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Abstract
Nitrogenase functions at or near its maximum capacity in vivo , despite a reported energy charge in the cell that should severely inhibit the enzyme. Deenergizing cellular membranes, which is postulated to release magnesium in mitochondria, has been reported to produce rapid inhibition of nitrogenase activity while giving only small changes in energy charge and NAD + NADH ratio. It is proposed that the level of magnesium available for complexation by the potent inhibitor ADP is the rate controlling variable for nitrogenase activity.
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