A novel S = 3/2 EPR signal associated with native Fe-proteins of nitrogenase

Abstract

In addition to their g = 1.94 EPR signal, nitrogenase Fe-proteins from Azotobacter vinelandii, Azotobacter chroococcum and Klebsiella pneumoniae exhibit a weak EPR signal with g [congruent with]5. Temperature dependence of the signal was consistent with an S = 3/2 system with negative zero-field splitting, d = -5 +/- 0.7 cm-1. The ms, = +/- 3/2 ground state doublet gives rise to a transition with geff = 5.90 and the transition within the excited ms = +/- 1/2 doublet has a split geff = 4.8, 3.4. Quantitation gave 0.6 to 0.8 spin mol-1 which summed with the spin intensity of the S = 1/2 G = 1.94 line to roughly 1 spin/mol. MgATP and MgADP decreased the intensity of the s = 3/2 signal with no concomitant changes in intensity of the s = 1/2 signal.