Super-exchange mechanism and quantum many body excitations in the archetypal hemocyanin/tyrosinase di-Cu oxo-bridge

Mohamed Ali al-Badri, Edward Linscott, Antoine Georges, Daniel J. Cole, and Cedric Weber

Dec 04, 2018

Received Date: 19th November 18

We perform first-principles quantum mechanical studies of dioxygen ligand binding to the hemocyanin protein.Electronic correlation effects in the functional site of hemocyanin are investigated using a state-of-the-art approach, treating the localized copper 3d electrons with cluster dynamical mean field theory (DMFT) for the first time.This approach has enabled us to account for dynamical and multi-reference quantum mechanics, capturing valence and spin fluctuations of the 3d electrons. Our approach predicts the stabilization of a quantum entangled di-Cu singlet in the London-Heitler limit, with localized charge andincoherent scattering processes across the oxo-bridge, that prevent long-lived charge excitations. This suggests that the magnetic structureof hemocyanin is largely influenced by the many-body corrections. Our computational model is supported by remarkable agreement with experimental optical absorption data,and provides a revised understanding of the bonding of the peroxide to the di-Cu system.

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