We have studied both the atomic and electronic structures of nitrogenase Mo-Fe proteins using EXAFS and L-edge spectroscopy. The Mo and Fe K-edge EXAFS data show not only 2.37, 2.70, 2.29, and 2.63 Å first shell Mo-S, Mo-Fe, Fe-S, and Fe-Fe distances, but also 3.8, 4.3 and 5.1 Å second shell Fe-Fe, Fe-S, and Mo-Fe interactions. These observed distances are consistent with recent crystallographic models for the M-center. The average Mcenter distances have been defined with unprecedented accuracy. The nitrogenase Fe L-edge spectra have been obtained for the first time, and the result suggests that the Fe exists in both Fe2+ and Fe3+ states.