Early studies in which nitrogenase was freeze-trapped during enzymatic turnover revealed the presence of high-spin (S = 3/2) electron paramagnetic resonance (EPR) signals from the active-site FeMo-cofactor (FeMo-co) in electron-reduced intermediates of the MoFe protein. Historically denoted as 1b and 1c, each of the signals is describable as a fictitious spin system, S' = 1/2, with anisotropic g' tensor, 1b with g' = [4.21, 3.76, ?] and 1c with g' = [4.69,similar to 3.20, ?]. A clear discrepancy between the magnetic properties of lb and 1c and the kinetic analysis of their appearance during pre-steady-state turnover left their identities in doubt, however. We subsequently associated lb with the state having accumulated 2[e(-)/H+], denoted as E-2(2H), and suggested that the reducing equivalents are stored on the catalytic FeMo-co cluster as an iron hydride, likely an [Fe-H-Fe] hydride bridge. Intra-EPR cavity photolysis (450 nm; temperature- independent from 4 to 12 K) of the E-2(2H)/1b state now corroborates the identification of this state as storing two reducing equivalents as a hydride. Photolysis converts E-2(2H)/1b to a state with the same EPR spectrum, and thus the same cofactor structure as pre-steady-state turnover 1c, but with a different active-site environment. Upon annealing of the photogenerated state at temperature T = 145 K, it relaxes back to E-2(2H)/lb. This implies that the 1c signal comes from an E-2(2H) hydride isomer of E-2(2H)/1b that stores its two reducing equivalents either as a hydride bridge between a different pair of iron atoms or an Fe-H terminal hydride.