Characterization of a covalent polysulfane bridge in copper-zinc superoxide dismutase .
作者： Zheng You , Xiaohang Cao , Alexander B. Taylor , P. John Hart , Rodney L. Levine
DOI: 10.1021/BI901844D
关键词:
摘要: In the course of studies on human copper-zinc superoxide dismutase (SOD1) we observed a modified form protein whose mass was increased by 158 units. The covalent modification characterized, and established that it is novel heptasulfane bridge connecting two Cys111 residues in SOD1 homodimer. visualized directly crystal structure recombinant mutant SOD1, H46R/H48Q, produced yeast. reversible, with being cleaved thiols, cyanide, unfolding to expose polysulfane. polysulfane can be introduced vitro incubation purified elemental sulfur, even under anaerobic conditions presence metal chelator. Because polysulfanes polysulfides catalyze generation reactive oxygen sulfur species, may endow toxic gain function.
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