Light-dependent degradation of nitrophenols by the phototrophic bacterium Rhodobacter capsulatus E1F1
Article Abstract:
Nitrophenol microaerobic photodegradation by the phototrophic bacterium Rhodobacter capsulatus with acetate as a carbon source was observed in this study. Growth of the bacterium showed a dependence on the nitrophenol concentration in the culture medium under microaerobic conditions. Photoreduction of 2,4-dinitrophenol (2,4-DNP) by the bacterium was controlled by factors such as dioxygen tension and light intensity. The reaction was also inhibited by ammonium and followed by the stoichiometric production of the nonmetabolizable 2-amino-4-nitrophenol (ANP).
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1992
User Contributions:
Comment about this article or add new information about this topic:
Halotolerance of the phototrophic bacterium Rhodobacter capsulatus E1F1 is dependent on the nitrogen source
Article Abstract:
In medium with oxidized nitrogen sources such as nitrate, increased salinity appears to inhibit growth of Rhodobacter capsulatus E1F1 by inhibiting nitrate uptake and reducing nitrogenase and nitrate reductase activities. Sources of reduced nitrogen, such as ammonium, allowed growth in the presence of up to 0.3 M NaCl. Glycine betaine also promoted tolerance to salinity. The use of ammonium by the glutamine synthetase-glutamate synthase pathway was not affected by NaCl.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1995
User Contributions:
Comment about this article or add new information about this topic:
Characterization of a nitrophenol reductase from the phototrophic bacterium Rhodobacter capsulatus E1F1
Article Abstract:
The enzyme responsible for the photoreduction of 2,4-DNP to 2-amino-4 nitrophenol in Rhodobacter capsulatus E1F1 is studied. The nitrophenol reductase activity is induced in the presence of nitrophenols and is repressed in ammonium grown cells. It is also purified to electrophoretic homogeneity. The molecular and regulatory properties of the enzyme are described.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1993
User Contributions:
Comment about this article or add new information about this topic:
- Abstracts: Limited degradation of chlorophenols by anaerobic sludge granules. Reductive dehalogenation of chlorophenol by Desulfomonile tiedjei DCB-1
- Abstracts: Anaerobic degradation of m-cresol by a sulfate-reducing bacterium. Methanogenic degradation of poly(3-hydroxyalkanoates)
- Abstracts: Sequential transhydroxylations converting hydroxyhydroquinone to phloroglucinol in the strictly anaerobic, fermentative bacterium Pelobacter massiliensis
- Abstracts: Ennoblement of stainless steel by the manganese-depositing bacterium Leptothrix discophora. Enzymatic iron oxidation by Leptothrix discophora: identification of an ironoxidizing protein
- Abstracts: Cloning, sequencing and expression in Escherichia coli of lcnB, a third bacteriocin determinant from the lactococcal bacteriocin plasmid p9B4-6