| Range |
-0.26 to -0.28 V
|
| Organism |
Bacteria Escherichia coli |
| Reference |
Hwang, C., Sinskey, A. J., and Lodish, H. F. (1992). Oxidized redox state of glutathione in the endoplasmic reticulum. Science 257, 1496–1502 p.1499 left column top paragraphPubMed ID1523409
|
| Primary Source |
[4] Gilbert HF. Molecular and cellular aspects of thiol-disulfide exchange. Adv Enzymol Relat Areas Mol Biol. 1990 63 :69-172.PubMed ID2407068
|
| Method |
P.1499 left column top paragraph: "...calculated from the reduced state of E. coli thioredoxin." |
| Comments |
P.1498 right column: "These analyses explain why Escherichia coli cannot properly fold recombinant proteins with disulfide bonds, typical GSH/GSSG ratios for E. coli are in the range of 50:1 to 200:1 (ref 20), which is in agreement with the estimated redox potential of ~-0.26 to -0.28 V calculated from the redox state of E. coli thioredoxin (primary source)." |
| Entered by |
Avi Flamholz |
| ID |
113978 |