Superexchange mechanism and quantum many body excitations in the archetypal di-Cu oxo-bridge

The hemocyanin protein binds and transports molecular oxygen via two copper atoms at its core. The singlet state of the Cu2O2 core is thought to be stabilised by a superexchange pathway, but detailed in situ computational analysis is complicated by the multi-reference character of the electronic ground state. Here, electronic correlation effects in the functional site of hemocyanin are investigated using a novel approach, treating the localised copper 3d electrons with cluster dynamical mean field theory. This enables us to account for dynamical and multi-reference quantum mechanics, capturing valence and spin fluctuations of the 3d electrons. Our approach explains the stabilisation of the experimentally observed di-Cu singlet for the butterflied Cu2O2 core, with localised charge and incoherent scattering processes across the oxo-bridge that prevent long-lived charge excitations. This suggests that the magnetic structure of hemocyanin is largely influenced by the many-body corrections.


Published in:
Communications Physics, 3, 1, 4
Year:
Jan 13 2020
Publisher:
London, NATURE PUBLISHING GROUP
ISSN:
2399-3650
Keywords:
Laboratories:


Note: The status of this file is: Anyone


 Record created 2020-03-03, last modified 2020-04-20

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