Peridinin–chlorophyll–protein reconstituted with chlorophyll mixtures: Preparation, bulk and single molecule spectroscopy
Reconstitution of the 16 kDa N-terminal domain of the peridinin–chlorophyll–protein, N-PCP, with mixtures of chlorophyll a (Chl a) and Chl b, resulted in 32 kDa complexes containing two pigment clusters, each bound to one N-PCP. Besides homo-chlorophyllous complexes, hetero-chlorophyllous ones were...
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| Veröffentlicht in: | FEBS letters 2006-10, Vol.580 (22), p.5257-5262 |
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| creator | Brotosudarmo, T.H.P. Hofmann, E. Hiller, R.G. Wörmke, S. Mackowski, S. Zumbusch, A. Bräuchle, C. Scheer, H. |
| description | Reconstitution of the 16
kDa N-terminal domain of the peridinin–chlorophyll–protein, N-PCP, with mixtures of chlorophyll
a (Chl
a) and Chl
b, resulted in 32
kDa complexes containing two pigment clusters, each bound to one N-PCP. Besides homo-chlorophyllous complexes, hetero-chlorophyllous ones were obtained that contain Chl
a in one pigment cluster, and Chl
b in the other. Binding of Chl
b is stronger than that of the native pigment, Chl
a. Energy transfer from Chl
b to Chl
a is efficient, but there are only weak interactions between the two pigments. Individual homo- and hetero-chlorophyllous complexes were investigated by single molecule spectroscopy using excitation into the peridinin absorption band and scanning of the Chl fluorescence, the latter show frequently well resolved emissions of the two pigments. |
| doi_str_mv | 10.1016/j.febslet.2006.08.049 |
| format | Article |
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kDa N-terminal domain of the peridinin–chlorophyll–protein, N-PCP, with mixtures of chlorophyll
a (Chl
a) and Chl
b, resulted in 32
kDa complexes containing two pigment clusters, each bound to one N-PCP. Besides homo-chlorophyllous complexes, hetero-chlorophyllous ones were obtained that contain Chl
a in one pigment cluster, and Chl
b in the other. Binding of Chl
b is stronger than that of the native pigment, Chl
a. Energy transfer from Chl
b to Chl
a is efficient, but there are only weak interactions between the two pigments. Individual homo- and hetero-chlorophyllous complexes were investigated by single molecule spectroscopy using excitation into the peridinin absorption band and scanning of the Chl fluorescence, the latter show frequently well resolved emissions of the two pigments.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/j.febslet.2006.08.049</identifier><identifier>PMID: 16962590</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>Amphidinium ; Animals ; Carotenoid ; Carotenoids - chemistry ; Carotenoids - metabolism ; Chl ; Chlorophyll ; Chlorophyll - chemistry ; Chlorophyll - metabolism ; circular dichroism ; EET ; Energy transfer ; Eukaryota - chemistry ; Eukaryota - metabolism ; excitation energy transfer ; l-PCP ; large (32 kDa PCP) ; Light-harvesting ; N-PCP ; N-terminal 16 kDa-domain of PCP ; PCP ; Per ; peridinin ; peridinin–chlorophyll–protein ; Photosynthesis ; Protozoan Proteins - chemistry ; Protozoan Proteins - metabolism ; s-PCP ; Single molecule spectroscopy ; small (16 kDa) PCP ; SMS ; Spectrophotometry - methods</subject><ispartof>FEBS letters, 2006-10, Vol.580 (22), p.5257-5262</ispartof><rights>2006 Federation of European Biochemical Societies</rights><rights>FEBS Letters 580 (2006) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4751-370fee84fae95e25d125182370275782279a51ef16c37b0806c0ac692565966f3</citedby><cites>FETCH-LOGICAL-c4751-370fee84fae95e25d125182370275782279a51ef16c37b0806c0ac692565966f3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1016%2Fj.febslet.2006.08.049$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.febslet.2006.08.049$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>315,781,785,1418,1434,3551,27926,27927,45576,45577,45997,46411,46835</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16962590$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Brotosudarmo, T.H.P.