Say, I have a protein in cytoplasm, which redox potential measured in vitro is +200 mV. The redox potential of cytoplasm appears to be say +50 eV. Knowing that, can I conclude that my protein is in reduced state at that moment? Is that possible, that protein would stay oxidized even if placed in reducing environment?
Yes, you may conclude that your protein is reduced. The tendency for oxidation can depend on other protein specific factors other than redox potential. For example, the copper center of the electron transfer mediating protein amicyanin is not readily oxidized my molecular oxygen in the reaction buffer. It requires an oxidizing agent such as ferrocyanide or it's biological electron acceptor cytochrome c551. However, the heme in MauG protein is readily reoxidized and requires an anaerobic environment.
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