Pope N R, Cole J A
J Gen Microbiol. 1982 Jan;128(1):219-22. doi: 10.1099/00221287-128-1-219.
A set of four isogenic Escherichia coli strains has been constructed in which all possible combinations of NADH- and formate-dependent nitrite reductases are active or inactive. Each pathway can be inactivated genetically without a corresponding loss in the other activity: the two pathways are therefore biochemically independent. The generation of a membrane potential during nitrite reduction by formate has been demonstrated using an ion-selective electrode specific for a lipophilic cation. The observed energy conservation results, at least in part, from the ability of formate dehydrogenase in E. coli to pump protons.
构建了一组四个同基因大肠杆菌菌株，其中NADH依赖性和甲酸依赖性亚硝酸还原酶的所有可能组合均处于活性或非活性状态。每条途径都可以通过基因方式失活，而不会相应地损失另一种活性：因此，这两条途径在生化上是独立的。使用对亲脂性阳离子具有特异性的离子选择性电极，已证明在甲酸还原亚硝酸盐的过程中会产生膜电位。观察到的能量守恒结果至少部分源于大肠杆菌中的甲酸脱氢酶泵送质子的能力。