</creatorcontrib><creatorcontrib>Hofmann, E.</creatorcontrib><creatorcontrib>Hiller, R.G.</creatorcontrib><creatorcontrib>Wörmke, S.</creatorcontrib><creatorcontrib>Mackowski, S.</creatorcontrib><creatorcontrib>Zumbusch, A.</creatorcontrib><creatorcontrib>Bräuchle, C.</creatorcontrib><creatorcontrib>Scheer, H.</creatorcontrib><title>Peridinin–chlorophyll–protein reconstituted with chlorophyll mixtures: Preparation, bulk and single molecule spectroscopy</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>Reconstitution of the 16
kDa N-terminal domain of the peridinin–chlorophyll–protein, N-PCP, with mixtures of chlorophyll
a (Chl
a) and Chl
b, resulted in 32
kDa complexes containing two pigment clusters, each bound to one N-PCP. Besides homo-chlorophyllous complexes, hetero-chlorophyllous ones were obtained that contain Chl
a in one pigment cluster, and Chl
b in the other. Binding of Chl
b is stronger than that of the native pigment, Chl
a. Energy transfer from Chl
b to Chl
a is efficient, but there are only weak interactions between the two pigments. Individual homo- and hetero-chlorophyllous complexes were investigated by single molecule spectroscopy using excitation into the peridinin absorption band and scanning of the Chl fluorescence, the latter show frequently well resolved emissions of the two pigments.</description><subject>Amphidinium</subject><subject>Animals</subject><subject>Carotenoid</subject><subject>Carotenoids - chemistry</subject><subject>Carotenoids - metabolism</subject><subject>Chl</subject><subject>Chlorophyll</subject><subject>Chlorophyll - chemistry</subject><subject>Chlorophyll - metabolism</subject><subject>circular dichroism</subject><subject>EET</subject><subject>Energy transfer</subject><subject>Eukaryota - chemistry</subject><subject>Eukaryota - metabolism</subject><subject>excitation energy transfer</subject><subject>l-PCP</subject><subject>large (32 kDa PCP)</subject><subject>Light-harvesting</subject><subject>N-PCP</subject><subject>N-terminal 16 kDa-domain of PCP</subject><subject>PCP</subject><subject>Per</subject><subject>peridinin</subject><subject>peridinin–chlorophyll–protein</subject><subject>Photosynthesis</subject><subject>Protozoan Proteins - chemistry</subject><subject>Protozoan Proteins - metabolism</subject><subject>s-PCP</subject><subject>Single molecule spectroscopy</subject><subject>small (16 kDa) PCP</subject><subject>SMS</subject><subject>Spectrophotometry - methods</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkU2O1DAQhS0EYpqBI4CyYkVC2Ykdmw2C0fwgjcRIwNpKOxXajRMH22HoBRJ34IZzEtzqlmAHK7usV6_K3yPkKYWKAhUvt9WA6-gwVQxAVCAraNQ9sqKyrcu6EfI-WQHQpuStqk_Ioxi3kGtJ1UNyQoUSjCtYkR83GGxvJzvd_fxlNs4HP292zuVqDj6hnYqAxk8x2bQk7ItbmzbFX8JitN_TEjC-Km4Czl3okvXTi2K9uC9FN_VFtNNnh8XoHZolX-KMJgUfjZ93j8mDoXMRnxzPU_Lp4vzj2VV5_f7y3dmb69I0Ladl3cKAKJuhQ8WR8Z4yTiXLz6zlrWSsVR2nOFBh6nYNEoSBzgjFuOBKiKE-Jc8PvvlPXxeMSY82GnSum9AvUQsplWStzEJ-EJq8YQw46DnYsQs7TUHvueutPnLXe-4apM7cc9-z44BlPWL_p-sIOguuDoJb63D3f6764vwt-7APcZ8hCKDQNDRbvT5YYSb2zWLQ0VicDPY2R5V07-0_tv0N6gSxIw</recordid><startdate>20061002</startdate><enddate>20061002</enddate><creator>Brotosudarmo, T.H.P.</creator><creator>Hofmann, E.</creator><creator>Hiller, R.G.</creator><creator>Wörmke, S.</creator><creator>Mackowski, S.</creator><creator>Zumbusch, A.</creator><creator>Bräuchle, C.</creator><creator>Scheer, H.</creator><general>Elsevier B.V</general><scope>6I.</scope><scope>AAFTH</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></search><sort><creationdate>20061002</creationdate><title>Peridinin–chlorophyll–protein reconstituted with chlorophyll mixtures: Preparation, bulk and single molecule spectroscopy</title><author>Brotosudarmo, T.H.P. ; Hofmann, E. ; Hiller, R.G. ; Wörmke, S. ; Mackowski, S. ; Zumbusch, A. ; Bräuchle, C. ; Scheer, H.