| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 5152483 | Journal of Inorganic Biochemistry | 2017 | 13 Pages |
Abstract
183Electrochemical and superoxide dismutase (SOD) activity studies of Cu(II) complexes of multihistidine peptides revealed that the imidazole coordinated [CuL]2+ complex of the peptide containing the HXH sequence exhibits the most significant activity, but the presence of amide nitrogen coordinated species with slightly distorted geometry could considerably contribute to the SOD activity.
Related Topics
Physical Sciences and Engineering
Chemistry
Inorganic Chemistry
Authors
Gizella Csire, Sarolta Timári, József Asztalos, Judit Mária Király, Mariann Kiss, Katalin Várnagy,