Source:http://linkedlifedata.com/resource/pubmed/id/10818791
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
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pubmed:dateCreated |
2000-6-5
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pubmed:abstractText |
Transformation among the aggregate forms of bacteriochlorophyll (BChl) c characterized by the wavelength of the Qy absorption, i.e. the dimer (B675), B705, B720 and B745, was traced by electronic-absorption spectroscopy for each of the isomers including R[E,E], R[P,E], R[I,E], S[P,E] and S[I,E] suspended in the mixtures of methylene chloride and n-hexane. A combination of NMR spectroscopy determining the structural motifs and calculation of the shift of the Qy absorption reflecting the long-range transition dipole-transition dipole interactions among the macrocycles in the entire aggregate structures proposed the following models: B705d (B705d'), a linear array of straight (inclined) columns consisting of a pair of the piggyback dimers; B720d and B745d, an assembly of two and five shifted-inclined columns consisting of more than six piggyback dimers; and B720m and B745m, an assembly of one and two parallel stepwise stacking of approximately 30 monomers. Calculations of the steric energies rationalized two different pathways of transformations: the dimer-->B705d (B705d')-->B720d-->B745d for the R isomers; and the monomer-->(B720m)-->B745m for the S isomers. Addition of S[I,E] seems to trigger the B745d-->B745m transformation of the R isomers.
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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 |
May
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pubmed:issn |
0031-8655
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
71
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
596-609
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:10818791-Bacterial Proteins,
pubmed-meshheading:10818791-Bacteriochlorophylls,
pubmed-meshheading:10818791-Chlorobi,
pubmed-meshheading:10818791-Electrons,
pubmed-meshheading:10818791-Magnetic Resonance Spectroscopy,
pubmed-meshheading:10818791-Protein Conformation,
pubmed-meshheading:10818791-Stereoisomerism
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pubmed:year |
2000
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pubmed:articleTitle |
Structural transformation among the aggregate forms of bacteriochlorophyll c as determined by electronic-absorption and NMR spectroscopies: dependence on the stereoisomeric configuration and on the bulkiness of the 8-C side chain.
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pubmed:affiliation |
Faculty of Science, Kwansei Gakuin University, Nishinomiya, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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