glutathione s-transferase gst activity Glutathione S‐transferase (GST) activity in

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These variants equally preserved their GSH-transferase activity, suggesting the importance of additional factors in the modulation of the negative log of GSHs acid dissociation constant (p K a ), including the ability to optimally arrange the well-described electron-sharing network which generates a positively charged electrostatic field in the G-site of GSTs 40,41

aegerita , H

The emission spectra show that the spectrum of TPE-DCV peaks at 523 nm in the presence of GSH, which blue-shifts about 40 nm as compared to that of the TPE-DCV aggregates in water (Figure S3)