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Biochemistry|April 16, 1996
Elucidation of a MgATP signal transduction pathway in the nitrogenase iron protein: formation of a conformation resembling the MgATP-bound state by protein engineeringM J Ryle, L C SeefeldtBiochemistry|July 15, 1997
Reduction of thiocyanate, cyanate, and carbon disulfide by nitrogenase: kinetic characterization and EPR spectroscopic analysisM E Rasche, L C SeefeldtThe Journal of Biological Chemistry|February 29, 2000
Hydrolysis of nucleoside triphosphates other than ATP by nitrogenaseM J Ryle, L C SeefeldtProtein Science : a Publication of the Protein Society|January 1, 1993
Increasing nitrogenase catalytic efficiency for MgATP by changing serine 16 of its Fe protein to threonine: use of Mn2+ to show interaction of serine 16 with Mg2+L C Seefeldt, L E MortensonJournal of Bacteriology|June 1, 1989
Cyanide inactivation of hydrogenase from Azotobacter vinelandiiL C Seefeldt, D J ArpBiochemistry|December 10, 1996
The [4Fe-4S] cluster domain of the nitrogenase iron protein facilitates conformational changes required for the cooperative binding of two nucleotidesM J Ryle, L C SeefeldtThe Journal of Biological Chemistry|December 15, 1987
Redox-dependent subunit dissociation of Azotobacter vinelandii hydrogenase in the presence of sodium dodecyl sulfateL C Seefeldt, D J ArpBiochimie|January 1, 1986
Purification to homogeneity of Azotobacter vinelandii hydrogenase: a nickel and iron containing alpha beta dimerL C Seefeldt, D J ArpThe Journal of Biological Chemistry|February 14, 1997
Evidence for electron transfer-dependent formation of a nitrogenase iron protein-molybdenum-iron protein tight complex. The role of aspartate 39W N Lanzilotta, K Fisher, L C SeefeldtBiochemistry|June 4, 1996
Evidence for electron transfer from the nitrogenase iron protein to the molybdenum-iron protein without MgATP hydrolysis: characterization of a tight protein-protein complexW N Lanzilotta, K Fisher, L C SeefeldtPageof 7