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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

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.

Key words

Nitrogenase Nitrogen fixation Regulation Photosynthetic bacteria Chromatium Ammonia switch off 

Abbreviation

HEPES

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

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References

  1. Bognar A, Desrosiers L, Libman M, Newman EB (1982) Control of nitrogenase in a photosynthetic autotrophic bacterium, Ectothiorhodospira sp. J Bacteriol 152:706–713Google Scholar
  2. Bose SK (1963) Media for anaerobic growth of photosynthetic bacteria. In: Gest H, San Pietro A, Vernon LP (eds) Bacterial photosynthesis. Antioch Press, Yellow Springs, Ohio, pp 501–510Google Scholar
  3. Bregoff HM, Kamen MD (1952) Photohydrogen production in Chromatium. J Bacteriol 63:147–149Google Scholar
  4. Carithers RP, Yoch DC, Arnon DI (1979) Two forms of nitrogenase from the photosynthetic bacterium Rhodospirillum rubrum. J Bacteriol 137:779–789Google Scholar
  5. Evans MCW, Telfer A, Smith RV (1973) The purification and some properties of the molybdenum-iron protein of Chromatium nitrogenase. Biochim Biophys Acta 310:344–352Google Scholar
  6. Gest H, Kamen MD, Bregoff HM (1950) Studies on the metabolism of photosynthetic bacteria. V. Photoproduction of hydrogen and nitrogen fixation by Rhodospirillum rubrum. J Biol Chem 182:153–170Google Scholar
  7. Gotto JW, Yoch DC (1982a) Regulation of Rhodospirillum rubrum nitrogenase activity: properties and interconversion of active and inactive Fe protein. J Biol Chem 257:2868–2873Google Scholar
  8. Gotto JW, Yoch DC (1982b) Purification and Mn2+ activation of Rhodospirillum rubrum nitrogenase activating enzyme. J Bacteriol 152:714–721Google Scholar
  9. Jouanneau Y, Meyer CM, Vignais PM (1983) Regulation of nitrogenase activity through iron protein interconversion into an active and an inactive form in Rhodopseudomonas capsulata. Biochim Biophys Acta 749:318–328Google Scholar
  10. Lowry OH, Rosebrough NJ, Farr AL, Randall RJ (1951) Protein measurement with the Folin phenol reagent. J Biol Chem 193:265–275Google Scholar
  11. Ludden PW, Burris RH (1976) Activating factor for the iron protein of nitrogenase from Rhodospirillum rubrum. Science 194:424–426Google Scholar
  12. Ludden PW, Okon Y, Burris RH (1978) The nitrogenase system of Spirillum lipoferum. Biochem J 173:1001–1003Google Scholar
  13. Ludden PW, Preston GG, Dowling TE (1982) Comparison of active and inactive forms of iron protein from Rhodospirillum rubrum. Biochem J 203:663–668Google Scholar
  14. Murrell JC, Dalton H (1983) Nitrogen fixation in obligate methanotrophs. J Gen Microbiol 129:3481–3486Google Scholar
  15. Nordlund S, Eriksson U (1979) Relation between ‘switch-off’ effect and the membrane component. Hydrogen production and acetylene reduction with different nitrogenase component ratios. Biochim Biophys Acta 547:429–437Google Scholar
  16. Nordlund S, Eriksson U, Baltscheffsky H (1977) Necessity of a membrane component for nitrogenase activity in Rhodospirillum rubrum. Biochim Biophys Acta 462:187–195Google Scholar
  17. Preston GG, Ludden PW (1982) Change in subunit composition of the iron protein of nitrogenase from Rhodospirillum rubrum during activation and inactivation of iron protein. Biochem J 205:489–494Google Scholar
  18. Stackebrandt E, Woese CR (1981) The evolution of prokaryotes. In: Carlile MJ, Collins JE, Moseley BEB (eds) Molecular and cellular aspects of microbial evolution. Cambridge University Press, Cambridge, pp 1–31Google Scholar
  19. Stewart WDP (1982) The fundamentals of nitrogen fixation. Cambridge University Press, CambridgeGoogle Scholar
  20. Weber K, Osborn M (1975) Proteins and sodium dodecyl sulfate: molecular weight determination on polyacrylamide gels and related procedures. In: Neurath H, Hill RT (eds) The proteins, vol I, 3rd edn. Academic Press, New York, pp 179–223Google Scholar
  21. Winter HC, Arnon DI (1970) The nitrogen fixation system of photosynthestic bacteria. I. Preparation and properties of a cell-free extract from Chromatium. Biochim Biophys Acta 197:170–179Google Scholar
  22. Yoch DC (1979) Manganese, an essential trace element for N2 fixation by Rhodospirillum rubrum and Rhodopseudomonas capsulata: role in nitrogenase regulation. J Bacteriol 140:987–995Google Scholar
  23. Yoch DC (1980) Regulation of nitrogenase A and R concentrations in Rhodopseudomonas capsulata by glutamine synthetase. Biochem J 187:273–276Google Scholar
  24. Yoch DC, Arnon DI (1970) The nitrogen fixation system of photosynthetic bacteria. II. Chromatium nitrogenase activity linked to photochemically generated assimilatory power. Biochim Biophys Acta 197:180–184Google Scholar
  25. Yoch DC, Cantu M (1980) Changes in the regulatory form of Rhodospirillum rubrum nitrogenase as influenced by nutritional and environmental factors. J Bacteriol 142:899–907Google Scholar

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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