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These percentages are almost identical to the percentages for the second-order rate constants of the same mutants with GSSCys as a substrate 14 , indicating that GSH also occupies the 1st glutathione-interaction site of PfGrx for the reduction of roGFP2 WT (S 2 )

The shift in the redox-potential was around 14 mV to 243 mV, supporting the role of DsbA in oxidative protein folding, however, the relatively small size of the shift suggests the presence of an alternative mechanism for the introduction of disulfide bonds

Journal of medicine and life 2019, 12 (2), 113

designed and constructed the mutant and complemented strains used in this study

10.1073/pnas.0404458101 Proc
