Archives of Microbiology

, Volume 141, Issue 1, pp 40–43 | Cite as

Regulation of nitrogenase activity by covalent modification in Chromatium vinosum

  • John W. Gotto
  • Duane C. Yoch
Original Papers


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.

Key words

Nitrogenase Nitrogen fixation Regulation Photosynthetic bacteria Chromatium Ammonia switch off 



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


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Copyright information

© Springer-Verlag 1985

Authors and Affiliations

  • John W. Gotto
    • 1
  • Duane C. Yoch
    • 1
  1. 1.Department of BiologyUniversity of South CarolinaColumbiaUSA

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