The hemocyanin protein binds and transports molecular oxygen via two copper atoms at its core. The singlet state of the \({{\rm{Cu}}}_{2}{{\rm{O}}}_{2}\) 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 \({{\rm{Cu}}}_{2}{{\rm{O}}}_{2}\) 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.

血色素蛋白通过其核心的两个铜原子结合并转运分子氧。的单重态\（{{\ RM {的Cu}}} _ {2} {{\ RM {ö}}} _ {2} \）芯被认为是由一个超交换途径来稳定，但在原位详述电子基态的多参考特征使计算分析变得复杂。在这里，使用一种新颖的方法研究血蓝蛋白功能位点的电子相关效应，并用簇动力学平均场理论处理局部3d铜电子。这使我们能够考虑动力学和多参考量子力学，捕获3d电子的化合价和自旋涨落。我们的方法解释了实验观察到的双铜单峰的稳定\（{{\ rm {Cu}}} _ {2} {{\ rm {O}}} _ {2} \）核，在氧桥上具有局部电荷和不相干的散射过程，可防止长寿命电荷激发。这表明血蓝蛋白的磁性结构在很大程度上受到多体校正的影响。