Regulation of nitrogenase activity by covalent modification in Chromatium vinosum
- 1 February 1985
- journal article
- research article
- Published by Springer Nature in Archiv für Mikrobiologie
- Vol. 141 (1) , 40-43
- https://doi.org/10.1007/bf00446737
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.Keywords
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