JBIC Journal of Biological Inorganic Chemistry

, Volume 18, Issue 8, pp 985–992

Yeast copper–zinc superoxide dismutase can be activated in the absence of its copper chaperone

Authors

    • Department of Chemistry and BiochemistryUniversity of California
    • Department of ChemistryPomona College
  • Yuewei Sheng
    • Department of Chemistry and BiochemistryUniversity of California
  • Herman L. Lelie
    • Department of Chemistry and BiochemistryUniversity of California
    • Bruin Biometrics LLC
  • Lindsay Kane Barnese
    • Department of Chemistry and BiochemistryUniversity of California
    • Concordia University
  • Armando Durazo
    • Department of Chemistry and BiochemistryUniversity of California
    • Department of Chemical and Environmental EngineeringUniversity of Arizona
  • Joan Selverstone Valentine
    • Department of Chemistry and BiochemistryUniversity of California
    • Department of Bioinspired ScienceEwha Womans University
  • Edith Butler Gralla
    • Department of Chemistry and BiochemistryUniversity of California
Original Paper

DOI: 10.1007/s00775-013-1047-8

Cite this article as:
Sea, K.W., Sheng, Y., Lelie, H.L. et al. J Biol Inorg Chem (2013) 18: 985. doi:10.1007/s00775-013-1047-8

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.

Keywords

Disulfide bond Sod1 Copper chaperone CCS1 Copper transport

Copyright information

© SBIC 2013