RRC ID 69307
Author Streckaite S, Llansola-Portoles MJ, Pascal AA, Ilioaia C, Gall A, Seki S, Fujii R, Robert B.
Title Pigment structure in the light-harvesting protein of the siphonous green alga Codium fragile.
Journal Biochim Biophys Acta Bioenerg
Abstract The siphonaxanthin-siphonein-chlorophyll-a/b-binding protein (SCP), a trimeric light-harvesting complex isolated from photosystem II of the siphonous green alga Codium fragile, binds the carotenoid siphonaxanthin (Sx) and/or its ester siphonein in place of lutein, in addition to chlorophylls a/b and neoxanthin. SCP exhibits a higher content of chlorophyll b (Chl-b) than its counterpart in green plants, light-harvesting complex II (LHCII), increasing the relative absorption of blue-green light for photosynthesis. Using low temperature absorption and resonance Raman spectroscopies, we reveal the presence of two non-equivalent Sx molecules in SCP, and assign their absorption peaks at 501 and 535 nm. The red-absorbing Sx population exhibits a significant distortion that is reminiscent of lutein 2 in trimeric LHCII. Unexpected enhancement of the Raman modes of Chls-b in SCP allows an unequivocal description of seven to nine non-equivalent Chls-b, and six distinct Chl-a populations in this protein.
Volume 1862(5)
Pages 148384
Published 2021-5-1
DOI 10.1016/j.bbabio.2021.148384
PII S0005-2728(21)00017-7
PMID 33545114
MeSH Chlorophyll / metabolism* Chlorophyll A / metabolism* Chlorophyta / metabolism* Light-Harvesting Protein Complexes / metabolism* Photosynthesis Photosystem II Protein Complex / metabolism* Pigments, Biological / chemistry* Pigments, Biological / metabolism Xanthophylls / metabolism*
IF 4.441
Algae Codium fragile