Interactions of heterologous nitrogenase components that generate catalytically inactive complexes.

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Abstract
A unique method is described for inhibiting nitrogenase. When Clostridium pasteurianum nitrogenase is assayed in the presence of the Mo-Fe protein of Azotobacter vinelandii, all the characteristic activities of nitrogenase are inhibited. C. pasteurianum nitrogenase is unaffected by the Fe protein of A. vinelandii. The Fe protein, but not the Mo-Fe protein of C. pasteurianum, inhibits A. vinelandii nitrogenase. Both inhibitions described result from the formation of an inactive complex of A. vinelandii Mo-Fe protein and C. pasteurianum Fe protein. Complex formation requires active components, as O2 denatured proteins are ineffective. The results for titration of components of the complex against each other and kinetic data each indicate that the inactive complex consists of 2 molecules of C. pasteurianum Fe protein/molecule of A. vinelandii Mo-Fe protein. The results of kinetic experiments suggest that the Fe protein from each organism competes for the same site(s) on the A. vinelandii Mo-Fe protein. The Fe protein of C. pasteurianum will thus form an active or an inactive complex with the Mo-Fe proteins from 6 different organisms [Rhodospirillum rubrum, Spirillum lipoferum, Chromatium vinosum, Klebsiella pneumoniae, Bacillus polymyxa and A. vinelandii]. Inhibition by nitrogenase components that form inactive complexes provides numerous ways to study the mechanism of nitrogenase action.