Diffuse binding of Zn(2+) to the denatured ensemble of Cu/Zn superoxide dismutase 1.

ABSTRACT: The stability and structural properties of the metalloprotein superoxide dismutase 1 (SOD1) are found to depend critically on metal ions. Native SOD1 monomers coordinate one structural Zn(2+) and one redox-active Cu(2+/1+) to the active site. To do this, the Zn(2+) ions need to interact with the SOD1 protein on the denatured side of the folding barrier, prior to the formation of the folding nucleus. In this study, we have examined at residue level the nature of this early Zn(2+) binding by NMR studies on the urea denatured-state of SOD1. Nearly complete backbone chemical shift assignments were obtained in 9 M urea at physiological pH, conditions at which NMR studies are scarce. Our results demonstrate that SOD1 is predominantly unstructured under these conditions. Chemical-shift changes up

SUBMITTER: Szpryngiel S 

PROVIDER: S-EPMC4309841 | biostudies-literature | 2015

REPOSITORIES: biostudies-literature