Catalysis of exchange of terminal phosphate groups of ATP and ADP by purified nitrogenase proteins

摘要: A crude Azotobacter nitrogenase complex contained a highly active adenylate kinase which caused rapid equilibration of AMP, ADP, and ATP. Purified molybdenum–iron protein preparations also measurable activity could be removed by adsorption elution from hydroxylapatite. Independent kinase, the purified both Klebsiella pneumoniae chroococcum catalyzed exchange [32P]orthophosphate with terminal phosphate ATP or ADP. The labeling was stimulated ferricyanide ion due to inhibition hydrolysis linked substrate reductions cannot occur in absence reductant. This reaction is responsible for reported synthesis preparations.Binding labeled 32P group measured directly concentrated solutions K. column gel filtration ...