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Resonance Raman spectroscopy of xanthophylls in pigment mutant thylakoid membranes of pea
Author(s) -
Andreeva Atanaska,
Stoitchkova Katerina,
Busheva Mira,
Apostolova Emilia,
Várkonyi Zsuzsanna,
Garab Gyözö
Publication year - 2004
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.20050
Subject(s) - neoxanthin , xanthophyll , thylakoid , chemistry , lutein , resonance raman spectroscopy , raman spectroscopy , pigment , mutant , biophysics , chlorophyll , chloroplast , biochemistry , zeaxanthin , carotenoid , biology , organic chemistry , optics , physics , gene
Low‐temperature resonance Raman spectroscopy was used to study the changes in the molecular structure and configuration of the major xanthophylls in thylakoid membranes isolated from mutants of pea with modified pigment content and altered structural organization of their pigment–protein complexes. The Raman spectra contained four known groups of bands, ν 1 –ν 4 , which could be assigned to originate mainly from the long wavelength absorbing lutein and neoxanthin upon 514.5 nm and at 488 nm excitations, respectively. The overall configuration of these bound xanthophyll molecules in the mutants appeared to be similar to the wild type, and the configuration in the wild type was almost identical with that in the isolated main chlorophyll a / b light harvesting protein complex of photosystem II (LHCII). Significant differences were found mainly in the region of ν 4 (around 960 cm −1 ), which suggest that the macroorganization of PS II–LHCII supercomplexes and/or of the LHCII‐only domains are modified in the mutants compared to the wild type. © 2004 Wiley Periodicals, Inc. Biopolymers, 2004