Abstract
A simple gel equilibration method differing from gel filtration was used for the measurement of ATP binding by purified nitrogenase components from Clostridium pasteurianum. It was clearly established that the binding site in on the iron protein of nitrogenase (Fe protein). Mg 2+ is required for the binding. The Fe protein also binds MgADP. The number of binding sites and the dissociation constants of the MgATP- and MgADP-Fe protein complexes were measured. Inhibition studies indicate that MgADP inhibits MgATP binding by occupying one of the two MgATP sites; MgADP appears to increase slightly the binding of MgATP at its second site.
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