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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.

biochemical journal

Nitrogenase of <i>Klebsiella pneumoniae</i>. Inhibition of acetylene reduction by magnesium ion explained by the formation of an inactive dimagnesium–adenosine triphosphate complex

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