Nitrogenase of Klebsiella pneumoniae. Inhibition of acetylene reduction by magnesium ion explained by the formation of an inactive dimagnesium-adenosine triphophate complex.

Acetylene-reducing activity of purified nitrogenase from Klebsiella pneumoniae was studied over a range of ATP and Mg(2+) concentrations at 15 degrees C, pH7.8. Inhibition at Mg(2+) concentrations of 2.5-30mm was due to the formation of the inactive complex, Mg(2)ATP. At higher Mg(2+) concentrations an additional inhibitory effect was observed. The results were consistent with a MgATP complex being the active substrate with an apparent K(m)(MgATP)=0.4mm.