Changes in excitation relaxation of diatoms in response to fluctuating light, probed by fluorescence spectroscopies
A marine pennate diatom Phaeodactylum tricornutum ( Pt ) and a marine centric diatom Chaetoceros gracilis ( Cg ) possess unique light-harvesting complexes, fucoxanthin chlorophyll a / c -binding proteins (FCPs). FCPs have dual functions: light harvesting in the blue to green regions and quenching of...
Gespeichert in:
| Veröffentlicht in: | Photosynthesis research 2020-12, Vol.146 (1-3), p.143-150 |
|---|---|
| Hauptverfasser: | , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 150 |
|---|---|
| container_issue | 1-3 |
| container_start_page | 143 |
| container_title | Photosynthesis research |
| container_volume | 146 |
| creator | Tanabe, Miyuki Ueno, Yoshifumi Yokono, Makio Shen, Jian-Ren Nagao, Ryo Akimoto, Seiji |
| description | A marine pennate diatom
Phaeodactylum tricornutum
(
Pt
) and a marine centric diatom
Chaetoceros gracilis
(
Cg
) possess unique light-harvesting complexes, fucoxanthin chlorophyll
a
/
c
-binding proteins (FCPs). FCPs have dual functions: light harvesting in the blue to green regions and quenching of excess energy. So far, excitation dynamics including FCPs have been studied by altering continuous light conditions. In the present study, we examined responses of the diatom cells to fluctuating light (FL) conditions. Excitation dynamics in the cells incubated under the FL conditions were analyzed by time-resolved fluorescence measurements followed by global analysis. As responses common to the
Pt
and
Cg
cells, quenching behaviors were observed in photosystem (PS) II with time constants of hundreds of picoseconds. The PSII → PSI energy transfer was modified only in the
Pt
cells, whereas quenching in FCPs was suggested only in the
Cg
cells, indicating different strategy for the dissipation of excess energy under the FL conditions. |
| doi_str_mv | 10.1007/s11120-020-00720-3 |
| format | Article |
| fullrecord | <record><control><sourceid>gale_proqu</sourceid><recordid>TN_cdi_proquest_miscellaneous_2357461944</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><galeid>A639207178</galeid><sourcerecordid>A639207178</sourcerecordid><originalsourceid>FETCH-LOGICAL-c514t-ff24406d73846add3a8674b4c4ae3b3f0b1603c3eccd633d9d7224cbc693cff53</originalsourceid><addsrcrecordid>eNp9kd1r3iAUxsPYWN92-wd2MYTdtLB0x2g0uSwv-ygUBvu4FqPH1JLEd9HA2_9-Zuk2uoshR0V_z-HRpyheUbikAPJdpJRWUMJaIPPMnhQ7WktW1iDbp8UOqBBlU7f1SXEa4x0ANIKy58UJq0BIyppdEfe3euoxEj8RPBqfdPJhIjMO-rhtgyPW6xTGX8yM8RCmiCQF4obFpCVTU08G39-mt-Qwhw4t6e7Xy5Bhg5NBEg9o0hyiCQeP8UXxzOkh4suH9az4_uH9t_2n8ubzx-v91U1paspT6VzFOQgrWcOFtpbpRkjeccM1so456KgAZhgaYwVjtrWyqrjpjGiZca5mZ8X51je7-rFgTGr02dAw6AnDElXFaskFbTnP6Jt_0LuwzFN2pyouad2ABMjU5Ub1ekDlJxfSrE0eFkdvwoTO5_MrwdoKJJVNFlw8EmQm4TH1eolRXX_98pitNtbkj4ozOnWY_ajne0VBrXmrLW8Fa615K5ZFrx98L92I9o_kd8AZYBsQ81UOev77sP-0_QlfeLYA</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2471580700</pqid></control><display><type>article</type><title>Changes in excitation relaxation of diatoms in response to fluctuating light, probed by fluorescence spectroscopies</title><source>SpringerLink Journals - AutoHoldings</source><creator>Tanabe, Miyuki ; Ueno, Yoshifumi ; Yokono, Makio ; Shen, Jian-Ren ; Nagao, Ryo ; Akimoto, Seiji</creator><creatorcontrib>Tanabe, Miyuki ; Ueno, Yoshifumi ; Yokono, Makio ; Shen, Jian-Ren ; Nagao, Ryo ; Akimoto, Seiji</creatorcontrib><description>A marine pennate diatom
Phaeodactylum tricornutum
(
Pt
) and a marine centric diatom
