Cu/Zn superoxide dismutase (SOD1), a major intracellular antioxidant enzyme, metabolizes superoxide radicals to molecular oxygen and hydrogen peroxide (1). SOD1 is primarily a cytosolic protein, and is ubiquitously expressed in many tissues at higher levels than in the brain and spinal cord (1, 2). The structural interplay of the conserved disulfide bond and metal-site occupancy in SOD1 is of increasing interest as these post-translational modifications are known to dramatically alter the catalytic chemistry, the subcellular localization, and the susceptibility of the protein to aggregation (3). Defective SOD is linked to motor neuron death and carries implications for understanding and possible treatment of the fatal neurodegenerative disorder familial amyotrophic lateral sclerosis (FALS) (4).
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