title: Spontaneous Nif- mutants of Rhodopseudomonas capsulata.
abstract: Revertible, spontaneous Nif- mutants of Rhodopseudomonas capsulata have been shown to accumulate in cultures growing photosynthetically with an amino acid as the nitrogen source such that H2 is maximally produced. The majority of such strains carry mutations which are clustered in a short region of the chromosome, probably representing one or two genes. Because this cluster includes temperature-sensitive mutations, it is also likely that it identifies the structural gene of a polypeptide. The phenotypic characterization of these spontaneous mutants showed (i) an inability to grow with N2 as the nitrogen source, no measurable nitrogenase activity, a reduction or absence of the three polypeptides of the MoFe and Fe proteins of the nitrogenase complex, a faster growth rate on glutamate as the nitrogen source under saturating light, and frequently a small increase in glutamine synthetase activity relative to that of the wild type when grown with glutamate as the nitrogen source. Alterations in other ammonium-assimilatory enzyme activities were not observed. Taken together, these properties suggest that the mutations have affected a regulatory protein necessary for nitrogen fixation.
mesh_terms: D050788:Alanine Dehydrogenase; D000594:Amino Acid Oxidoreductases / Q000378:metabolism; D005838:Genotype; D005969:Glutamate Dehydrogenase / Q000378:metabolism; D005970:Glutamate Synthase / Q000378:metabolism; D005974:Glutamate-Ammonia Ligase / Q000378:metabolism; D007700:Kinetics; D009154:Mutation; D009591:Nitrogenase / Q000378:metabolism; D010788:Photosynthesis; D012241:Rhodopseudomonas / Q000201:enzymology / Q000235:genetics*; D013045:Species Specificity
chemical_list: D009591:Nitrogenase; D000594:Amino Acid Oxidoreductases; D050788:Alanine Dehydrogenase; D005970:Glutamate Synthase; D005969:Glutamate Dehydrogenase; D005974:Glutamate-Ammonia Ligase