Superoxide dismutase functions to catalyze the disproportionation of superoxide into dioxygen and hydrogen peroxide. In order for the enzyme to be fully functional it must obtain copper and zinc, have an intrasubunit disulfide bond, and it must be in a dimer with another CuZnSOD (Sod1). The Copper Chaperone for CuZnSOD (CCS) has been identified as a source for copper and disulfide bond formation for CuZnSOD in Saccharomyces cerevisiae for which it is necessary for copper insertion in CuZnSOD. CCS has three distinct domains, and mutational analysis studies have confirmed that the cysteines found in domain III forming a CXC motif are essential to CCS activity. We show that the addition of copper allows for Sod1 activation in yeast via a CCS-independent mechanism. We first discovered that CCS CXC mutants previously thought to be inactive could be activated by the addition of excess copper. The addition of excess copper to ccs∆ yeast can also rescue the methionine auxotrophy and dioxygen sensitivity. This rescue can be attributed to an increase in SOD activity as a measurable increase in activity is observed. We have also shown that reduced glutathione is needed for CCS-independent activation of Sod1 in yeast. Over-expressing yeast Sod1 in ccs∆ yeast has been demonstrated to rescue the lysine auxotrophy, a sensitive test for Sod1 activity. Yeast lacking GSH1 and CCS but overexpressing Sod1 appear to have an inactive Sod1 since they are still auxotrophic for lysine. In summary, CCS may have molecular chaperone duties in addition to its role as a metallochaperone.