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For the cofactor-free 1-H-3-hydroxy-4-oxoquinaldine-2,4-dioxygenase (HOD),the dioxygen (O2) dependent steps are rate-limiting along with a spin statecrossover to the singlet spin state. Here, the primary triplet O2 moleculeactivation on the 2-methyl-3-hydroxy-4(1H)-quinolone (MHQ) is investigated, andthe catalytic role of the intersystem crossing effects is highlighted bydirectly comparing results from the Born-Oppenheimer dynamics and non-adiabaticsurface hopping dynamics. This work confirms non-adiabatic dynamical effectsare essential to modulate the O2 activation on the substrate MHQ. The timescale of the equilibration and conversion from triplet to singlet state shouldbe in the range of a few hundreds of femtoseconds. We hope this work providesus a fresh look at the underlying physics of dioxygen activation reactionsinvolving more than one spin state.

Understanding the Spin Crossover Dynamical Effects of the Dioxygen Binding and Activation on HOD enzyme