The Fe(II)- and alpha-ketoglutarate (alpha KG)-dependent enzymes are a functionally and mechanistically diverse group of mononuclear nonheme-iron enzymes that activate dioxygen to couple the decarboxylation of alpha KG, which yields succinate and CO2, to the oxidation of an aliphatic C-H bond of their substrates. Their mechanisms have been studied in detail by a combination of kinetic, spectroscopic, and computational methods. Two reaction intermediates have been trapped and characterized for several members of this enzyme family. The first intermediate is the C-H-cleaving Fe(IV)-oxo complex, which exhibits a large deuterium kinetic isotope effect on its decay. The second intermediate is a Fe(II):product complex. Reaction intermediates proposed to occur before the Fe(IV)-oxo intermediate do not accumulate and therefore cannot be characterized experimentally. One of these intermediates is the initial O-2 adduct, which is a {FeO2}(8) species in the notation introduced by Enemark and Feltham. Here, we report spectroscopic and computational studies on the stable NO-adduct of taurine:alpha KG dioxygenase (TauD), termed TauD-{FeNO}(7), and its one-electron reduced form, TauD {FeNO}(8). The latter is isoelectronic with the proposed O-2 adduct and was generated by low-temperature gamma-irradiation of TauD-{FeNO}(7). To our knowledge, TauD-{FeNO}(8) is the first paramagnetic {FeNO}(8) complex. The detailed analysis of experimental and computational results shows that TauD-(FeNO}(8) has a triplet ground state. This has mechanistic implications that are discussed in this Article. Annealing of the triplet {FeNO}(8) species presumably leads to an equally elusive {FeHNO}(8) complex with a quintet ground state.