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4751-370fee84fae95e25d125182370275782279a51ef16c37b0806c0ac692565966f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Amphidinium</topic><topic>Animals</topic><topic>Carotenoid</topic><topic>Carotenoids - chemistry</topic><topic>Carotenoids - metabolism</topic><topic>Chl</topic><topic>Chlorophyll</topic><topic>Chlorophyll - chemistry</topic><topic>Chlorophyll - metabolism</topic><topic>circular dichroism</topic><topic>EET</topic><topic>Energy transfer</topic><topic>Eukaryota - chemistry</topic><topic>Eukaryota - metabolism</topic><topic>excitation energy transfer</topic><topic>l-PCP</topic><topic>large (32 kDa PCP)</topic><topic>Light-harvesting</topic><topic>N-PCP</topic><topic>N-terminal 16 kDa-domain of PCP</topic><topic>PCP</topic><topic>Per</topic><topic>peridinin</topic><topic>peridinin–chlorophyll–protein</topic><topic>Photosynthesis</topic><topic>Protozoan Proteins - chemistry</topic><topic>Protozoan Proteins - metabolism</topic><topic>s-PCP</topic><topic>Single molecule spectroscopy</topic><topic>small (16 kDa) PCP</topic><topic>SMS</topic><topic>Spectrophotometry - methods</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Brotosudarmo, T.H.P.</creatorcontrib><creatorcontrib>Hofmann, E.</creatorcontrib><creatorcontrib>Hiller, R.G.</creatorcontrib><creatorcontrib>Wörmke, S.</creatorcontrib><creatorcontrib>Mackowski, S.</creatorcontrib><creatorcontrib>Zumbusch, A.</creatorcontrib><creatorcontrib>Bräuchle, C.</creatorcontrib><creatorcontrib>Scheer, H.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</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><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Brotosudarmo, T.H.P.</au><au>Hofmann, E.</au><au>Hiller, R.G.</au><au>Wörmke, S.</au><au>Mackowski, S.</au><au>Zumbusch, A.</au><au>Bräuchle, C.</au><au>Scheer, H.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Peridinin–chlorophyll–protein reconstituted with chlorophyll mixtures: Preparation, bulk and single molecule spectroscopy</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>2006-10-02</date><risdate>2006</risdate><volume>580</volume><issue>22</issue><spage>5257</spage><epage>5262</epage><pages>5257-5262</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>Reconstitution of the 16
kDa N-terminal domain of the peridinin–chlorophyll–protein, N-PCP, with mixtures of chlorophyll
a (Chl
a) and Chl
b, resulted in 32
kDa complexes containing two pigment clusters, each bound to one N-PCP. Besides homo-chlorophyllous complexes, hetero-chlorophyllous ones were obtained that contain Chl
a in one pigment cluster, and Chl
b in the other. Binding of Chl
b is stronger than that of the native pigment, Chl
a. Energy transfer from Chl
b to Chl
a is efficient, but there are only weak interactions between the two pigments. Individual homo- and hetero-chlorophyllous complexes were investigated by single molecule spectroscopy using excitation into the peridinin absorption band and scanning of the Chl fluorescence, the latter show frequently well resolved emissions of the two pigments.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>16962590</pmid><doi>10.1016/j.febslet.2006.08.049</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Wiley Online Library; Elsevier ScienceDirect Journals Complete; Wiley Free Archive; Alma/SFX Local Collection; EZB Electronic Journals Library |
| subjects | Amphidinium Animals Carotenoid Carotenoids - chemistry Carotenoids - metabolism Chl Chlorophyll Chlorophyll - chemistry Chlorophyll - metabolism circular dichroism EET Energy transfer Eukaryota - chemistry Eukaryota - metabolism excitation energy transfer l-PCP large (32 kDa PCP) Light-harvesting N-PCP N-terminal 16 kDa-domain of PCP PCP Per peridinin peridinin–chlorophyll–protein Photosynthesis Protozoan Proteins - chemistry Protozoan Proteins - metabolism s-PCP Single molecule spectroscopy small (16 kDa) PCP SMS Spectrophotometry - methods |
| title | Peridinin–chlorophyll–protein reconstituted with chlorophyll mixtures: Preparation, bulk and single molecule spectroscopy |
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