Chaetoceros gracilis
(
Cg
) possess unique light-harvesting complexes, fucoxanthin chlorophyll
a
/
c
-binding proteins (FCPs). FCPs have dual functions: light harvesting in the blue to green regions and quenching of excess energy. So far, excitation dynamics including FCPs have been studied by altering continuous light conditions. In the present study, we examined responses of the diatom cells to fluctuating light (FL) conditions. Excitation dynamics in the cells incubated under the FL conditions were analyzed by time-resolved fluorescence measurements followed by global analysis. As responses common to the
Pt
and
Cg
cells, quenching behaviors were observed in photosystem (PS) II with time constants of hundreds of picoseconds. The PSII → PSI energy transfer was modified only in the
Pt
cells, whereas quenching in FCPs was suggested only in the
Cg
cells, indicating different strategy for the dissipation of excess energy under the FL conditions.</description><identifier>ISSN: 0166-8595</identifier><identifier>EISSN: 1573-5079</identifier><identifier>DOI: 10.1007/s11120-020-00720-3</identifier><identifier>PMID: 32067138</identifier><language>eng</language><publisher>Dordrecht: Springer Netherlands</publisher><subject>Analysis ; Binding proteins ; Biochemistry ; Biomedical and Life Sciences ; Chlorophyll ; Fluorescence ; Fucoxanthin ; Investigations ; Life Sciences ; Marine microorganisms ; Original Article ; Photosystem II ; Plant Genetics and Genomics ; Plant Physiology ; Plant Sciences ; Protein binding</subject><ispartof>Photosynthesis research, 2020-12, Vol.146 (1-3), p.143-150</ispartof><rights>Springer Nature B.V. 2020</rights><rights>COPYRIGHT 2020 Springer</rights><rights>Springer Nature B.V. 2020.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c514t-ff24406d73846add3a8674b4c4ae3b3f0b1603c3eccd633d9d7224cbc693cff53</citedby><cites>FETCH-LOGICAL-c514t-ff24406d73846add3a8674b4c4ae3b3f0b1603c3eccd633d9d7224cbc693cff53</cites><orcidid>0000-0002-8951-8978</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s11120-020-00720-3$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s11120-020-00720-3$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/32067138$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Tanabe, Miyuki</creatorcontrib><creatorcontrib>Ueno, Yoshifumi</creatorcontrib><creatorcontrib>Yokono, Makio</creatorcontrib><creatorcontrib>Shen, Jian-Ren</creatorcontrib><creatorcontrib>Nagao, Ryo</creatorcontrib><creatorcontrib>Akimoto, Seiji</creatorcontrib><title>Changes in excitation relaxation of diatoms in response to fluctuating light, probed by fluorescence spectroscopies</title><title>Photosynthesis research</title><addtitle>Photosynth Res</addtitle><addtitle>Photosynth Res</addtitle><description>A marine pennate diatom
Phaeodactylum tricornutum
(
Pt
) and a marine centric diatom
Chaetoceros gracilis
(
Cg
) possess unique light-harvesting complexes, fucoxanthin chlorophyll
a
/
c
-binding proteins (FCPs). FCPs have dual functions: light harvesting in the blue to green regions and quenching of excess energy. So far, excitation dynamics including FCPs have been studied by altering continuous light conditions. In the present study, we examined responses of the diatom cells to fluctuating light (FL) conditions. Excitation dynamics in the cells incubated under the FL conditions were analyzed by time-resolved fluorescence measurements followed by global analysis. As responses common to the
Pt
and
Cg
