Regulation of nitrogenase activity by covalent modification in Chromatium vinosum |
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Authors: | John W. Gotto Duane C. Yoch |
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Affiliation: | (1) Department of Biology, University of South Carolina, 29208 Columbia, SC, USA |
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Abstract: | Nitrogenase in Chromatium vinosum was rapidly, but reversibly inhibited by NH4+. 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.Abbreviation HEPES N-2-hydroxyethyl piperazine-N-2-ethanesulfonic acid |
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Keywords: | Nitrogenase Nitrogen fixation Regulation Photosynthetic bacteria Chromatium Ammonia switch off |
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