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An investigation of the in vitro and in vivo redox states of the Escherichia coli periplasmic oxidoreductases DsbA and DsbC was conducted using genetic selections. Results indicated DsbC acts as a disulfide isomerase. Furthermore, DsbA is a more effective oxidant than DsbC of protein dithiols. Proteins which are effected by DsbC deletions do not have cysteines paired consecutively.

The oxidized state of dsbA periplasmic protein catalyzes disulfide bond formation in proteins. The dsbA protein refolds the misfolded IGF-I by restructuring two disulfide bonds. Disulfide isomerase is the reduction state of dsbA protein. The function of the dsbA protein depends on the redox state of the protein under physiological conditions.