Article Dans Une Revue Science Advances Année : 2025

Proteorhodopsin insights into the molecular mechanism of vectorial proton transport

Vitaly Polovinkin
Anatoly Mikhaylov
Siarhei Bukhalovich
Daria Kuklina
Tatyana Rokitskaya
Chavdar Stoev
Dmitrii Zabelskii
Andrey Rogachev
Valentin Borshchevskiy
Rohit Ghai
Gleb Bourenkov
Mahel Zeghouf
Jacqueline Cherfils
Martin Engelhard
  • Fonction : Auteur
Igor Chizhov
Francisco Rodriguez-Valera
Ernst Bamberg
Valentin Gordeliy

Résumé

Bacterial proton pumps, proteorhodopsins (PRs), are a major group of light-driven membrane proteins found in marine bacteria. They are functionally and structurally distinct from archaeal and eukaryotic proton pumps. To elucidate the proton transfer mechanism by PRs and understand the differences to nonbacterial pumps on a molecular level, high-resolution structures of PRs’ functional states are needed. In this work, we have determined atomic-resolution structures of MAR, a PR from marine actinobacteria, in various functional states, notably the challenging late O intermediate state. These data and information from recent atomic-resolution structures on an archaeal outward proton pump bacteriorhodopsin and bacterial inward proton pump xenorhodopsin allow for deducing key universal elements for light-driven proton pumping. First, long hydrogen-bonded chains characterize proton pathways. Second, short hydrogen bonds allow proton storage and inhibit their backflow. Last, the retinal Schiff base is the active proton donor and acceptor to and from hydrogen-bonded chains.

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Sergey Bukhdruker, Ivan Gushchin, Vitaly Shevchenko, Kirill Kovalev, Vitaly Polovinkin, et al.. Proteorhodopsin insights into the molecular mechanism of vectorial proton transport. Science Advances , 2025, 11 (16), ⟨10.1126/sciadv.adu5303⟩. ⟨hal-05168363⟩
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