ADP-ribosylation of dinitrogenase reductase from Clostridium pasteurianum prevents its inhibition of nitrogenase from Azotobacter vinelandii.
The effect of ADP-ribosylation of dinitrogenase reductase on its binding to dinitrogenase was investigated. Dinitrogenase reductase from Clostridium pasteurianum (Cp2) was a substrate for the ADP-ribosyltransferase and the dinitrogenase-reductase-activating glycohydrolase from Rhodospirillum rubrum. ADP-ribosylation inactivated Cp2 and prevented its formation of a tight complex with dinitrogenase from Azotobacter vinelandii (Av1). The complex between Cp2 and Av1 could not be ADP-ribosylated once it formed.
D000246:Adenosine Diphosphate Ribose / Q000378:metabolism*; D001395:Azotobacter / Q000201:enzymology*; D003013:Clostridium / Q000201:enzymology*; D017037:Dinitrogenase Reductase; D004591:Electrophoresis, Polyacrylamide Gel; D005288:Ferredoxins / Q000378:metabolism*; D007527:Isoenzymes / Q000378:metabolism; D046911:Macromolecular Substances; D009591:Nitrogenase / Q000037:antagonists & inhibitors*; D011485:Protein Binding
D017037:Dinitrogenase Reductase; D005288:Ferredoxins; D007527:Isoenzymes; D046911:Macromolecular Substances; D000246:Adenosine Diphosphate Ribose; D009591:Nitrogenase