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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1976 Dec;73(12):4369–4373. doi: 10.1073/pnas.73.12.4369

Interactions of heterologous nitrogenase components that generate catalytically inactive complexes.

D W Emerich, R H Burris
PMCID: PMC431458  PMID: 1069989

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 oxygen-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 two molecules of C. pasteurianum Fe protein per 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 form an active or an inactive complex with the Mo-Fe proteins from six different organisms. Inhibition by nitrogenase components that form inactive complexes provides numeroius ways to study the mechanism of nitrogenase action.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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