Pigment organisation in the membrane-intrinsic major light-harvesting complex of Amphidinium carterae: Structural characterisation of the peridinins and chlorophylls a and c2 by resonance Raman spectroscopy and from sequence analysis.
Identifieur interne : 002860 ( PubMed/Corpus ); précédent : 002859; suivant : 002861Pigment organisation in the membrane-intrinsic major light-harvesting complex of Amphidinium carterae: Structural characterisation of the peridinins and chlorophylls a and c2 by resonance Raman spectroscopy and from sequence analysis.
Auteurs : Lavanya Premvardhan ; Bruno Robert ; Roger G. HillerSource :
- Biochimica et biophysica acta [ 0006-3002 ] ; 2015.
Abstract
The structures and environments of the protein-bound peridinins (Pers) and chlorophylls (Chls) a/c2 in the membrane-intrinsic major light-harvesting complex of the dinoflagellate Amphidinium carterae (LHCAmph) are characterised using resonance Raman (RR) spectroscopy with 11 excitation wavelengths, at 77K. The excitation-dependent variation in the CC stretching mode (ν1) suggests the presence of three Pers with conjugation lengths over 8 double bonds (dBs), and one diadinoxanthin, between 413.7 and 528.7nm. Two Perred species are revealed on excitation at 550 and 560nm. These Perred species exhibit anomalously low ν1 values, together with notable resonant enhancement of lactone ring-breathing and -deformation modes. To discern protein-specific effects, the RR spectra are compared to that of Per in polar (acetonitrile), polarisable (toluene) and polar-protic (ethanol) solvents. Resonantly enhanced lactone, ring-breathing (942cm(-1)) and ring-deformation (~650cm(-1)), modes are identified both in solution, and in the protein, and discussed in the context of the mixing of the S1 and S2 states, and formation of the intramolecular charge-transfer (ICT) state. In the Chl-absorbing region, two sets of Chl c2's, and (at least) six Chl a's can be differentiated. With a pigment ratio of 5-6 (Chl a):2 (Chl c2):5-6 (Per):1 Ddx determined from the fit to the RT absorption and 77K RR spectra, sequence comparison of LHCAmp to LHCII, and the diatom LHC, fucoxanthin-chlorophyll-a/c-protein (FCP), a template for the conserved pigment binding sites is proposed, to fill the paucity of structural information in the absence of a crystal structure for LHCAmph.
DOI: 10.1016/j.bbabio.2015.05.006
PubMed: 25982356
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Electronic address: premvard@gmail.com.</nlm:affiliation></affiliation></author><author><name sortKey="Robert, Bruno" sort="Robert, Bruno" uniqKey="Robert B" first="Bruno" last="Robert">Bruno Robert</name><affiliation><nlm:affiliation>Institut de Biologie et de Technologie de Saclay, CEA, and URA 2096, CNRS, CEA-Saclay, 91191 Gif-sur-Yvette CEDEX, France.</nlm:affiliation></affiliation></author><author><name sortKey="Hiller, Roger G" sort="Hiller, Roger G" uniqKey="Hiller R" first="Roger G" last="Hiller">Roger G. Hiller</name><affiliation><nlm:affiliation>Department of Biological Sciences, Macquarie University, NSW 2109, Australia.</nlm:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2015">2015</date><idno type="RBID">pubmed:25982356</idno><idno type="pmid">25982356</idno><idno type="doi">10.1016/j.bbabio.2015.05.006</idno><idno type="wicri:Area/PubMed/Corpus">002860</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">002860</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Pigment organisation in the membrane-intrinsic major light-harvesting complex of Amphidinium carterae: Structural characterisation of the peridinins and chlorophylls a and c2 by resonance Raman spectroscopy and from sequence analysis.</title><author><name sortKey="Premvardhan, Lavanya" sort="Premvardhan, Lavanya" uniqKey="Premvardhan L" first="Lavanya" last="Premvardhan">Lavanya Premvardhan</name><affiliation><nlm:affiliation>Institut de Biologie et de Technologie de Saclay, CEA, and URA 2096, CNRS, CEA-Saclay, 91191 Gif-sur-Yvette CEDEX, France. Electronic address: premvard@gmail.com.