True-atomic-resolution insights into the structure and functional role of linear chains and low-barrier hydrogen bonds in proteins

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Borshchevskiy, Valentin | Kovalev, Kirill | Round, Ekaterina | Efremov, Rouslan | Astashkin, Roman | Bourenkov, Gleb | Bratanov, Dmitry | Balandin, Taras | Chizhov, Igor | Baeken, Christian | Gushchin, Ivan | Kuzmin, Alexander | Alekseev, Alexey | Rogachev, Andrey | Willbold, Dieter | Engelhard, Martin | Bamberg, Ernst | Büldt, Georg | Gordeliy, Valentin

Edité par CCSD ; Nature Publishing Group -

International audience. Hydrogen bonds are fundamental to the structure and function of biological macromolecules and have been explored in detail. The chains of hydrogen bonds (CHBs) and low-barrier hydrogen bonds (LBHBs) were proposed to play essential roles in enzyme catalysis and proton transport. However, high-resolution structural data from CHBs and LBHBs is limited. The challenge is that their 'visualization' requires ultrahigh-resolution structures of the ground and functionally important intermediate states to identify proton translocation events and perform their structural assignment. Our true-atomic-resolution structures of the light-driven proton pump bacteriorhodopsin, a model in studies of proton transport, show that CHBs and LBHBs not only serve as proton pathways, but also are indispensable for long-range communications, signaling and proton storage in proteins. The complete picture of CHBs and LBHBs discloses their multifunctional roles in providing protein functions and presents a consistent picture of proton transport and storage resolving long-standing debates and controversies.

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