The Zn-Site in Bovine Copper, Zinc Superoxide Dismutase Studied by ¹¹¹Cd Pac

Abstract

The active site in bovine copper, zinc superoxide dismutase (Cu₂. Zn₂ SOD) has been studied by ¹¹¹Cd time differential Perturbed Angular Correlation (PAC) on enzyme with Zn²⁺ replaced by excited 'Cd²⁺. The PAC spectra obtained for both the oxidized and the reduced form of Cu₂Cd₂SOD show no asymmetry between the two Zn-sites in the dimeric enzyme. The spectv further reveal that a significant change has taken place at the Zn-site in the reduced form compared to the oxidized form.

Semi-empirical calculations based on the Angular Overlap Model (AOM) and coordinates from the crystal structure of the native enzyme are in agreement with the experimental PAC data of the oxidized enzyme. The results indicate that Cd²⁺ coordinates in the same manner as Zn²⁺ and that the crystal structure of SOD is valid for the enzyme in solution. The PAC spectrum of the reduced enzyme can be explained by extending the AOM calculations to the enzyme in the reduced form and assuming that the imidazol ring of His61 is no longer bridging the copper and cadmium ions in the reduced state.

Key Words:

• Superoxide dismutase
• zinc
• cadmium
• active site
• structure
• spectroscopy.