</nlm:affiliation></affiliation></author><author><name sortKey="Robert, Bruno" sort="Robert, Bruno" uniqKey="Robert B" first="Bruno" last="Robert">Bruno Robert</name><affiliation><nlm:affiliation>Institut de Biologie et de Technologie de Saclay, CEA, and URA 2096, CNRS, CEA-Saclay, 91191 Gif-sur-Yvette CEDEX, France.</nlm:affiliation></affiliation></author><author><name sortKey="Hiller, Roger G" sort="Hiller, Roger G" uniqKey="Hiller R" first="Roger G" last="Hiller">Roger G. Hiller</name><affiliation><nlm:affiliation>Department of Biological Sciences, Macquarie University, NSW 2109, Australia.</nlm:affiliation></affiliation></author></analytic><series><title level="j">Biochimica et biophysica acta</title><idno type="ISSN">0006-3002</idno><imprint><date when="2015" type="published">2015</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The structures and environments of the protein-bound peridinins (Pers) and chlorophylls (Chls) a/c2 in the membrane-intrinsic major light-harvesting complex of the dinoflagellate Amphidinium carterae (LHCAmph) are characterised using resonance Raman (RR) spectroscopy with 11 excitation wavelengths, at 77K. The excitation-dependent variation in the CC stretching mode (ν1) suggests the presence of three Pers with conjugation lengths over 8 double bonds (dBs), and one diadinoxanthin, between 413.7 and 528.7nm. Two Perred species are revealed on excitation at 550 and 560nm. These Perred species exhibit anomalously low ν1 values, together with notable resonant enhancement of lactone ring-breathing and -deformation modes. To discern protein-specific effects, the RR spectra are compared to that of Per in polar (acetonitrile), polarisable (toluene) and polar-protic (ethanol) solvents. Resonantly enhanced lactone, ring-breathing (942cm(-1)) and ring-deformation (~650cm(-1)), modes are identified both in solution, and in the protein, and discussed in the context of the mixing of the S1 and S2 states, and formation of the intramolecular charge-transfer (ICT) state. In the Chl-absorbing region, two sets of Chl c2's, and (at least) six Chl a's can be differentiated. With a pigment ratio of 5-6 (Chl a):2 (Chl c2):5-6 (Per):1 Ddx determined from the fit to the RT absorption and 77K RR spectra, sequence comparison of LHCAmp to LHCII, and the diatom LHC, fucoxanthin-chlorophyll-a/c-protein (FCP), a template for the conserved pigment binding sites is proposed, to fill the paucity of structural information in the absence of a crystal structure for LHCAmph.</div></front></TEI><pubmed><MedlineCitation Status="In-Data-Review" Owner="NLM"><PMID Version="1">25982356</PMID><DateCreated><Year>2015</Year><Month>08</Month><Day>24</Day></DateCreated><DateRevised><Year>2017</Year><Month>08</Month><Day>17</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0006-3002</ISSN><JournalIssue CitedMedium="Print"><Volume>1847</Volume><Issue>10</Issue><PubDate><Year>2015</Year><Month>Oct</Month></PubDate></JournalIssue><Title>Biochimica et biophysica acta</Title><ISOAbbreviation>Biochim. Biophys. Acta</ISOAbbreviation></Journal><ArticleTitle>Pigment organisation in the membrane-intrinsic major light-harvesting complex of Amphidinium carterae: Structural characterisation of the peridinins and chlorophylls a and c2 by resonance Raman spectroscopy and from sequence analysis.