Affordable Access

Publisher Website

Catalytic activity studies of some copper(II)-histidine-containing dipeptide complexes on aqueous superoxide ion dismutation

Authors
Journal
Journal of Inorganic Biochemistry
0162-0134
Publisher
Elsevier
Publication Date
Volume
17
Issue
4
Identifiers
DOI: 10.1016/s0162-0134(00)80092-6

Abstract

Abstract The reactivity of histidine-containing copper(II)-dipeptide complexes toward O 2 − produced by the pulse radiolysis technique was investigated. Whereas the His-X-Cu 2− complexes (X = Phe, Ala, Val, Tyr) display a relatively high superoxide dismutase (SOD) activity, that of the Ala-His-Cu 2+ complex is very low and Val-His-Cu 2+ as well as Phe-His-Cu 2+ are ineffective. This difference in behavior can be explained by the fact that the Cu ion is not chelated in the same way in the different complexes, as shown by stability constant determination and other spectral studies. This allows one to conclude that in His-X-Cu 2+, the dipeptide coordinates to the metal ion by only two nitrogens, whereas in X-His-Cu 2+ it behaves as a tridentate ligand with three nitrogen atoms bound to the metal.

There are no comments yet on this publication. Be the first to share your thoughts.