Capturing structural changes of the S1 to S2 transition of photosystem II using time-resolved serial femtosecond crystallography
Photosystem II (PSII) catalyzes light-induced water oxidation through an Si-state cycle, leading to the generation of di-oxygen, protons and electrons. Pump–probe time-resolved serial femtosecond crystallography (TR-SFX) has been used to capture structural dynamics of light-sensitive proteins. In th...
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| Format: | Article |
| Language: | English |
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International Union of Crystallography
2021-05-01
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| Series: | IUCrJ |
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| Online Access: | http://scripts.iucr.org/cgi-bin/paper?S2052252521002177 |
| _version_ | 1828893576233222144 |
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| author | Hongjie Li Yoshiki Nakajima Takashi Nomura Michihiro Sugahara Shinichiro Yonekura Siu Kit Chan Takanori Nakane Takahiro Yamane Yasufumi Umena Mamoru Suzuki Tetsuya Masuda Taiki Motomura Hisashi Naitow Yoshinori Matsuura Tetsunari Kimura Kensuke Tono Shigeki Owada Yasumasa Joti Rie Tanaka Eriko Nango Fusamichi Akita Minoru Kubo So Iwata Jian-Ren Shen Michihiro Suga |
| author_facet | Hongjie Li Yoshiki Nakajima Takashi Nomura Michihiro Sugahara Shinichiro Yonekura Siu Kit Chan Takanori Nakane Takahiro Yamane Yasufumi Umena Mamoru Suzuki Tetsuya Masuda Taiki Motomura Hisashi Naitow Yoshinori Matsuura Tetsunari Kimura Kensuke Tono Shigeki Owada Yasumasa Joti Rie Tanaka Eriko Nango Fusamichi Akita Minoru Kubo So Iwata Jian-Ren Shen Michihiro Suga |
| author_sort | Hongjie Li |
| collection | DOAJ |
| description | Photosystem II (PSII) catalyzes light-induced water oxidation through an Si-state cycle, leading to the generation of di-oxygen, protons and electrons. Pump–probe time-resolved serial femtosecond crystallography (TR-SFX) has been used to capture structural dynamics of light-sensitive proteins. In this approach, it is crucial to avoid light contamination in the samples when analyzing a particular reaction intermediate. Here, a method for determining a condition that avoids light contamination of the PSII microcrystals while minimizing sample consumption in TR-SFX is described. By swapping the pump and probe pulses with a very short delay between them, the structural changes that occur during the S1-to-S2 transition were examined and a boundary of the excitation region was accurately determined. With the sample flow rate and concomitant illumination conditions determined, the S2-state structure of PSII could be analyzed at room temperature, revealing the structural changes that occur during the S1-to-S2 transition at ambient temperature. Though the structure of the manganese cluster was similar to previous studies, the behaviors of the water molecules in the two channels (O1 and O4 channels) were found to be different. By comparing with the previous studies performed at low temperature or with a different delay time, the possible channels for water inlet and structural changes important for the water-splitting reaction were revealed. |
| first_indexed | 2024-12-13T13:55:39Z |
| format | Article |
| id | doaj.art-35188f25a618474b8a4bc94e01f925d7 |
| institution | Directory Open Access Journal |
| issn | 2052-2525 |
| language | English |
| last_indexed | 2024-12-13T13:55:39Z |
| publishDate | 2021-05-01 |
| publisher | International Union of Crystallography |
| record_format | Article |
| series | IUCrJ |
| spelling | doaj.art-35188f25a618474b8a4bc94e01f925d72022-12-21T23:42:54ZengInternational Union of CrystallographyIUCrJ2052-25252021-05-018343144310.1107/S2052252521002177zf5015Capturing structural changes of the S1 to S2 transition of photosystem II using time-resolved serial femtosecond crystallographyHongjie Li0Yoshiki Nakajima1Takashi Nomura2Michihiro Sugahara3Shinichiro Yonekura4Siu Kit Chan5Takanori Nakane6Takahiro Yamane7Yasufumi Umena8Mamoru Suzuki9Tetsuya Masuda10Taiki Motomura11Hisashi Naitow12Yoshinori Matsuura13Tetsunari Kimura14Kensuke Tono15Shigeki Owada16Yasumasa Joti17Rie Tanaka18Eriko Nango19Fusamichi Akita20Minoru Kubo21So Iwata22Jian-Ren Shen23Michihiro Suga24Research Institute for Interdisciplinary Science and Graduate School of Natural Science and Technology, Okayama University, 3-1-1 Tsushima-naka, Kitaku, Okayama, Okayama 700-8530, JapanResearch Institute for Interdisciplinary Science and Graduate School of Natural Science and Technology, Okayama University, 3-1-1 Tsushima-naka, Kitaku, Okayama, Okayama 700-8530, JapanGraduate School of Life Science, University of Hyogo, 3-2-1 Kouto, Kamigori-cho, Ako-gun, Hyogo 678-1297, JapanRIKEN SPring-8 Center, 1-1-1 Kouto, Sayo-cho, Sayo-gun, Hyogo 679-5148, JapanResearch Institute for Interdisciplinary Science and Graduate School of Natural Science and Technology, Okayama University, 3-1-1 Tsushima-naka, Kitaku, Okayama, Okayama 700-8530, JapanResearch Institute for Interdisciplinary Science and Graduate School of Natural Science and Technology, Okayama University, 3-1-1 Tsushima-naka, Kitaku, Okayama, Okayama 700-8530, JapanDepartment of Biological Science, Graduate School of Science, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, JapanResearch Institute for Interdisciplinary Science and Graduate School of Natural Science and Technology, Okayama University, 3-1-1 Tsushima-naka, Kitaku, Okayama, Okayama 