Ammonia switch-off of nitrogenase from Rhodobacter sphaeroides and Methylosinus trichosporium: no evidence for Fe protein modification.
In vivo switch-off of nitrogenase activity by NH4+ is a reversible process in Rhodobacter sphaeroides and Methylosinus trichosporium OB3b. The same pattern of switch-off in Rhodospirillum rubrum is explained by ADP-ribosylation of one of the Fe protein subunits, however, no evidence of covalent modification could be found in the subunits from either R. sphaeroides or M. trichosporium. Fe protein subunits from these organisms showed no variant behaviour on SDS-PAGE, nor were they 32P-labeled following switch-off. These observations suggest either that the attachment of the modifying group to the Fe protein in these organisms is quite labile and does not survive in vitro manipulation, or that the mechanism of switch-off is different than that seen in Rhodospirillum.
D000244:Adenosine Diphosphate / Q000378:metabolism; D000641:Ammonia / Q000494:pharmacology*; D001345:Autoradiography; D004591:Electrophoresis, Polyacrylamide Gel; D007118:Immunoassay; D008772:Methylococcaceae / Q000187:drug effects / Q000201:enzymology* / Q000378:metabolism; D009591:Nitrogenase / Q000037:antagonists & inhibitors* / Q000378:metabolism*; D010088:Oxidoreductases; D012242:Rhodobacter sphaeroides / Q000187:drug effects / Q000201:enzymology* / Q000378:metabolism
D000244:Adenosine Diphosphate; D000641:Ammonia; D010088:Oxidoreductases; D009591:Nitrogenase; C029130:nitrogenase reductase