Chaperones for Copper-Zinc Superoxide Dismutase

Copper Chaperones for Copper-Zinc Superoxide Dismutase 

The studies presented in Sections I and II above hrmly establish the need for a copper chaperone to deliver the reactive metal to the enzymes 

EDTA (Ki 1.6 X 10 M) (Rae et al., 1999). The primary conclusion derived from these studies is that in the presence of copper scavengers, Cu(I)yCCS activates ySODl hut Cu(l)GSH and CUSO4 cannot. Importantly, the copper insertion event likely occurs with direct transfer of the metal ion from yCCS to the ySODl, as copper ions that might possibly dissociate from the yCCS or GSH donor molecules are rapidly sequestered by the BCS competitor molecule, which is present in 20-fold excess over the copper donor molecules under these assay conditions. This in turn suggests that specific protein-protein interactions are involved in the recognition of ySODl by yCCS (Rae et al., 1999). 

ScNzosaccharomyces pombe Arabldopsis lhallana Tomalo Soybean 

G K sjjwix ehae.lksvneg [Metallothionein-llke domain truncated] 

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III. Copper Chaperones for Copper-Zinc Superoxide Dismutase. 180... 

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