ATP synthetase associated with the nitrogenase of Azotobacter vinelandii.

Preparations of nitrogenase from $\text{Azotobacter vinelandii}$ show an ATP synthetase activity when incubated in the presence of ADP, phosphate, ammonium chloride and an oxidizing agent. The synthesis is linked to an oxidation-reduction and the activity parallels nitrogenase activity through purification and in a step gradient sedimentation. The reductive dephosphorylation of nitrogen fixation may possibly be reversed to yield an oxidative phosphorylation.