ArticleJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2013
Yeast copper-zinc superoxide dismutase can be activated in the absence of its copper chaperone.
Article in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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5 citing papers in PubMed, 7 citations in OpenAlex.
- The structure-function relationships and physiological roles of MnSOD mutants.Bioscience reports · 2022Review
- Article
- Copper-zinc superoxide dismutase is activated through a sulfenic acid intermediate at a copper ion entry site.The Journal of biological chemistry · 2017Article
- Insights into the role of the unusual disulfide bond in copper-zinc superoxide dismutase.The Journal of biological chemistry · 2015Article
- Superoxide dismutases and superoxide reductases.Chemical reviews · 2014Review
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Authors and funding
7 authors at 3 institutions in 3 countries.
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Abstract
Copper-zinc superoxide dismutase (Sod1) is an abundant intracellular enzyme that catalyzes the disproportionation of superoxide to give hydrogen peroxide and dioxygen. In most organisms, Sod1 acquires copper by a combination of two pathways, one dependent on the copper chaperone for Sod1 (CCS), and the other independent of CCS. Examples have been reported of two exceptions: Saccharomyces cerevisiae, in which Sod1 appeared to be fully dependent on CCS, and Caenorhabditis elegans, in which Sod1 was completely independent of CCS. Here, however, using overexpressed Sod1, we show there is also a significant amount of CCS-independent activation of S. cerevisiae Sod1, even in low-copper medium. In addition, we show CCS-independent oxidation of the disulfide bond in S. cerevisiae Sod1. There appears to be a continuum between CCS-dependent and CCS-independent activation of Sod1, with yeast falling near but not at the CCS-dependent end.
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