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

Research output: Contribution to journalArticle

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

Original languageEnglish
Article number4
JournalCommunications Physics
Volume3
Issue number1
Early online date13 Jan 2020
DOIs
Accepted/In press26 Nov 2019
E-pub ahead of print13 Jan 2020
Published1 Dec 2020

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Abstract

The hemocyanin protein binds and transports molecular oxygen via two copper atoms at its core. The singlet state of the Cu 2O 2 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 Cu 2O 2 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.

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