中通过产生活性氧物质来降解生物分子的应用。