Resonance Raman spectroscopy of a light-harvesting protein from the brown alga Laminaria saccharina.

Détails

ID Serval
serval:BIB_ADEA1C48A563
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Resonance Raman spectroscopy of a light-harvesting protein from the brown alga Laminaria saccharina.
Périodique
Biochemistry
Auteur(s)
Pascal A.A., Caron L., Rousseau B., Lapouge K., Duval J., Robert B.
ISSN
0006-2960 (Print)
ISSN-L
0006-2960
Statut éditorial
Publié
Date de publication
1998
Volume
37
Numéro
8
Pages
2450-2457
Langue
anglais
Résumé
Resonance Raman spectroscopy of an antenna protein from the brown alga Laminaria saccharina has been used to investigate the molecular structure of this light-harvesting complex (LHC) at the level of its bound pigments, chlorophylls (chl) a and c and the xanthophyll fucoxanthin. Evidence has been obtained for the conservation of pigment structure during the isolation procedure used. Six chl a and two chl c molecules are indicated from the positions and relative contributions of stretching modes of their keto-carbonyl groups. Of special interest is the presence of a population of chls a having a protein-binding conformation highly similar to that seen in antenna proteins from higher plants, possibly indicating a common structural motif within this extended gene family. The eight fucoxanthin molecules evidenced are all in the all-trans conformation; however, one or two have a highly twisted configuration. The results are discussed in terms of common and varying structural features of LHCs in higher plants and algae.
Mots-clé
Binding Sites, Carotenoids/analogs & derivatives, Carotenoids/chemistry, Chlorophyll/chemistry, Laminaria/chemistry, Light-Harvesting Protein Complexes, Molecular Conformation, Photosynthetic Reaction Center Complex Proteins/chemistry, Protein Conformation, Spectrum Analysis, Raman, Xanthophylls
Pubmed
Web of science
Création de la notice
28/11/2011 16:09
Dernière modification de la notice
20/08/2019 16:17
Données d'usage