Regulation of nitrogenase synthesis by oxygen in Klebsiella pneumoniae.
Klebsiella pneumoniae does not fix N(2) under aerobic conditions. The two protein components required for nitrogenase activity were studied during aeration of cells in nitrogen-free media. Component II of nitrogenase was inactivated more slowly in vivo than component I during aeration. The rate of loss of component II was less than the rate of component II synthesis during derepression. No inactive components were detected in cells that had been growing on NH(4) (+) and then aerated in nitrogen-free medium. This supports the hypothesis that O(2) somehow represses the formation of nitrogenase.
D000332:Aerobiosis; D000693:Anaerobiosis; D002474:Cell-Free System; D002701:Chloramphenicol / Q000494:pharmacology; D003470:Culture Media; D004794:Enzyme Repression; D006845:Hydrocarbons, Fluorinated / Q000494:pharmacology; D007122:Immunoelectrophoresis; D007711:Klebsiella pneumoniae / Q000201:enzymology* / Q000378:metabolism; D009586:Nitrogen Fixation; D009591:Nitrogenase / Q000096:biosynthesis* / Q000378:metabolism; D010100:Oxygen; D000644:Quaternary Ammonium Compounds / Q000378:metabolism; D012694:Serine / Q000378:metabolism
D003470:Culture Media; D006845:Hydrocarbons, Fluorinated; D000644:Quaternary Ammonium Compounds; D012694:Serine; D002701:Chloramphenicol; D009591:Nitrogenase; D010100:Oxygen