Proteorhodopsin insights into the molecular mechanism of vectorial proton transport

Bukhdruker, S.; Gushchin, I.; Shevchenko, V.; Kovalev, K.; Polovinkin, V.; Tsybrov, F.; Astashkin, R.; Alekseev, A.; Mikhaylov, A.; Bukhalovich, S.; Bratanov, D.; Ryzhykau, Y.; Kuklina, D.; Caramello, N.; Rokitskaya, T.; Antonenko, Y.; Rulev, M.; Stoev, C.; Zabelskii, D.; Round, E.; Rogachev, A.; Borshchevskiy, V.; Ghai, R.; Bourenkov, G.; Zeghouf, M.; Cherfils, J.; Engelhard, M.; Chizhov, I.; Rodriguez-Valera, F.; Bamberg, E.; Gordeliy, V.

Авторы: Bukhdruker Sergey, Gushchin Ivan, Shevchenko Vitaly, Kovalev Kirill, Polovinkin Vitaly, Tsybrov Fedor, Astashkin Roman, Alekseev Alexey, Mikhaylov Anatoly, Bukhalovich Siarhei, Bratanov Dmitry, Ryzhykau Yury, Kuklina Daria, Caramello Nicolas, Rokitskaya Tatyana, Antonenko Yuri, Rulev Maksim, Stoev Chavdar, Zabelskii Dmitrii, Round Ekaterina, Rogachev Andrey, Borshchevskiy Valentin, Ghai Rohit, Bourenkov Gleb, Zeghouf Mahel, Cherfils Jacqueline, Engelhard Martin, Chizhov Igor, Rodriguez-Valera Francisco, Bamberg Ernst, Gordeliy Valentin
Журнал: Science Advances
Том: 11
Номер: 16
Год издания: 2025
DOI: 10.1126/sciadv.adu5303
Аннотация: 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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