Quantum effects in CH activation with [CuO] complexes.

We investigate the mechanism of primary alkane CH bond activation with dioxo-dicopper ([CuO]) complexes, which serve as model catalysts for enzymes capable of activating CH bonds under mild conditions. As large H/D kinetic isotope effects (KIEs) are observed in enzymes and their synthetic mimics, we employ density functional theory along with variational transition-state theory with multidimensional tunneling to estimate reaction rate coefficients. By systematically varying ligand electrophilicity and substrate chain length, we examine trends in rate coefficients and kinetic isotope effects for the two proposed CH activation pathways - one-step oxo-insertion and two-step radical recombination. Although larger tunneling transmission coefficients are obtained for the radical pathway, the oxo-insertion mechanism yields higher rate coefficients on account of lower activation barriers. The question of the preferred CH activation mechanism, however, remains open: excellent agreement is observed between the predicted and known experimental KIE results for the radical pathway, while calculated Hammett slopes for the oxo-insertion pathway closely mirror experiments.