Femtosecond Spectroscopy of Native and Carotenoidless Purple-Bacterial LH2 Clarifies Functions of Carotenoids
EET between the two circular bacteriochlorophyll compartments B800 and B850 in native (containing the carotenoid rhodopin) and carotenoidless LH2 isolated from the photosynthetic purple sulfur bacterium Allochromatium minutissimum was investigated by femtosecond time-resolved transient absorption sp...
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| Veröffentlicht in: | Biophysical journal 2008-06, Vol.94 (12), p.4808-4811 |
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| creator | Theiss, Christoph Leupold, Dieter Moskalenko, Andrei A. Razjivin, Andrei P. Eichler, Hans J. Lokstein, Heiko |
| description | EET between the two circular bacteriochlorophyll compartments B800 and B850 in native (containing the carotenoid rhodopin) and carotenoidless LH2 isolated from the photosynthetic purple sulfur bacterium Allochromatium minutissimum was investigated by femtosecond time-resolved transient absorption spectroscopy. Both samples were excited with 120-fs laser pulses at 800nm, and spectral evolution was followed in the 720–955nm range at different delay times. No dependence of transient absorption in the B800 band on the presence of the carotenoid rhodopin was found. Together with the likewise virtually unchanged absorption spectra in the bacteriochlorophyll Qy region, these observations suggest that absence of rhodopin does not significantly alter the structure of the pigment-protein complex including interactions between bacteriochlorophylls. Apparently, rhodopin does also not accelerate B800 to B850 EET in LH2, contrary to what has been suggested previously. Moreover, “carotenoid-catalyzed internal conversion” can also be excluded for the bacteriochlorophylls in LH2 of A. minutissimum. Together with previous results obtained with two-photon fluorescence excitation spectroscopy, it can also be concluded that there is neither EET from rhodopin to B800 nor (back-)EET from B800 to rhodopin. |
| doi_str_mv | 10.1529/biophysj.107.121681 |
| format | Article |
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Both samples were excited with 120-fs laser pulses at 800nm, and spectral evolution was followed in the 720–955nm range at different delay times. No dependence of transient absorption in the B800 band on the presence of the carotenoid rhodopin was found. Together with the likewise virtually unchanged absorption spectra in the bacteriochlorophyll Qy region, these observations suggest that absence of rhodopin does not significantly alter the structure of the pigment-protein complex including interactions between bacteriochlorophylls. Apparently, rhodopin does also not accelerate B800 to B850 EET in LH2, contrary to what has been suggested previously. Moreover, “carotenoid-catalyzed internal conversion” can also be excluded for the bacteriochlorophylls in LH2 of A. minutissimum. Together with previous results obtained with two-photon fluorescence excitation spectroscopy, it can also be concluded that there is neither EET from rhodopin to B800 nor (back-)EET from B800 to rhodopin.</description><identifier>ISSN: 0006-3495</identifier><identifier>EISSN: 1542-0086</identifier><identifier>DOI: 10.1529/biophysj.107.121681</identifier><identifier>PMID: 18339744</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Bacteria ; Biophysics ; Carotenoids ; Carotenoids - chemistry ; Carotenoids - radiation effects ; Delay ; Dose-Response Relationship, Radiation ; Evolution ; Excitation spectra ; Femtosecond ; Kinetics ; Lasers ; Light ; Light-Harvesting Protein Complexes - chemistry ; Light-Harvesting Protein Complexes - radiation effects ; Photobiophysics ; Pigments ; Proteobacteria - physiology ; Proteobacteria - radiation effects ; Radiation Dosage ; Spectra ; Spectroscopy ; Spectrum Analysis</subject><ispartof>Biophysical journal, 2008-06, Vol.94 (12), p.4808-4811</ispartof><rights>2008 The Biophysical Society</rights><rights>Copyright Biophysical Society Jun 15, 2008</rights><rights>Copyright © 