The Cu, Zn Superoxide Dismutase: Not Only a Dismutase Enzyme

The Cu, Zn Superoxide Dismutase: Not Only a Dismutase Enzyme

The Cu,Zn superoxide dismutase (SOD1) is an ubiquitary cytosolic dimeric carbohydrate free molecule, belonging to a family of isoenzymes involved in the scavenger of superoxide anions. This effect certainly represents the main and well known function ascribed to this enzyme. Here we highlight new aspects of SOD1 physiology that point out some inedited effects of this enzyme in addition to the c...

Copper chaperone for superoxide dismutase is essential to activate mammalian Cu/Zn superoxide dismutase.

Recent studies in Saccharomyces cerevisiae suggest that the delivery of copper to Cu/Zn superoxide dismutase (SOD1) is mediated by a cytosolic protein termed the copper chaperone for superoxide dismutase (CCS). To determine the role of CCS in mammalian copper homeostasis, we generated mice with targeted disruption of CCS alleles (CCS(-/-) mice). Although CCS(-/-) mice are viable and possess nor...

Cu/Zn Superoxide Dismutase Misfolding in Amyotrophic Lateral Sclerosis

Folding and Aggregation of Cu, Zn-Superoxide Dismutase

1.1 ALS and SOD1 In 1993, a genetic link was established between amyotrophic lateral sclerosis (ALS) and mutant forms of Cu,Zn superoxide dismutase (SOD1) (Deng et al. 1993; Rosen et al. 1993), an antioxidant enzyme that catalyzes the dismutation of the damaging free radical superoxide anion (O2-) to hydrogen peroxide (H2O2) and diatomic oxygen (O2) via cyclic reduction and oxidation of a prote...

Redox activation of mitochondrial intermembrane space Cu,Zn-superoxide dismutase.

The localization of Cu,Zn-superoxide dismutase in the mitochondrial intermembrane space suggests a functional relationship with superoxide anion (O2*-) released into this compartment. The present study was aimed at examining the functionality of Cu,Zn-superoxide dismutase and elucidating the molecular basis for its activation in the intermembrane space. Intact rat liver mitochondria neither sca...