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. 2021 Jun 4;10(6):913. doi: 10.3390/antiox10060913

Figure 4.

Figure 4

Reduction of disulfide bridges C141-C144 and C104-C133 of FurA by TrxA. One micromolar of FurA triple cysteine mutants C101/104/133S (A) and C101/104/133S (B) were incubated with 0.5 µM TrxA in the presence of 0.2 mM NADPH, 0.5 mM EDTA, and 5 nM NTR to assess their reduction by NTR-reduced TrxA. FurA triple cysteine mutants were also incubated with 0.2 mM NADPH and 5 nM NRT to determine whether NADPH-reduced NTR affected their redox status and with 1 mM DTT as a positive control for protein reduction. Proteins were then precipitated with 10% (w/v) TCA, incubated with 20 mM AMS, loaded on non-reducing 15% SDS–polyacrylamide gels and stained with Coomassie.