What do experimentally measured kinetic isotope effects (KIEs) tell us about H-abstraction reactions with multispinstate reactivity options? Using DFT calculations with tunneling corrections for experimentally studied H-abstraction reactions of porphyrin-Compound II species (Chem.-Eur. J. 2014, 20, 14437; Angew. Chem., Int. Ed. 2008, 47, 7321) with cyclohexane, dihydroanthracene (DHA), and xanthene (Xan), we show here that KIE is a selective probe that identifies the experimentally reactive spin state. At the same time, comparison of calculated and experimental KIE values permits us to determine the structural orientation of the transition states, as well as the presence/absence of an axial ligand, and the effect of porphyrin substituents. The studied compound II (Cpd II) species involve porphine, and porphyrin ligands with different meso-substituents, TPFPP (tetrakis(pentafluorophenyl)porphyrin dianion) and TMP (tetramesitylporphyrin dianion), with and without imidazole axial ligands. The DFT calculations reveal three potential pathways: quintet and triplet alpha-pathways (H-5 sigma and H-3 sigma) that possess linear transition state (TS) structures, and a triplet pi-pathway (H-3 pi) having a bent TS structure. Without an axial ligand; the H-5 sigma pathways for these Cpd II complexes cross below the triplet states. The axial ligand raises the barriers for the quintet and triplet 6-pathways and quenches any chances for two-state reactivity, thus proceeding via the H-3 sigma pathway. All of these pathways exhibit characteristic KIE values: very large for H-3 pi (48-200), small for H-3 sigma (3-9), and intermediate for H-3 sigma (23-51). The calculated KIEs for (TPFPP)Fe-IV=O without an axial ligand reveal that H-3 sigma is the only pathway having a KIE that matches the experimental valises, for the reactions with DHA and Xan (Angew. Chem., Int. Ed. 2008, 47, 7321). Indeed, theory shows that tunneling significantly lowers the H-3 sigma barrier rendering it the sole reactive state for the reaction. A prediction is made for the reactivity and KIE of (TMP)Fe-IV=0 complex, and a comparison is made with the analogous nonheme complexes.