700-8530, JapanResearch Institute for Interdisciplinary Science and Graduate School of Natural Science and Technology, Okayama University, 3-1-1 Tsushima-naka, Kitaku, Okayama, Okayama 700-8530, JapanInstitute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka 565-0871, JapanDivision of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Gokasho, Uji, Kyoto 611-0011, JapanResearch Institute for Interdisciplinary Science and Graduate School of Natural Science and Technology, Okayama University, 3-1-1 Tsushima-naka, Kitaku, Okayama, Okayama 700-8530, JapanRIKEN SPring-8 Center, 1-1-1 Kouto, Sayo-cho, Sayo-gun, Hyogo 679-5148, JapanRIKEN SPring-8 Center, 1-1-1 Kouto, Sayo-cho, Sayo-gun, Hyogo 679-5148, JapanDepartment of Chemistry, Graduate School of Science, Kobe University, -1 Rokkodai, Nada-ku, Kobe 657-8501, JapanRIKEN SPring-8 Center, 1-1-1 Kouto, Sayo-cho, Sayo-gun, Hyogo 679-5148, JapanRIKEN SPring-8 Center, 1-1-1 Kouto, Sayo-cho, Sayo-gun, Hyogo 679-5148, JapanRIKEN SPring-8 Center, 1-1-1 Kouto, Sayo-cho, Sayo-gun, Hyogo 679-5148, JapanRIKEN SPring-8 Center, 1-1-1 Kouto, Sayo-cho, Sayo-gun, Hyogo 679-5148, JapanRIKEN SPring-8 Center, 1-1-1 Kouto, Sayo-cho, Sayo-gun, Hyogo 679-5148, JapanResearch Institute for Interdisciplinary Science and Graduate School of Natural Science and Technology, Okayama University, 3-1-1 Tsushima-naka, Kitaku, Okayama, Okayama 700-8530, JapanGraduate School of Life Science, University of Hyogo, 3-2-1 Kouto, Kamigori-cho, Ako-gun, Hyogo 678-1297, JapanRIKEN SPring-8 Center, 1-1-1 Kouto, Sayo-cho, Sayo-gun, Hyogo 679-5148, JapanResearch Institute for Interdisciplinary Science and Graduate School of Natural Science and Technology, Okayama University, 3-1-1 Tsushima-naka, Kitaku, Okayama, Okayama 700-8530, JapanResearch Institute for Interdisciplinary Science and Graduate School of Natural Science and Technology, Okayama University, 3-1-1 Tsushima-naka, Kitaku, Okayama, Okayama 700-8530, JapanPhotosystem II (PSII) catalyzes light-induced water oxidation through an Si-state cycle, leading to the generation of di-oxygen, protons and electrons. Pump–probe time-resolved serial femtosecond crystallography (TR-SFX) has been used to capture structural dynamics of light-sensitive proteins. In this approach, it is crucial to avoid light contamination in the samples when analyzing a particular reaction intermediate. Here, a method for determining a condition that avoids light contamination of the PSII microcrystals while minimizing sample consumption in TR-SFX is described. By swapping the pump and probe pulses with a very short delay between them, the structural changes that occur during the S1-to-S2 transition were examined and a boundary of the excitation region was accurately determined. With the sample flow rate and concomitant illumination conditions determined, the S2-state structure of PSII could be analyzed at room temperature, revealing the structural changes that occur during the S1-to-S2 transition at ambient temperature. Though the structure of the manganese cluster was similar to previous studies, the behaviors of the water molecules in the two channels (O1 and O4 channels) were found to be different. By comparing with the previous studies performed at low temperature or with a different delay time, the possible channels for water inlet and structural changes important for the water-splitting reaction were revealed.http://scripts.iucr.org/cgi-bin/paper?S2052252521002177time-resolved serial crystallographyx-ray free-electron lasersmembrane proteinsphotosystem iiserial crystallographymolecular moviesprotein structures |
| spellingShingle | Hongjie Li Yoshiki Nakajima Takashi Nomura Michihiro Sugahara Shinichiro Yonekura Siu Kit Chan Takanori Nakane Takahiro Yamane Yasufumi Umena Mamoru Suzuki Tetsuya Masuda Taiki Motomura Hisashi Naitow Yoshinori Matsuura Tetsunari Kimura Kensuke Tono Shigeki Owada Yasumasa Joti Rie Tanaka Eriko Nango Fusamichi Akita Minoru Kubo So Iwata Jian-Ren Shen Michihiro Suga Capturing structural changes of the S1 to S2 transition of photosystem II using time-resolved serial femtosecond crystallography IUCrJ time-resolved serial crystallography x-ray free-electron lasers membrane proteins photosystem ii serial crystallography molecular movies protein structures |
| title | Capturing structural changes of the S1 to S2 transition of photosystem II using time-resolved serial femtosecond crystallography |
| title_full | Capturing structural changes of the S1 to S2 transition of photosystem II using time-resolved serial femtosecond crystallography |
| title_fullStr | Capturing structural changes of the S1 to S2 transition of photosystem II using time-resolved serial femtosecond crystallography |
| title_full_unstemmed | Capturing structural changes of the S1 to S2 transition of photosystem II using time-resolved serial femtosecond crystallography |
| title_short | Capturing structural changes of the S1 to S2 transition of photosystem II using time-resolved serial femtosecond crystallography |
| title_sort | capturing structural changes of the s1 to s2 transition of photosystem ii using time resolved serial femtosecond crystallography |
| topic | time-resolved serial crystallography x-ray free-electron lasers membrane proteins photosystem ii serial crystallography molecular movies protein structures |
| url | http://scripts.iucr.org/cgi-bin/paper?S2052252521002177 |
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