Structural effects of stabilization and complexation of a zinc-deficient superoxide dismutase.

ABSTRACT: The activity of the erythrocyte Cu₂,Zn₂-superoxide dismutase (SOD1) is altered in Alzheimer's disease (AD) patients. These patients, compared to healthy subjects, exhibit low plasmatic zinc (Zn) levels in the presence of high plasmatic levels of copper (Cu). SOD1 is an antioxidant enzyme characterized by the presence of two metal ions, Cu and Zn, on its active site. On the SOD1, Cu exerts a catalytic role, and Zn serves a structural function. In this study, we generated a modified SOD1 characterized by an altered capacity to complex Zn. The study investigates the metal-binding dynamics of the enzyme, estimating the stability of a SOD1 protein lacking the appropriate Zn site complexation. Our mutant SOD1 possesses a double amino acid mutation (T135S and K136E) that int

SUBMITTER: Manieri TM 

PROVIDER: S-EPMC7848637 | biostudies-literature | 2021 Jan

REPOSITORIES: biostudies-literature