Linked Life Data

111711

Source:http://linkedlifedata.com/resource/pubmed/id/111711

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1979-10-17
pubmed:abstractText
Using fourth derivative analysis, differences between room and low temperature absorption spectra were studied. The positions of most absorption bands of the water-soluble, accessory pigment complex, the phycobilisome, remained unchanged after cooling. The stability of the wavelength positions of chlorophyll a forms in vivo as a function of temperature (Gulyaev, B.A. and Litvin, F.F. (1967) Biofizika 12, 845--854) was generally confirmed. The wavelength positions of all chlorophyll a forms in the P-700 chlorophyll a protein complex were unchanged when the preparations were cooled to -196 degrees C. Likewise, with other chlorophyll-containing materials: the light-harvesting chlorophyll a/b protein complex and the thylakoids of higher plants, algae, and cyanobacteria, the wavelengths positions of most chlorophyll a forms were stable upon cooling. An exception was a 680 nm chlorophyll a band which was generally split at low temperature into two bands with the materials investigated. An interpretation of the multiplicity of chlorophyll spectral forms and the spectral changes induced by cooling for these forms is given using exciton theory and the energy-coupling variation of chlorophyll a molecules.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
14
pubmed:volume
547
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
398-409
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
1979
pubmed:articleTitle
Analysis of absorption spectra changes induced by temperature lowering on phycobilisomes, thylakoids and chlorophyll-protein complexes.
pubmed:publicationType
Journal Article, Comparative Study