The structural analysis of the pro-oxidant copper-binding site of denatured apo-H43R SOD1 and the elucidation of the origin of the acquisition of the pro-oxidant activity.

Abstract excerpt

The pathogenesis of amyotrophic lateral sclerosis (ALS) is associated with mutations of Cu,Zn-superoxide dismutase (SOD1), which is a representative antioxidant enzyme. A previous study showed that the denatured apo-form of an ALS-linked mutant of human SOD1, His43 → Arg (H43R), obtains pro-oxidant activity as the reverse behavior of the native antioxidant activity by rebinding Cu(2+), which is considered to be...

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