2008, Biophysical Society</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c549t-c8802017f40600d6755da070aca2da0d89688fd3440bf191b7203fdfd9bc102c3</citedby><cites>FETCH-LOGICAL-c549t-c8802017f40600d6755da070aca2da0d89688fd3440bf191b7203fdfd9bc102c3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2397352/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://dx.doi.org/10.1529/biophysj.107.121681$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,885,3548,27923,27924,45994,53790,53792</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18339744$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Theiss, Christoph</creatorcontrib><creatorcontrib>Leupold, Dieter</creatorcontrib><creatorcontrib>Moskalenko, Andrei A.</creatorcontrib><creatorcontrib>Razjivin, Andrei P.</creatorcontrib><creatorcontrib>Eichler, Hans J.</creatorcontrib><creatorcontrib>Lokstein, Heiko</creatorcontrib><title>Femtosecond Spectroscopy of Native and Carotenoidless Purple-Bacterial LH2 Clarifies Functions of Carotenoids</title><title>Biophysical journal</title><addtitle>Biophys J</addtitle><description>EET between the two circular bacteriochlorophyll compartments B800 and B850 in native (containing the carotenoid rhodopin) and carotenoidless LH2 isolated from the photosynthetic purple sulfur bacterium Allochromatium minutissimum was investigated by femtosecond time-resolved transient absorption spectroscopy. Both samples were excited with 120-fs laser pulses at 800nm, and spectral evolution was followed in the 720–955nm range at different delay times. No dependence of transient absorption in the B800 band on the presence of the carotenoid rhodopin was found. Together with the likewise virtually unchanged absorption spectra in the bacteriochlorophyll Qy region, these observations suggest that absence of rhodopin does not significantly alter the structure of the pigment-protein complex including interactions between bacteriochlorophylls. Apparently, rhodopin does also not accelerate B800 to B850 EET in LH2, contrary to what has been suggested previously. Moreover, “carotenoid-catalyzed internal conversion” can also be excluded for the bacteriochlorophylls in LH2 of A. minutissimum. Together with previous results obtained with two-photon fluorescence excitation spectroscopy, it can also be concluded that there is neither EET from rhodopin to B800 nor (back-)EET from B800 to rhodopin.</description><subject>Bacteria</subject><subject>Biophysics</subject><subject>Carotenoids</subject><subject>Carotenoids - chemistry</subject><subject>Carotenoids - radiation effects</subject><subject>Delay</subject><subject>Dose-Response Relationship, Radiation</subject><subject>Evolution</subject><subject>Excitation spectra</subject><subject>Femtosecond</subject><subject>Kinetics</subject><subject>Lasers</subject><subject>Light</subject><subject>Light-Harvesting Protein Complexes - chemistry</subject><subject>Light-Harvesting Protein Complexes - radiation effects</subject><subject>Photobiophysics</subject><subject>Pigments</subject><subject>Proteobacteria - physiology</subject><subject>Proteobacteria - radiation effects</subject><subject>Radiation Dosage</subject><subject>Spectra</subject><subject>Spectroscopy</subject><subject>Spectrum Analysis</subject><issn>0006-3495</issn><issn>1542-0086</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNp9kk-P0zAQxS0EYsvCJ0BCEQeWS8rYcfznABJbURapAiTgbDm2w7pK4qydVOq3x1ULCxx6suX5zRv5zUPoOYYlrol80_gw3u7TdomBLzHBTOAHaIFrSkoAwR6iBQCwsqKyvkBPUtoCYFIDfowusKgqySldoH7t-ikkZ8Jgi2-jM1MMyYRxX4S2-Kwnv3OFzqWVjmFyQ_C2cykVX-c4dq681mZy0euu2NyQYtXp6FvvUrGeBzP5MKSDyn1reooetbpL7tnpvEQ_1h--r27KzZePn1bvN6WpqZxKIwQQwLylwAAs43VtNXDQRpN8sUIyIVpbUQpNiyVuOIGqta2VjcFATHWJ3h11x7npnTVumKLu1Bh9r-NeBe3Vv5XB36qfYadItqWqSRa4OgnEcDe7NKneJ-O6Tg8uzEkJRimhUtaZfHWW5MA5AwoZfH0WxIxjKirBD9Nf_oduwxyH7JgiuGZSgKAZqo6QyRtL0bV_vodBHQKifgckP3B1DEjuevG3M_c9p0Rk4O0RcHk_O--iSsa7wTjrY06HssGfHfALC4TPMg</recordid><startdate>200806</startdate><enddate>200806</enddate><creator>Theiss, Christoph</creator><creator>Leupold, Dieter</creator><creator>Moskalenko, Andrei A.