Protection of nitrogenase in Azotobacter vinelandii.
The site or sites that protect nitrogenase from O(2) inactivation in vivo are sensitive to sodium azide or 2,4-dinitrophenol. Both components of nitrogenase can be synthesized when oxidative phosphorylation is disrupted.
D000085:Acetates; D000388:Air; D000693:Anaerobiosis; D001386:Azides / Q000494:pharmacology; D001395:Azotobacter / Q000201:enzymology* / Q000254:growth & development / Q000378:metabolism; D002701:Chloramphenicol / Q000494:pharmacology; D003470:Culture Media; D004140:Dinitrophenols / Q000494:pharmacology; D006371:Helium; D009154:Mutation; D009584:Nitrogen; D010085:Oxidative Phosphorylation; D010088:Oxidoreductases / Q000096:biosynthesis / Q000378:metabolism*; D000644:Quaternary Ammonium Compounds / Q000378:metabolism
D000085:Acetates; D001386:Azides; D003470:Culture Media; D004140:Dinitrophenols; D000644:Quaternary Ammonium Compounds; D006371:Helium; D002701:Chloramphenicol; D010088:Oxidoreductases; D009584:Nitrogen