Protein ligand migration mapped by nonequilibrium 2D-IR exchange spectroscopy
作者： J. Bredenbeck , J. Helbing , K. Nienhaus , G. U. Nienhaus , P. Hamm
关键词: Analytical chemistry 、 Protein ligand 、 Binding site 、 Docking (molecular) 、 Crystallography 、 Carbon monoxide 、 Ligand 、 Myoglobin 、 Two-dimensional nuclear magnetic resonance spectroscopy 、 Heme 、 Chemistry
摘要: 2D-IR exchange spectroscopy has been introduced recently to map chemical networks in equilibrium with subpicosecond time resolution. Here, we demonstrate the generalization of nonequilibrium systems and its application light-triggered migration ligands between different sites a protein. Within picoseconds after photodissociating laser pulse, carbon monoxide relocate from their binding site A at heme prosthetic group myoglobin primary docking B distal pocket. Multiple CO stretching bands are observed for ligand B, indicating that several distinct conformational substates myoglobin:ligand complex coexist solution. Exchange cross-peaks associated heme-bound photodissociated reveal substate connectivity physiological temperature.
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