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. 2012 Dec 24;14(1):434–456. doi: 10.3390/ijms14010434

Figure 2.

Figure 2

Pathway of oxidative protein folding. The formation of disulfide bonds in proteins in the ER is driven by protein disulfide isomerase (PDI) and endoplasmic reticulum oxidoreductin-1 (ERO-1). ERO-1 uses a (FAD)-dependent reaction to transfer electrons from PDI to molecular oxygen (O2), resulting in ER protein folding-induced oxidative stress. When incorrect disulfide bonds are formed, GSH assists in reducing them, and this decreases the GSH/GSSG ratio. This condition alters the redox environment in the ER.