[HTML][HTML] Insights into the role of the unusual disulfide bond in copper-zinc superoxide dismutase
The functional and structural significance of the intrasubunit disulfide bond in copper-zinc
superoxide dismutase (SOD1) was studied by characterizing mutant forms of human SOD1
(hSOD) and yeast SOD1 lacking the disulfide bond. We determined x-ray crystal structures
of metal-bound and metal-deficient hC57S SOD1. C57S hSOD1 isolated from yeast
contained four zinc ions per protein dimer and was structurally very similar to wild type. The
addition of copper to this four-zinc protein gave properly reconstituted 2Cu, 2Zn C57S …
superoxide dismutase (SOD1) was studied by characterizing mutant forms of human SOD1
(hSOD) and yeast SOD1 lacking the disulfide bond. We determined x-ray crystal structures
of metal-bound and metal-deficient hC57S SOD1. C57S hSOD1 isolated from yeast
contained four zinc ions per protein dimer and was structurally very similar to wild type. The
addition of copper to this four-zinc protein gave properly reconstituted 2Cu, 2Zn C57S …
