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To address the reactivities of the redox-sensitive cysteinyl residues, we also analyzed the recombinant monothiol roGFP2 variants roGFP2 C151S and roGFP2 C208S and detected small but reproducible glutathionylation-dependent changes of fluorescence at both excitation wavelengths for roGFP2 C151S (SSG) and roGFP2 C208S (SSG) (Fig

Interestingly, their analysis demonstrated that different GS-like enzymes accepted various alternate nucleophiles, including d-serine, non-natural amino acids, and alpha-amino alcohols, to yield a range of glutathione variants, but did not produce either serine- or glutamate-substituted analogs

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