Toward Elucidation of the Photosynthetic Electron Transfer Mechanism
Ferredoxins (Fds) are iron–sulfur proteins found in various organisms, and they act as multifunctional electron carriers in diverse redox systems. In plants, numerous Fd-dependent enzymes such as dark-operative protochlorophyllide reductase (DPOR), glutamate synthase (Fd-GOGAT), sulfite reductase (S...
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Veröffentlicht in: | Journal of the Physical Society of Japan 2022-09, Vol.91 (9), p.1 |
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description | Ferredoxins (Fds) are iron–sulfur proteins found in various organisms, and they act as multifunctional electron carriers in diverse redox systems. In plants, numerous Fd-dependent enzymes such as dark-operative protochlorophyllide reductase (DPOR), glutamate synthase (Fd-GOGAT), sulfite reductase (SiR), FTR (ferredoxin-thioredoxin reductase), and ferredoxin:NADP+ reductase (FNR) exist. However, there are no consensus sequences for Fd dependence, which is why we are interested in the molecular interaction between Fd and Fd-interacting proteins, including Photosystem I. The efficient electron transfer and backflow prevention mechanisms by Fd are also very interesting. Ultrahigh-resolution X-ray structure analysis by low-dose data collection will greatly advance our understanding of the electron transfer mechanism by Fd. |
doi_str_mv | 10.7566/JPSJ.91.091002 |
format | Article |
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In plants, numerous Fd-dependent enzymes such as dark-operative protochlorophyllide reductase (DPOR), glutamate synthase (Fd-GOGAT), sulfite reductase (SiR), FTR (ferredoxin-thioredoxin reductase), and ferredoxin:NADP+ reductase (FNR) exist. However, there are no consensus sequences for Fd dependence, which is why we are interested in the molecular interaction between Fd and Fd-interacting proteins, including Photosystem I. The efficient electron transfer and backflow prevention mechanisms by Fd are also very interesting. Ultrahigh-resolution X-ray structure analysis by low-dose data collection will greatly advance our understanding of the electron transfer mechanism by Fd.</description><identifier>ISSN: 0031-9015</identifier><identifier>EISSN: 1347-4073</identifier><identifier>DOI: 10.7566/JPSJ.91.091002</identifier><language>eng</language><publisher>Tokyo: The Physical Society of Japan</publisher><subject>Electron transfer ; Molecular interactions ; Photosynthesis ; Proteins ; Reductases ; Structural analysis</subject><ispartof>Journal of the Physical Society of Japan, 2022-09, Vol.91 (9), p.1</ispartof><rights>Copyright The Physical Society of Japan Sep 15, 2022</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c355t-3181aff0cc78ef54ac2a0eacf027becbf0b39749692c50adf8b15c8ee9aaaafc3</cites><orcidid>0000-0003-2035-954X</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27922,27923</link.rule.ids></links><search><creatorcontrib>Tanaka, Hideaki</creatorcontrib><title>Toward Elucidation of the Photosynthetic Electron Transfer Mechanism</title><title>Journal of the Physical Society of Japan</title><description>Ferredoxins (Fds) are iron–sulfur proteins found in various organisms, and they act as multifunctional electron carriers in diverse redox systems. In plants, numerous Fd-dependent enzymes such as dark-operative protochlorophyllide reductase (DPOR), glutamate synthase (Fd-GOGAT), sulfite reductase (SiR), FTR (ferredoxin-thioredoxin reductase), and ferredoxin:NADP+ reductase (FNR) exist. However, there are no consensus sequences for Fd dependence, which is why we are interested in the molecular interaction between Fd and Fd-interacting proteins, including Photosystem I. The efficient electron transfer and backflow prevention mechanisms by Fd are also very interesting. Ultrahigh-resolution X-ray structure analysis by low-dose data collection will greatly advance our understanding of the electron transfer mechanism by Fd.</description><subject>Electron transfer</subject><subject>Molecular interactions</subject><subject>Photosynthesis</subject><subject>Proteins</subject><subject>Reductases</subject><subject>Structural analysis</subject><issn>0031-9015</issn><issn>1347-4073</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2022</creationdate><recordtype>article</recordtype><recordid>eNotkE1LAzEQhoMoWKtXzwued51JNs3mKLV-lIoF13PIpgnd0m5qkiL996bUuczAPLwvPITcI1SCTyaP8-XXvJJYgUQAekFGyGpR1iDYJRkBMCwlIL8mNzFuMsCR1iPy3PpfHVbFbHsw_Uqn3g-Fd0Va22K59snH45Dv1JtMWJNCfrdBD9HZUHxYs9ZDH3e35MrpbbR3_3tMvl9m7fStXHy-vk-fFqVhnKeSYYPaOTBGNNbxWhuqwWrjgIrOms5Bx6So5URSw0GvXNMhN421Uudxho3Jwzl3H_zPwcakNv4QhlypqADEGgWjmarOlAk-xmCd2od-p8NRIaiTKXUypSSqsyn2B0G8XSo</recordid><startdate>20220915</startdate><enddate>20220915</enddate><creator>Tanaka, Hideaki</creator><general>The Physical Society of Japan</general><scope>AAYXX</scope><scope>CITATION</scope><scope>7U5</scope><scope>8FD</scope><scope>H8D</scope><scope>L7M</scope><orcidid>https://orcid.org/0000-0003-2035-954X</orcidid></search><sort><creationdate>20220915</creationdate><title>Toward Elucidation of the Photosynthetic Electron Transfer Mechanism</title><author>Tanaka, Hideaki</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c355t-3181aff0cc78ef54ac2a0eacf027becbf0b39749692c50adf8b15c8ee9aaaafc3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2022</creationdate><topic>Electron transfer</topic><topic>Molecular interactions</topic><topic>Photosynthesis</topic><topic>Proteins</topic><topic>Reductases</topic><topic>Structural analysis</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Tanaka, Hideaki</creatorcontrib><collection>CrossRef</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>Technology Research Database</collection><collection>Aerospace Database</collection><collection>Advanced Technologies Database with Aerospace</collection><jtitle>Journal of the Physical Society of Japan</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Tanaka, Hideaki</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Toward Elucidation of the Photosynthetic Electron Transfer Mechanism</atitle><jtitle>Journal of the Physical Society of Japan</jtitle><date>2022-09-15</date><risdate>2022</risdate><volume>91</volume><issue>9</issue><spage>1</spage><pages>1-</pages><issn>0031-9015</issn><eissn>1347-4073</eissn><abstract>Ferredoxins (Fds) are iron–sulfur proteins found in various organisms, and they act as multifunctional electron carriers in diverse redox systems. 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subjects | Electron transfer Molecular interactions Photosynthesis Proteins Reductases Structural analysis |
title | Toward Elucidation of the Photosynthetic Electron Transfer Mechanism |
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