An essential role of N-terminal domain of copper chaperone in the enzymatic activation of Cu/Zn-superoxide dismutase

Cu/Zn-superoxide dismutase (SOD1) acquires a copper ion from its copper chaperone protein (CCS). While domains 2 and 3 of CCS play roles in the SOD1 recognition and the copper binding, respectively, we propose that domain 1 is required for CCS to release the bound copper ion to SOD1.95