Linked Life Data

7419516

Source:http://linkedlifedata.com/resource/pubmed/id/7419516

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1980-12-18
pubmed:abstractText
alpha-Crustacyanin exhibits two CD extrema with negative and positive bands at 690 and 583 nm in phosphate buffer, respectively. The CD spectrum is interpreted in terms of dipoledipole coupling between the transition moments of the two astaxanthin molecules on each subunit. The CD splitting yields an exciton bandwidth of 2800 cm-1, corresponding to an inter-chromophore distance of ca. 13 A in which the two astaxanthin molecules exist in a dimeric array with a mutual orientation angle of ca. 90 degrees. The SDS denaturation completely abolishes the long wavelength CD splitting, while 2 M NaCl reduces the overall CD intensity without destroying the split CD spectrum. It is suggested that the characteristic CD extrema at 583 and 690 nm arise from the intra-subunit astaxanthin-astaxanthin coupling. The binding site for astaxanthin contains one or more tryptophan residues, as the tryptophan fluorescence is quenched by energy transfer from the tryptophan to the prosthetic group in the native form of the carotenoprotein. The strong red shift (lambda max 487 nm) is probably due to interactions between tryptophan residue(s) and the chromophore molecules through dipole-dipole or partial charge transfer forces.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0021-924X
pubmed:author
pubmed:issnType
Print
pubmed:volume
88
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
663-8
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1980
pubmed:articleTitle
Spectroscopic characterization of alpha-crustacyanin.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't