ISSN:
1432-072X
Keywords:
Nitrogenase
;
Nitrogen fixation
;
Regulation
;
Photosynthetic bacteria
;
Chromatium
;
Ammonia switch off
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
Notes:
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.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00446737
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