cells, quenching behaviors were observed in photosystem (PS) II with time constants of hundreds of picoseconds. The PSII → PSI energy transfer was modified only in the
Pt
cells, whereas quenching in FCPs was suggested only in the
Cg
cells, indicating different strategy for the dissipation of excess energy under the FL conditions.</description><subject>Analysis</subject><subject>Binding proteins</subject><subject>Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Chlorophyll</subject><subject>Fluorescence</subject><subject>Fucoxanthin</subject><subject>Investigations</subject><subject>Life Sciences</subject><subject>Marine microorganisms</subject><subject>Original Article</subject><subject>Photosystem II</subject><subject>Plant Genetics and Genomics</subject><subject>Plant Physiology</subject><subject>Plant Sciences</subject><subject>Protein binding</subject><issn>0166-8595</issn><issn>1573-5079</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2020</creationdate><recordtype>article</recordtype><sourceid>BENPR</sourceid><recordid>eNp9kd1r3iAUxsPYWN92-wd2MYTdtLB0x2g0uSwv-ygUBvu4FqPH1JLEd9HA2_9-Zuk2uoshR0V_z-HRpyheUbikAPJdpJRWUMJaIPPMnhQ7WktW1iDbp8UOqBBlU7f1SXEa4x0ANIKy58UJq0BIyppdEfe3euoxEj8RPBqfdPJhIjMO-rhtgyPW6xTGX8yM8RCmiCQF4obFpCVTU08G39-mt-Qwhw4t6e7Xy5Bhg5NBEg9o0hyiCQeP8UXxzOkh4suH9az4_uH9t_2n8ubzx-v91U1paspT6VzFOQgrWcOFtpbpRkjeccM1so456KgAZhgaYwVjtrWyqrjpjGiZca5mZ8X51je7-rFgTGr02dAw6AnDElXFaskFbTnP6Jt_0LuwzFN2pyouad2ABMjU5Ub1ekDlJxfSrE0eFkdvwoTO5_MrwdoKJJVNFlw8EmQm4TH1eolRXX_98pitNtbkj4ozOnWY_ajne0VBrXmrLW8Fa615K5ZFrx98L92I9o_kd8AZYBsQ81UOev77sP-0_QlfeLYA</recordid><startdate>20201201</startdate><enddate>20201201</enddate><creator>Tanabe, Miyuki</creator><creator>Ueno, Yoshifumi</creator><creator>Yokono, Makio</creator><creator>Shen, Jian-Ren</creator><creator>Nagao, Ryo</creator><creator>Akimoto, Seiji</creator><general>Springer Netherlands</general><general>Springer</general><general>Springer Nature B.V</general><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>ISR</scope><scope>3V.</scope><scope>7QP</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AO</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0002-8951-8978</orcidid></search><sort><creationdate>20201201</creationdate><title>Changes in excitation relaxation of diatoms in response to fluctuating light, probed by fluorescence spectroscopies</title><author>Tanabe, Miyuki ; Ueno, Yoshifumi ; Yokono, Makio ; Shen, Jian-Ren ; Nagao, Ryo ; Akimoto, Seiji</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c514t-ff24406d73846add3a8674b4c4ae3b3f0b1603c3eccd633d9d7224cbc693cff53</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2020</creationdate><topic>Analysis</topic><topic>Binding proteins</topic><topic>Biochemistry</topic><topic>Biomedical and Life Sciences</topic><topic>Chlorophyll</topic><topic>Fluorescence</topic><topic>Fucoxanthin</topic><topic>Investigations</topic><topic>Life Sciences</topic><topic>Marine microorganisms</topic><topic>Original Article</topic><topic>Photosystem II</topic><topic>Plant Genetics and Genomics</topic><topic>Plant Physiology</topic><topic>Plant Sciences</topic><topic>Protein binding</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Tanabe, Miyuki</creatorcontrib><creatorcontrib>Ueno, Yoshifumi</creatorcontrib><creatorcontrib>Yokono, Makio</creatorcontrib><creatorcontrib>Shen, Jian-Ren</creatorcontrib><creatorcontrib>Nagao, Ryo</creatorcontrib><creatorcontrib>Akimoto, Seiji</creatorcontrib><collection>PubMed</collection><collection>CrossRef</collection><collection>Gale In Context: Science</collection><collection>ProQuest Central (Corporate)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Science Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><jtitle>Photosynthesis research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Tanabe, Miyuki</au><au>Ueno, Yoshifumi</au><au>Yokono, Makio</au><au>Shen, Jian-Ren</au><au>Nagao, Ryo</au><au>Akimoto, Seiji</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Changes in excitation relaxation of diatoms in response to fluctuating light, probed by fluorescence spectroscopies</atitle><jtitle>Photosynthesis research</jtitle><stitle>Photosynth Res</stitle><addtitle>Photosynth Res</addtitle><date>2020-12-01</date><risdate>2020</risdate><volume>146</volume><issue>1-3</issue><spage>143</spage><epage>150</epage><pages>143-150</pages><issn>0166-8595</issn><eissn>1573-5079</eissn><abstract>A marine pennate diatom
Phaeodactylum tricornutum
(
Pt
) and a marine centric diatom
Chaetoceros gracilis
(
Cg
) possess unique light-harvesting complexes, fucoxanthin chlorophyll
a
/
c
-binding proteins (FCPs). FCPs have dual functions: light harvesting in the blue to green regions and quenching of excess energy. So far, excitation dynamics including FCPs have been studied by altering continuous light conditions. In the present study, we examined responses of the diatom cells to fluctuating light (FL) conditions. Excitation dynamics in the cells incubated under the FL conditions were analyzed by time-resolved fluorescence measurements followed by global analysis. As responses common to the
Pt
and
Cg
cells, quenching behaviors were observed in photosystem (PS) II with time constants of hundreds of picoseconds. The PSII → PSI energy transfer was modified only in the
Pt
cells, whereas quenching in FCPs was suggested only in the
Cg
cells, indicating different strategy for the dissipation of excess energy under the FL conditions.</abstract><cop>Dordrecht</cop><pub>Springer Netherlands</pub><pmid>32067138</pmid><doi>10.1007/s11120-020-00720-3</doi><tpages>8</tpages><orcidid>https://orcid.org/0000-0002-8951-8978</orcidid></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0166-8595 |
| ispartof | Photosynthesis research, 2020-12, Vol.146 (1-3), p.143-150 |
| issn | 0166-8595 1573-5079 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_2357461944 |
| source | SpringerLink Journals - AutoHoldings |
| subjects | Analysis Binding proteins Biochemistry Biomedical and Life Sciences Chlorophyll Fluorescence Fucoxanthin Investigations Life Sciences Marine microorganisms Original Article Photosystem II Plant Genetics and Genomics Plant Physiology Plant Sciences Protein binding |
| title | Changes in excitation relaxation of diatoms in response to fluctuating light, probed by fluorescence spectroscopies |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-28T18%3A24%3A28IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-gale_proqu&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Changes%20in%20excitation%20relaxation%20of%20diatoms%20in%20response%20to%20fluctuating%20light,%20probed%20by%20fluorescence%20spectroscopies&rft.jtitle=Photosynthesis%20research&rft.au=Tanabe,%20Miyuki&rft.date=2020-12-01&rft.volume=146&rft.issue=1-3&rft.spage=143&rft.epage=150&rft.pages=143-150&rft.issn=0166-8595&rft.eissn=1573-5079&rft_id=info:doi/10.1007/s11120-020-00720-3&rft_dat=%3Cgale_proqu%3EA639207178%3C/gale_proqu%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=2471580700&rft_id=info:pmid/32067138&rft_galeid=A639207178&rfr_iscdi=true |