</creator><creator>Razjivin, Andrei P.</creator><creator>Eichler, Hans J.</creator><creator>Lokstein, Heiko</creator><general>Elsevier Inc</general><general>Biophysical Society</general><general>The Biophysical Society</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>3V.</scope><scope>7QO</scope><scope>7QP</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AF</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M2P</scope><scope>M7P</scope><scope>MBDVC</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>S0X</scope><scope>7TB</scope><scope>7U5</scope><scope>L7M</scope><scope>7X8</scope><scope>7QL</scope><scope>C1K</scope><scope>5PM</scope></search><sort><creationdate>200806</creationdate><title>Femtosecond Spectroscopy of Native and Carotenoidless Purple-Bacterial LH2 Clarifies Functions of Carotenoids</title><author>Theiss, Christoph ; Leupold, Dieter ; Moskalenko, Andrei A. ; Razjivin, Andrei P. ; Eichler, Hans J. ; Lokstein, Heiko</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c549t-c8802017f40600d6755da070aca2da0d89688fd3440bf191b7203fdfd9bc102c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>Bacteria</topic><topic>Biophysics</topic><topic>Carotenoids</topic><topic>Carotenoids - 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Academic</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Biophysical journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Theiss, Christoph</au><au>Leupold, Dieter</au><au>Moskalenko, Andrei A.</au><au>Razjivin, Andrei P.</au><au>Eichler, Hans J.</au><au>Lokstein, Heiko</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Femtosecond Spectroscopy of Native and Carotenoidless Purple-Bacterial LH2 Clarifies Functions of Carotenoids</atitle><jtitle>Biophysical journal</jtitle><addtitle>Biophys J</addtitle><date>2008-06</date><risdate>2008</risdate><volume>94</volume><issue>12</issue><spage>4808</spage><epage>4811</epage><pages>4808-4811</pages><issn>0006-3495</issn><eissn>1542-0086</eissn><abstract>EET between the two circular bacteriochlorophyll compartments B800 and B850 in native (containing the carotenoid rhodopin) and carotenoidless LH2 isolated from the photosynthetic purple sulfur bacterium Allochromatium minutissimum was investigated by femtosecond time-resolved transient absorption spectroscopy. Both samples were excited with 120-fs laser pulses at 800nm, and spectral evolution was followed in the 720–955nm range at different delay times. No dependence of transient absorption in the B800 band on the presence of the carotenoid rhodopin was found. Together with the likewise virtually unchanged absorption spectra in the bacteriochlorophyll Qy region, these observations suggest that absence of rhodopin does not significantly alter the structure of the pigment-protein complex including interactions between bacteriochlorophylls. Apparently, rhodopin does also not accelerate B800 to B850 EET in LH2, contrary to what has been suggested previously. Moreover, “carotenoid-catalyzed internal conversion” can also be excluded for the bacteriochlorophylls in LH2 of A. minutissimum. Together with previous results obtained with two-photon fluorescence excitation spectroscopy, it can also be concluded that there is neither EET from rhodopin to B800 nor (back-)EET from B800 to rhodopin.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>18339744</pmid><doi>10.1529/biophysj.107.121681</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Bacteria Biophysics Carotenoids Carotenoids - chemistry Carotenoids - radiation effects Delay Dose-Response Relationship, Radiation Evolution Excitation spectra Femtosecond Kinetics Lasers Light Light-Harvesting Protein Complexes - chemistry Light-Harvesting Protein Complexes - radiation effects Photobiophysics Pigments Proteobacteria - physiology Proteobacteria - radiation effects Radiation Dosage Spectra Spectroscopy Spectrum Analysis |
| title | Femtosecond Spectroscopy of Native and Carotenoidless Purple-Bacterial LH2 Clarifies Functions of Carotenoids |
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