Tuggle C K, Fuchs J A
J Bacteriol. 1985 Apr;162(1):448-50. doi: 10.1128/jb.162.1.448-450.1985.
Seven independently isolated glutathione reductase-deficient (gor) Escherichia coli mutants were found to have an in vivo glutathione redox state that did not significantly differ from that of the parental strain, 98 to 99% reduced. Strains containing both a gor mutation and either a trxA mutation (thioredoxin deficient) or a trxB mutation (thioredoxin reductase deficient) were able to maintain a 94 to 96% reduced glutathione pool, suggesting that glutathione can be reduced independently of glutathione reductase and thioredoxin reductase.
七个独立分离的谷胱甘肽还原酶缺陷型（gor）大肠杆菌突变体被发现其体内谷胱甘肽氧化还原状态与亲本菌株相比无显著差异，还原型谷胱甘肽占98%至99%。同时含有gor突变以及trxA突变（硫氧还蛋白缺陷型）或trxB突变（硫氧还蛋白还原酶缺陷型）的菌株能够维持94%至96%的还原型谷胱甘肽水平，这表明谷胱甘肽可以独立于谷胱甘肽还原酶和硫氧还蛋白还原酶进行还原。
