Kinetics of phyllosemiquinone oxidation in the Photosystem I reaction centre of Acaryochloris marina
Light-induced electron transfer reactions in the chlorophyll a/d-binding Photosystem I reaction centre of Acaryochloris marina were investigated in whole cells by pump-probe optical spectroscopy with a temporal resolution of ~5ns at room temperature. It is shown that phyllosemiquinone, the secondary...
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| Veröffentlicht in: | Biochimica et biophysica acta 2012-02, Vol.1817 (2), p.328-335 |
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| container_title | Biochimica et biophysica acta |
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| creator | Santabarbara, Stefano Bailleul, Benjamin Redding, Kevin Barber, James Rappaport, Fabrice Telfer, Alison |
| description | Light-induced electron transfer reactions in the chlorophyll a/d-binding Photosystem I reaction centre of Acaryochloris marina were investigated in whole cells by pump-probe optical spectroscopy with a temporal resolution of ~5ns at room temperature. It is shown that phyllosemiquinone, the secondary electron transfer acceptor anion, is oxidised with bi-phasic kinetics characterised by lifetimes of 88±6ns and 345±10ns. These lifetimes, particularly the former, are significantly slower than those reported for chlorophyll a-binding Photosystem I, which typically range in the 5–30ns and 200–300ns intervals. The possible mechanism of electron transfer reactions in the chlorophyll a/d-binding Photosystem I and the slower oxidation kinetics of the secondary acceptors are discussed.
► The oxidation kinetics of secondary intermediates in PS I of A. marina are biphasic. ► The decay is characterised by lifetimes of 88±6ns and 345±10ns. ► Both these lifetimes are slower than in typical Chl a-binding PS I reaction centres. ► Possible mechanism of electron transfer is discussed. |
| doi_str_mv | 10.1016/j.bbabio.2011.10.003 |
| format | Article |
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► The oxidation kinetics of secondary intermediates in PS I of A. marina are biphasic. ► The decay is characterised by lifetimes of 88±6ns and 345±10ns. ► Both these lifetimes are slower than in typical Chl a-binding PS I reaction centres. ► Possible mechanism of electron transfer is discussed.</description><identifier>ISSN: 0005-2728</identifier><identifier>ISSN: 0006-3002</identifier><identifier>EISSN: 1879-2650</identifier><identifier>DOI: 10.1016/j.bbabio.2011.10.003</identifier><identifier>PMID: 22037394</identifier><language>eng</language><publisher>Netherlands: Elsevier B.V</publisher><subject>Acaryochloris marina ; ambient temperature ; Benzoquinones - metabolism ; Bidirectional electron transfer ; chlorophyll ; Chlorophyll d ; Cyanobacteria - chemistry ; Cyanobacteria - enzymology ; Cyanobacteria - growth & development ; Cyanobacteria - metabolism ; electron transfer ; Kinetics ; oxidation ; Oxidation-Reduction ; Photosystem I ; Photosystem I Protein Complex - chemistry ; Photosystem I Protein Complex - metabolism ; Phylloquinone ; Proteolysis ; Radical pair ; spectroscopy ; Spectrum Analysis ; Synechocystis - enzymology ; Synechocystis - growth & development ; Synechocystis - metabolism ; Time Factors ; Vitamin K 1 - chemistry ; Vitamin K 1 - metabolism</subject><ispartof>Biochimica et biophysica acta, 2012-02, Vol.1817 (2), p.328-335</ispartof><rights>2011 Elsevier B.V.</rights><rights>Copyright © 2011 Elsevier B.V. All rights reserved.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c458t-ec45e2f0022029f77e997abbde4a9f22aafffc26052218663ce618fda12ef9c3</citedby><cites>FETCH-LOGICAL-c458t-ec45e2f0022029f77e997abbde4a9f22aafffc26052218663ce618fda12ef9c3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.bbabio.2011.10.003$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>230,314,780,784,885,3548,27922,27923,45993</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22037394$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://www.osti.gov/biblio/1209632$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>Santabarbara, Stefano</creatorcontrib><creatorcontrib>Bailleul, Benjamin</creatorcontrib><creatorcontrib>Redding, Kevin</creatorcontrib><creatorcontrib>Barber, James</creatorcontrib><creatorcontrib>Rappaport, Fabrice</creatorcontrib><creatorcontrib>Telfer, Alison</creatorcontrib><title>Kinetics of phyllosemiquinone oxidation in the Photosystem I reaction centre of Acaryochloris marina</title><title>Biochimica et biophysica acta</title><addtitle>Biochim Biophys Acta</addtitle><description>Light-induced electron transfer reactions in the chlorophyll a/d-binding Photosystem I reaction centre of Acaryochloris marina were investigated in whole cells by pump-probe optical spectroscopy with a temporal resolution of ~5ns at room temperature. It is shown that phyllosemiquinone, the secondary electron transfer acceptor anion, is oxidised with bi-phasic kinetics characterised by lifetimes of 88±6ns and 345±10ns. These lifetimes, particularly the former, are significantly slower than those reported for chlorophyll a-binding Photosystem I, which typically range in the 5–30ns and 200–300ns intervals. The possible mechanism of electron transfer reactions in the chlorophyll a/d-binding Photosystem I and the slower oxidation kinetics of the secondary acceptors are discussed.
