In vitro activation of inactive nitrogenase component I with molybdate.
When Azotobacter vinelandii was derepressed for nitrogenase synthesis in the presence of WO42- rather than MoO42-, it synthesized active component II and inactive component I of nitrogenase. This inactive component I could be activated in vitro with the iron-molybdenum cofactor or with MoO42-. The latter reaction required adenosine 5'-triphosphate and was inhibited by adenosine 5'-diphosphate. FeMo cofactor and MoO42- produced different levels of activation, but there was no evidence that they acted upon different species of demolybdo component I. Rather, it may be that an additional factor necessary for MoO42-mediated activation but not for FeMo cofactor-mediated activation was limiting. Mo was inserted into component I during both FeMo cofactor- and MoO42- mediated activations.
D000255:Adenosine Triphosphate / Q000494:pharmacology; D001395:Azotobacter / Q000201:enzymology*; D004789:Enzyme Activation; D007501:Iron / Q000494:pharmacology; D008982:Molybdenum / Q000378:metabolism / Q000494:pharmacology*; D008983:Molybdoferredoxin / Q000494:pharmacology*; D009591:Nitrogenase / Q000378:metabolism*; D014414:Tungsten / Q000378:metabolism / Q000494:pharmacology
D008983:Molybdoferredoxin; D008982:Molybdenum; D000255:Adenosine Triphosphate; D007501:Iron; D009591:Nitrogenase; D014414:Tungsten