Redox-Dependent Vibrational Energy Flow in Amicyanin Revealed by Molecular Dynamics Simulations

interface reveals coherent interprotein coupling mediated by both residue-residue interactions and dynamically structured interfacial water. Hydrogen-bond lifetime analysis demonstrates that interfacial water exhibits confined, heterogeneous dynamics characteristic of protein-protein interfaces, providing a dynamical bottleneck that supports energy redistribution across the complex. Together, these results demonstrate that amicyanin employs a robust, preorganized vibrational communication network conserved under redox cycling, offering a mechanistic framework for reliable long-range dynamical coupling between local redox chemistry and global protein response.