Inhibition of nitrogenase activity by metronidazole in rhodopseudomonas capsulata.
Inhibition of photosynthetic growth of Rhodopseudomonas capsulata by metronidazole was dependent on the nitrogen supply in culture solutions. Cultures fixing dinitrogen were more susceptible to inhibition by low concentrations than those supplied with NH4+. Light-dependent C2H2 reduction and H2 production by washed cells were inhibited by 80% and 60% respectively by 1 mM metronidazole. When this compound was first reduced with H2-palladised asbestos prior to assay, it only partially restricted C2H2 reduction in washed cells (33%) compared with unreduced inhibitor (68%). Metronidazole was without effect on other metabolic functions. Thus, even at 40 mM it did not inhibit either (a) dark or light respiration in cells grown under photo- and chemo-heterotrophic conditions; (b) H2-dependent photoreduction of 14CO2; (C) gamma-glutamyltransferase activity of glutamine synthetase in cell-free extracts (25 mM inhibitor). Metronidazole (1 mM) completely inhibited C2H2 reduction by washed cells of Azotobacter vinelandii. The dithionite-dependent C2H2 reduction of a partially purified nitrogenase was only partially inhibited (30%) by 1 mM metronidazole.
D001395:Azotobacter / Q000201:enzymology; D005974:Glutamate-Ammonia Ligase / Q000037:antagonists & inhibitors; D008795:Metronidazole / Q000494:pharmacology*; D009586:Nitrogen Fixation / Q000187:drug effects; D009591:Nitrogenase / Q000037:antagonists & inhibitors*; D010101:Oxygen Consumption / Q000187:drug effects; D010788:Photosynthesis / Q000187:drug effects; D012241:Rhodopseudomonas / Q000201:enzymology*
D008795:Metronidazole; D009591:Nitrogenase; D005974:Glutamate-Ammonia Ligase