Figure 8: Cu(I)-hCCS catalyses disulfide bond formation on SOD1 mutants. | Nature Communications

Figure 8: Cu(I)-hCCS catalyses disulfide bond formation on SOD1 mutants.

From: In-cell NMR reveals potential precursor of toxic species from SOD1 fALS mutants

Figure 8: Cu(I)-hCCS catalyses disulfide bond formation on SOD1 mutants.

1H–15N SOFAST-HMQC spectra of cells expressing [15N]Cys-labelled fALS SOD1 mutants together with hCCS, in the presence of both zinc and copper, showing that Cu(I)-hCCS catalyses the formation of the SOD1 intramolecular disulfide bond. SOD1 cysteine crosspeaks (black) are labelled. For Cys57 and Cys146 crosspeaks, the oxidation state is also indicated. A crosspeak from [15N]Cys-labelled hCCS is marked with an asterisk. Signals arising from cellular background are shown in grey. The cysteine assignments of fALS SOD1 mutants are taken from that of WT SOD1 cysteines, which were obtained by comparing in vitro spectra of reduced and oxidized [15N]Cys-labelled SOD1 with the available backbone assignments4,58.

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