Linked Life Data

7918397

Source:http://linkedlifedata.com/resource/pubmed/id/7918397

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
39
pubmed:dateCreated
1994-11-8
pubmed:abstractText
Incubation of the D1-D2-cytochrome b559 complex with Triton X-100 modified the protein secondary structure, caused significant spectral modifications, and reduced the formation of light-induced spin-polarized triplet electron paramagnetic resonance (EPR) signal. After 24 h of incubation, the absorption spectrum shifted from 675.5 to 671.5 nm and the fluorescence spectrum shifted from 682 to 672 nm. These shifts were accompanied by an increase in the chlorophyll fluorescence yield and by decreases in the intensity of the circular dichroism in the red region and the secondary electron transport activity. The intensity of the light-induced triplet EPR signal was also markedly reduced in the same experimental conditions. Substitution of dodecyl beta-maltoside for Triton X-100 reversed all the above-mentioned parameters to the values exhibited by the native D1-D2-Cyt b559 complex, including the characteristic triplet EPR signal. We concluded that all observed changes were due to the destruction of P680 with Triton X-100 and to the reestablishment of P680 in the presence of dodecyl beta-maltoside. The easier but certainly not the only possible explanation to all these phenomena is to consider a dimeric structure for P680, at least in its ground state, where interactions take place within the two dimeric chromophores and with the apoprotein. Such a dimeric structure would be very sensitive to small modifications of the P680 domain, which convert the dimer absorbing at 680 into two chlorophyll monomers absorbing near 670 nm. The dodecyl beta-maltoside reestablished the structure of the native P680 domain.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
4
pubmed:volume
33
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
11798-804
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:7918397-Carotenoids, pubmed-meshheading:7918397-Chlorophyll, pubmed-meshheading:7918397-Circular Dichroism, pubmed-meshheading:7918397-Cytochrome b Group, pubmed-meshheading:7918397-Electron Spin Resonance Spectroscopy, pubmed-meshheading:7918397-Light-Harvesting Protein Complexes, pubmed-meshheading:7918397-Octoxynol, pubmed-meshheading:7918397-Photosynthetic Reaction Center Complex Proteins, pubmed-meshheading:7918397-Photosystem II Protein Complex, pubmed-meshheading:7918397-Plant Proteins, pubmed-meshheading:7918397-Protein Denaturation, pubmed-meshheading:7918397-Protein Structure, Secondary, pubmed-meshheading:7918397-Spectrometry, Fluorescence, pubmed-meshheading:7918397-Spectrophotometry, pubmed-meshheading:7918397-Tryptophan, pubmed-meshheading:7918397-Vegetables
pubmed:year
1994
pubmed:articleTitle
Detergent-induced reversible denaturation of the photosystem II reaction center: implications for pigment-protein interactions.
pubmed:affiliation
Estación Experimental de Aula Dei, CSIC, Zaragoza, Spain.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't