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The active site of Escherichia coli glutaredoxin-3 (Grx3) consists of two redox active cysteine residues in the sequence -C 11 -P-Y-C 14 -H-. The 1 H NMR resonance of the cysteine thiol proton of Cys-14 in reduced Grx3 is observed at 7.6 ppm. The large downfield shift and NOEs observed with this thiol proton resonance suggest the presence of a hydrogen bond with the...
We have examined the activity of protein disulfide isomerase (PDI) and glutaredoxin (Grx) 1, 2 and 3 from Escherichia coli to catalyze the cleavage of glutathionylated ribonuclease A (RNase-SG) by 1 mM GSH to yield reduced RNase. Apparent K m values for RNase-SG were similar, 2-10 μM, for Grx 1, 3 and PDI but Grx 1 and Grx 3 showed 500-fold higher turnover numbers than PDI. The atypical Grx...
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