► The oxidation kinetics of secondary intermediates in PS I of A. marina are biphasic. ► The decay is characterised by lifetimes of 88±6ns and 345±10ns. ► Both these lifetimes are slower than in typical Chl a-binding PS I reaction centres. ► Possible mechanism of electron transfer is discussed.</description><subject>Acaryochloris marina</subject><subject>ambient temperature</subject><subject>Benzoquinones - metabolism</subject><subject>Bidirectional electron transfer</subject><subject>chlorophyll</subject><subject>Chlorophyll d</subject><subject>Cyanobacteria - chemistry</subject><subject>Cyanobacteria - enzymology</subject><subject>Cyanobacteria - growth & development</subject><subject>Cyanobacteria - metabolism</subject><subject>electron transfer</subject><subject>Kinetics</subject><subject>oxidation</subject><subject>Oxidation-Reduction</subject><subject>Photosystem I</subject><subject>Photosystem I Protein Complex - chemistry</subject><subject>Photosystem I Protein Complex - metabolism</subject><subject>Phylloquinone</subject><subject>Proteolysis</subject><subject>Radical pair</subject><subject>spectroscopy</subject><subject>Spectrum Analysis</subject><subject>Synechocystis - enzymology</subject><subject>Synechocystis - growth & development</subject><subject>Synechocystis - metabolism</subject><subject>Time Factors</subject><subject>Vitamin K 1 - chemistry</subject><subject>Vitamin K 1 - metabolism</subject><issn>0005-2728</issn><issn>0006-3002</issn><issn>1879-2650</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kUFv1DAQhS0EotvCP0AQceGUxR5n4_iCVFVQKiqBRDlbjjMmXiX21vZW7L_HIYUjp5HG34zfvEfIK0a3jLL2_X7b97p3YQuUsdLaUsqfkA3rhKyh3dGnZEMp3dUgoDsj5yntaRlrgD8nZwCUCy6bDRm-OI_ZmVQFWx3G0zSFhLO7PzofPFbhlxt0dsFXzld5xOrbGHJIp5Rxrm6qiNr8eTXoc8Rlx6XR8RTMOIXoUjXr6Lx-QZ5ZPSV8-VgvyN2nj3dXn-vbr9c3V5e3tWl2Xa6xFARLaZEH0gqBUgrd9wM2WloAra21Blq6A2Bd23KDLevsoBmglYZfkLfr2pCyU8m4jGY0wXs0WTGgsuVQoHcrdIjh_ogpq9klg9OkPYZjUpJxAUyAKGSzkiaGlCJadYiuHHRSjKolArVXawRqiWDplgjK2OvHD479jMO_ob-eF-DNClgdlP5ZbFI_vpcNbYmLN123aPywEljMenAYl2PQGxxcXG4Zgvu_ht9K9KPD</recordid><startdate>20120201</startdate><enddate>20120201</enddate><creator>Santabarbara, Stefano</creator><creator>Bailleul, Benjamin</creator><creator>Redding, Kevin</creator><creator>Barber, James</creator><creator>Rappaport, Fabrice</creator><creator>Telfer, Alison</creator><general>Elsevier B.V</general><general>Elsevier</general><scope>6I.</scope><scope>AAFTH</scope><scope>FBQ</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>OTOTI</scope></search><sort><creationdate>20120201</creationdate><title>Kinetics of phyllosemiquinone oxidation in the Photosystem I reaction centre of Acaryochloris marina</title><author>Santabarbara, Stefano ; Bailleul, Benjamin ; Redding, Kevin ; Barber, James ; Rappaport, Fabrice ; Telfer, Alison</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c458t-ec45e2f0022029f77e997abbde4a9f22aafffc26052218663ce618fda12ef9c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>Acaryochloris marina</topic><topic>ambient temperature</topic><topic>Benzoquinones - metabolism</topic><topic>Bidirectional electron transfer</topic><topic>chlorophyll</topic><topic>Chlorophyll d</topic><topic>Cyanobacteria - chemistry</topic><topic>Cyanobacteria - enzymology</topic><topic>Cyanobacteria - growth & development</topic><topic>Cyanobacteria - metabolism</topic><topic>electron transfer</topic><topic>Kinetics</topic><topic>oxidation</topic><topic>Oxidation-Reduction</topic><topic>Photosystem I</topic><topic>Photosystem I Protein Complex - chemistry</topic><topic>Photosystem I Protein Complex - metabolism</topic><topic>Phylloquinone</topic><topic>Proteolysis</topic><topic>Radical pair</topic><topic>spectroscopy</topic><topic>Spectrum Analysis</topic><topic>Synechocystis - enzymology</topic><topic>Synechocystis - growth & development</topic><topic>Synechocystis - metabolism</topic><topic>Time Factors</topic><topic>Vitamin K 1 - chemistry</topic><topic>Vitamin K 1 - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Santabarbara, Stefano</creatorcontrib><creatorcontrib>Bailleul, Benjamin</creatorcontrib><creatorcontrib>Redding, Kevin</creatorcontrib><creatorcontrib>Barber, James</creatorcontrib><creatorcontrib>Rappaport, Fabrice</creatorcontrib><creatorcontrib>Telfer, Alison</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>OSTI.GOV</collection><jtitle>Biochimica et biophysica acta</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Santabarbara, Stefano</au><au>Bailleul, Benjamin</au><au>Redding, Kevin</au><au>Barber, James</au><au>Rappaport, Fabrice</au><au>Telfer, Alison</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Kinetics of phyllosemiquinone oxidation in the Photosystem I reaction centre of Acaryochloris marina</atitle><jtitle>Biochimica et biophysica acta</jtitle><addtitle>Biochim Biophys Acta</addtitle><date>2012-02-01</date><risdate>2012</risdate><volume>1817</volume><issue>2</issue><spage>328</spage><epage>335</epage><pages>328-335</pages><issn>0005-2728</issn><issn>0006-3002</issn><eissn>1879-2650</eissn><abstract>Light-induced electron transfer reactions in the chlorophyll a/d-binding Photosystem I reaction centre of Acaryochloris marina were investigated in whole cells by pump-probe optical spectroscopy with a temporal resolution of ~5ns at room temperature. It is shown that phyllosemiquinone, the secondary electron transfer acceptor anion, is oxidised with bi-phasic kinetics characterised by lifetimes of 88±6ns and 345±10ns. These lifetimes, particularly the former, are significantly slower than those reported for chlorophyll a-binding Photosystem I, which typically range in the 5–30ns and 200–300ns intervals. The possible mechanism of electron transfer reactions in the chlorophyll a/d-binding Photosystem I and the slower oxidation kinetics of the secondary acceptors are discussed.
► The oxidation kinetics of secondary intermediates in PS I of A. marina are biphasic. ► The decay is characterised by lifetimes of 88±6ns and 345±10ns. ► Both these lifetimes are slower than in typical Chl a-binding PS I reaction centres. ► Possible mechanism of electron transfer is discussed.</abstract><cop>Netherlands</cop><pub>Elsevier B.V</pub><pmid>22037394</pmid><doi>10.1016/j.bbabio.2011.10.003</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Acaryochloris marina ambient temperature Benzoquinones - metabolism Bidirectional electron transfer chlorophyll Chlorophyll d Cyanobacteria - chemistry Cyanobacteria - enzymology Cyanobacteria - growth & development Cyanobacteria - metabolism electron transfer Kinetics oxidation Oxidation-Reduction Photosystem I Photosystem I Protein Complex - chemistry Photosystem I Protein Complex - metabolism Phylloquinone Proteolysis Radical pair spectroscopy Spectrum Analysis Synechocystis - enzymology Synechocystis - growth & development Synechocystis - metabolism Time Factors Vitamin K 1 - chemistry Vitamin K 1 - metabolism |
| title | Kinetics of phyllosemiquinone oxidation in the Photosystem I reaction centre of Acaryochloris marina |
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