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Regulation of nitrogenase activity by covalent modification in Chromatium vinosum

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Abstract

Nitrogenase in Chromatium vinosum was rapidly, but reversibly inhibited by NH +4 . Activity of the Fe protin component of nitrogenase required both Mn2+ and activating enzyme. Activating enzyme from Rhodospirillum rubrum could replace Chromatium chromatophores in activating the Chromatium Fe protein, and conversely, a protein fraction prepared from Chromatium chromatophores was effective in activating R. rubrum Fe protein. Inactive Chromatium Fe protein contained a peptide covalently modified by a phosphate-containing molecule, which migrated the same in SDS-polyacrylamide gels as the modified subunit of R. rubrum Fe protein. In sum, these observations suggest that Chromatium nitrogenase activity is regulated by a covalent modification of the Fe protein in a manner similar to that of R. rubrum.

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Abbreviations

HEPES:

N-2-hydroxyethyl piperazine-N-2-ethanesulfonic acid

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Gotto, J.W., Yoch, D.C. Regulation of nitrogenase activity by covalent modification in Chromatium vinosum . Arch. Microbiol. 141, 40–43 (1985). https://doi.org/10.1007/BF00446737

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  • DOI: https://doi.org/10.1007/BF00446737

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