</ArticleTitle><Pagination><MedlinePgn>1187-99</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.bbabio.2015.05.006</ELocationID><ELocationID EIdType="pii" ValidYN="Y">S0005-2728(15)00087-0</ELocationID><Abstract><AbstractText>The structures and environments of the protein-bound peridinins (Pers) and chlorophylls (Chls) a/c2 in the membrane-intrinsic major light-harvesting complex of the dinoflagellate Amphidinium carterae (LHCAmph) are characterised using resonance Raman (RR) spectroscopy with 11 excitation wavelengths, at 77K. The excitation-dependent variation in the CC stretching mode (ν1) suggests the presence of three Pers with conjugation lengths over 8 double bonds (dBs), and one diadinoxanthin, between 413.7 and 528.7nm. Two Perred species are revealed on excitation at 550 and 560nm. These Perred species exhibit anomalously low ν1 values, together with notable resonant enhancement of lactone ring-breathing and -deformation modes. To discern protein-specific effects, the RR spectra are compared to that of Per in polar (acetonitrile), polarisable (toluene) and polar-protic (ethanol) solvents. Resonantly enhanced lactone, ring-breathing (942cm(-1)) and ring-deformation (~650cm(-1)), modes are identified both in solution, and in the protein, and discussed in the context of the mixing of the S1 and S2 states, and formation of the intramolecular charge-transfer (ICT) state. In the Chl-absorbing region, two sets of Chl c2's, and (at least) six Chl a's can be differentiated. With a pigment ratio of 5-6 (Chl a):2 (Chl c2):5-6 (Per):1 Ddx determined from the fit to the RT absorption and 77K RR spectra, sequence comparison of LHCAmp to LHCII, and the diatom LHC, fucoxanthin-chlorophyll-a/c-protein (FCP), a template for the conserved pigment binding sites is proposed, to fill the paucity of structural information in the absence of a crystal structure for LHCAmph.</AbstractText><CopyrightInformation>Copyright © 2015 Elsevier B.V. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Premvardhan</LastName><ForeName>Lavanya</ForeName><Initials>L</Initials><AffiliationInfo><Affiliation>Institut de Biologie et de Technologie de Saclay, CEA, and URA 2096, CNRS, CEA-Saclay, 91191 Gif-sur-Yvette CEDEX, France. Electronic address: premvard@gmail.com.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Robert</LastName><ForeName>Bruno</ForeName><Initials>B</Initials><AffiliationInfo><Affiliation>Institut de Biologie et de Technologie de Saclay, CEA, and URA 2096, CNRS, CEA-Saclay, 91191 Gif-sur-Yvette CEDEX, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Hiller</LastName><ForeName>Roger G</ForeName><Initials>RG</Initials><AffiliationInfo><Affiliation>Department of Biological Sciences, Macquarie University, NSW 2109, Australia.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2015</Year><Month>05</Month><Day>14</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Biochim Biophys Acta</MedlineTA><NlmUniqueID>0217513</NlmUniqueID><ISSNLinking>0006-3002</ISSNLinking></MedlineJournalInfo><CitationSubset>IM</CitationSubset><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Chlorophyll c(2)</Keyword><Keyword MajorTopicYN="N">Peridinin lactone ring modes</Keyword><Keyword MajorTopicYN="N">Pigment organisation</Keyword><Keyword MajorTopicYN="N">Sequence analysis</Keyword><Keyword MajorTopicYN="N">Structure</Keyword><Keyword MajorTopicYN="N">light-harvesting complex</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2015</Year><Month>01</Month><Day>26</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2015</Year><Month>05</Month><Day>05</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2015</Year><Month>05</Month><Day>06</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2015</Year><Month>5</Month><Day>19</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2015</Year><Month>5</Month><Day>20</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2015</Year><Month>5</Month><Day>20</Day><Hour>6</Hour><Minute>1</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">25982356</ArticleId><ArticleId IdType="pii">S0005-2728(15)00087-0</ArticleId><ArticleId IdType="doi">10.1016/j.bbabio.2015.05.006</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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