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Regulation of nitrogenase activity by covalent modification inChromatium vinosum

✍ Scribed by John W. Gotto; Duane C. Yoch

Book ID
104777837
Publisher
Springer
Year
1985
Tongue
English
Weight
520 KB
Volume
141
Category
Article
ISSN
0302-8933

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✦ Synopsis

Nitrogenase in Chromatium vinosum was rapidly, but reversibly inhibited by NH2. Activity of the Fe protin component of nitrogenase required both Mn 2 + 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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