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Publikováno v:
Frontiers in Plant Science, Vol 14 (2023)
In photosystem II (PSII), the O3 and O4 sites of the Mn4CaO5 cluster form hydrogen bonds with D1-His337 and a water molecule (W539), respectively. The low-dose X-ray structure shows that these hydrogen bond distances differ between the two homogeneou
Externí odkaz:
https://doaj.org/article/5f74c5e9a9e341eb99fa41e1c9c8872d
Autor:
Yu Sugo, Hiroshi Ishikita
Publikováno v:
Frontiers in Plant Science, Vol 13 (2022)
Photo-induced charge separation, which is terminated by electron transfer from the primary quinone QA to the secondary quinone QB, provides the driving force for O2 evolution in photosystem II (PSII). However, the backward charge recombination using
Externí odkaz:
https://doaj.org/article/bd86a34b460c4ea4b81659f4b1e807cd
Autor:
Pablo Campomanes, Stefano Vanni
Publikováno v:
Molecules, Vol 26, Iss 7, p 2025 (2021)
The role and existence of low-barrier hydrogen bonds (LBHBs) in enzymatic and protein activity has been largely debated. An interesting case is that of the photoactive yellow protein (PYP). In this protein, two short HBs adjacent to the chromophore,
Externí odkaz:
https://doaj.org/article/5366ee870d3e4644b67b87fb83dbe995
Publikováno v:
Computational and Structural Biotechnology Journal, Vol 14, Iss C, Pp 16-19 (2016)
Photoactive yellow protein (PYP) has a characteristic hydrogen bond (H bond) between p-coumaric acid chromophore and Glu46, whose OH bond length has been observed to be 1.21 Å by the neutron diffraction technique [Proc. Natl. Acad. Sci. 106, 440–4
Externí odkaz:
https://doaj.org/article/384f61a959af48f8963dd8d7b3491033
Autor:
Jean-Louis Basdevant
Publikováno v:
Lectures on Quantum Mechanics ISBN: 9783031176340
Lectures on Quantum Mechanics ISBN: 9783319434780
Lectures on Quantum Mechanics ISBN: 9783319434780
The explanation of spectroscopic data was one of the first great victories of quantum theory. In modern science and technology, the mastery of atomic physics is responsible for decisive progress ranging from laser technology to the exploration of the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e793f9c73f57bb745c085bb26c3ad7d7
https://doi.org/10.1007/978-3-031-17635-7_12
https://doi.org/10.1007/978-3-031-17635-7_12
Publikováno v:
Biomolecules; Volume 12; Issue 10; Pages: 1346
To clarify the obscure hydrolysis mechanism of ubiquitous P-loop-fold nucleoside triphosphatases (Walker NTPases), we analysed the structures of 3136 catalytic sites with bound Mg-NTP complexes or their analogues. Our results are presented in two art
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::68f2555538e557ada1e2bb14d14e3b82
https://pubmed.ncbi.nlm.nih.gov/36291556
https://pubmed.ncbi.nlm.nih.gov/36291556
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America
Significance The crystal structures of photosynthetic reaction centers from purple bacteria (PbRCs) and photosystem II show large structural similarity. However, the proposed mechanisms of proton transfer toward the terminal electron acceptor quinone
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6962da588db63c4435dc578746f49419
https://doi.org/10.1073/pnas.2103203118
https://doi.org/10.1073/pnas.2103203118