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April 2025
npj Imaging
Schaeper JJ, Tafforeau P, Kampshoff CA, Thomas C, Meyer A, Stadelmann C, Liberman MC, Moser T, Salditt T
April 2025
Frontiers in Cellular Neuroscience
Groshkova MB, Alvanos T, Qi Y, Wang F, Wichmann C, Hua Y, Moser T
April 2025
Beilstein Journals of Organic Chemistry
Tovtik R, Marzin D, Weigel P, Crespi S, Simeth NA
April 2025
BioRxiv
Kapoor R, Kim H, Garlick E, Lima MARBF, Ruhwedel T, Moebius W, Wolf F, Moser T
April 2025
EMBO Journal
Cretu C, Chernev A, Szabo CZK, Pena V, Urlaub H, Moser T, Preobraschenski J
April 2025
Science Advances
Preobraschenski J, Kreutzberger AJB, Ganzella M, Münster-Wandowski A, Kreutzberger MAB, Oolsthorn LHM, Seibert S, Kiessling V, Riedel D, Witkowska A, Ahnert-Hilger G, Tamm LK, Jahn R
April 2025
Molecular Psychiatry
Solomon P, Kaurani L, Budde M, Guiné JB, Krüger DM, Riquin K, Pena T, Burkhardt S, Fourgeux C, Adorjan K, Heilbronner M, Kalman JL, Kohshour MO, Papiol S, Reich-Erkelenz D, Schaupp SK, Schulte EC, Senner F, Vogl T, Anghelescu IG, Arolt V, Baune BT, Dannlowski U, Dietrich DE, Fallgatter AJ, Figge C, Juckel G, Konrad C, Reimer J, Reininghaus EZ, Schmauß M, Spitzer C, Wiltfang J, Zimmermann J, Schütz AL, Sananbenesi F, Sauvaget A, Falkai P, Schulze TG, Fischer A, Heilbronner U, Poschmann J
April 2025
BioRxiv
Gönenc II, Wolff A, Busley AV, Wieland A, Tijhuis A, Müller C, Wardenaar R, Argyriou L, Kaulfuß S, Räschle M, Spierings DCJ, Foijer F, Bastians H, Yigit G, Zibat A, Cyganek L, Wollnik B
April 2025
BioRxiv
Kim M, Matthes D, Frieg B, Leonov A, Ryazanov S, Bleher D,Grotegerd AK, Dienemann C, Giese A, Schröder GF, Becker S, Herfert K, de Groot BL, Andreas LB, Griesinger C
April 2025
Science Advances
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

Authors

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

Journal

Science Advances

Citation

Sci Adv. 2025 Apr 18;11(16):eadu5303.

Abstract

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.

DOI

10.1126/sciadv.adu5303
 
Pubmed Link

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