Solubilization of the iron molybdenum cofactor of Azotobacter vinelandii nitrogenase in dimethylformamide and acetonitrile.
The iron molybdenum cofactor of Azotobacter vinelandii nitrogenase has been solubilized for the first time in dimethylformamide and acetonitrile. These solutions have the ability to reconstitute the inactive nitrogenase of the UW 45 mutant of A. vinelandii and exhibit an S = 3/2 EPR signal similar to that for the cofactor in N-methylformamide. Our ability to obtain solutions of FeMoco in these solvents seemingly refutes a previous hypothesis concerning the necessity of solvents with a dissociable proton for iron molybdenum cofactor solubility and should facilitate the spectroscopic characterization of this important species.
D000097:Acetonitriles; D001395:Azotobacter / Q000201:enzymology*; D004126:Dimethylformamide; D004578:Electron Spin Resonance Spectroscopy; D005288:Ferredoxins / Q000378:metabolism*; D008983:Molybdoferredoxin / Q000378:metabolism*; D009591:Nitrogenase / Q000378:metabolism*; D011489:Protein Denaturation; D012995:Solubility
D000097:Acetonitriles; D005288:Ferredoxins; D008983:Molybdoferredoxin; D004126:Dimethylformamide; D009591:Nitrogenase; C032159:acetonitrile