rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1-2
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pubmed:dateCreated |
2001-6-21
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pubmed:abstractText |
Selective destruction of the strongly dichroic red-shifted chlorophyll form (C709 nm) in photosystem I (PSI) trimers from Spirulina, by either non-selective high intensity illumination (photobleaching) or incubation with low concentrations of Triton X-100 is accompanied by changes in the circular dichroism spectrum of the same amplitude and of opposite sign at 677 nm. The data are interpreted in terms of a dimeric chlorophyll structure with excitonic bands at these two wavelengths. Similar photobleaching experiments with PSI-200 from maize also suggest the presence of bulk antenna/red form excitonic interactions.
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
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pubmed:chemical |
|
pubmed:status |
MEDLINE
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pubmed:month |
Jun
|
pubmed:issn |
0014-5793
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
499
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
112-5
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pubmed:dateRevised |
2003-11-14
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pubmed:meshHeading |
pubmed-meshheading:11418123-Chlorophyll,
pubmed-meshheading:11418123-Circular Dichroism,
pubmed-meshheading:11418123-Color,
pubmed-meshheading:11418123-Cyanobacteria,
pubmed-meshheading:11418123-Dimerization,
pubmed-meshheading:11418123-Light,
pubmed-meshheading:11418123-Light-Harvesting Protein Complexes,
pubmed-meshheading:11418123-Octoxynol,
pubmed-meshheading:11418123-Photosynthetic Reaction Center Complex Proteins,
pubmed-meshheading:11418123-Photosystem I Protein Complex,
pubmed-meshheading:11418123-Protein Binding,
pubmed-meshheading:11418123-Zea mays
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pubmed:year |
2001
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pubmed:articleTitle |
CD spectroscopy provides evidence for excitonic interactions involving red-shifted chlorophyll forms in photosystem I.
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pubmed:affiliation |
Centro C.N.R. Biologia Cellulare e Molecolare delle Piante, Dipartimento di Biologia, Università di Milano, Italy.
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pubmed:publicationType |
Journal Article
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