SUMMARY: A set of four isogenic 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 to pump protons.


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