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Электронный каталог: Bukhdruker, S. - Proteorhodopsin Insights into the Molecular Mechanism of Vectorial Proton Transport
Bukhdruker, S. - Proteorhodopsin Insights into the Molecular Mechanism of Vectorial Proton Transport
Статья
Автор: Bukhdruker, S.
Science Advances: Proteorhodopsin Insights into the Molecular Mechanism of Vectorial Proton Transport
б.г.
ISBN отсутствует
Автор: Bukhdruker, S.
Science Advances: Proteorhodopsin Insights into the Molecular Mechanism of Vectorial Proton Transport
б.г.
ISBN отсутствует
На полку
Статья
Bukhdruker, S.
Proteorhodopsin Insights into the Molecular Mechanism of Vectorial Proton Transport / S.Bukhdruker, Yu.Ryzhykau, [a.o.]. – Text : electronic // Science Advances. – 2025. – Vol. 11, No. 16. – P. 5303. – URL: https://www.science.org/doi/epdf/10.1126/sciadv.adu5303. – Bibliogr.: 127.
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 mo- lecular 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 character- ize 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.
ОИЯИ = ОИЯИ (JINR)2025
Спец.(статьи,препринты) = 28.0 - Биология$
Спец.(статьи,препринты) = С 350 - Приложения методов ядерной физики в смежных областях
Бюллетени = 34/025
Bukhdruker, S.
Proteorhodopsin Insights into the Molecular Mechanism of Vectorial Proton Transport / S.Bukhdruker, Yu.Ryzhykau, [a.o.]. – Text : electronic // Science Advances. – 2025. – Vol. 11, No. 16. – P. 5303. – URL: https://www.science.org/doi/epdf/10.1126/sciadv.adu5303. – Bibliogr.: 127.
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 mo- lecular 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 character- ize 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.
ОИЯИ = ОИЯИ (JINR)2025
Спец.(статьи,препринты) = 28.0 - Биология$
Спец.(статьи,препринты) = С 350 - Приложения методов ядерной физики в смежных областях
Бюллетени = 34/025
