Pigment structure in the light-harvesting protein of the siphonous green alga Codium fragile.


Journal

Biochimica et biophysica acta. Bioenergetics
ISSN: 1879-2650
Titre abrégé: Biochim Biophys Acta Bioenerg
Pays: Netherlands
ID NLM: 101731706

Informations de publication

Date de publication:
01 05 2021
Historique:
received: 13 10 2020
revised: 11 01 2021
accepted: 21 01 2021
pubmed: 6 2 2021
medline: 28 9 2021
entrez: 5 2 2021
Statut: ppublish

Résumé

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.

Identifiants

pubmed: 33545114
pii: S0005-2728(21)00017-7
doi: 10.1016/j.bbabio.2021.148384
pii:
doi:

Substances chimiques

Light-Harvesting Protein Complexes 0
Photosystem II Protein Complex 0
Pigments, Biological 0
Xanthophylls 0
Chlorophyll 1406-65-1
siphonaxanthin 28526-44-5
chlorophyll b 5712ZB110R
Chlorophyll A YF5Q9EJC8Y

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

148384

Informations de copyright

Copyright © 2021 Elsevier B.V. All rights reserved.

Auteurs

Simona Streckaite (S)

Université Paris-Saclay, CEA, CNRS, Institute for Integrative Biology of the Cell (I2BC), 91198 Gif-sur-Yvette, France.

Manuel J Llansola-Portoles (MJ)

Université Paris-Saclay, CEA, CNRS, Institute for Integrative Biology of the Cell (I2BC), 91198 Gif-sur-Yvette, France.

Andrew A Pascal (AA)

Université Paris-Saclay, CEA, CNRS, Institute for Integrative Biology of the Cell (I2BC), 91198 Gif-sur-Yvette, France.

Cristian Ilioaia (C)

Université Paris-Saclay, CEA, CNRS, Institute for Integrative Biology of the Cell (I2BC), 91198 Gif-sur-Yvette, France.

Andrew Gall (A)

Université Paris-Saclay, CEA, CNRS, Institute for Integrative Biology of the Cell (I2BC), 91198 Gif-sur-Yvette, France.

Soichiro Seki (S)

Osaka City University, Graduate School of Science, Sumiyoshi Ku, 3-3-138 Sugimoto, Osaka 5588585, Japan.

Ritsuko Fujii (R)

Osaka City University, Graduate School of Science, Sumiyoshi Ku, 3-3-138 Sugimoto, Osaka 5588585, Japan; Osaka City University, The OCU Research Center for Artificial Photosynthesis, Sumiyoshi Ku, 3-3-138 Sugimoto, Osaka 5588585, Japan.

Bruno Robert (B)

Université Paris-Saclay, CEA, CNRS, Institute for Integrative Biology of the Cell (I2BC), 91198 Gif-sur-Yvette, France. Electronic address: bruno.robert@cea.fr.

Articles similaires

Photosynthesis Ribulose-Bisphosphate Carboxylase Carbon Dioxide Molecular Dynamics Simulation Cyanobacteria
Semiconductors Photosynthesis Polymers Carbon Dioxide Bacteria

A molecular mechanism for bright color variation in parrots.

Roberto Arbore, Soraia Barbosa, Jindich Brejcha et al.
1.00
Animals Feathers Pigmentation Parrots Aldehyde Dehydrogenase

Structural basis for molecular assembly of fucoxanthin chlorophyll

Koji Kato, Yoshiki Nakajima, Jian Xing et al.
1.00
Diatoms Photosystem I Protein Complex Chlorophyll Binding Proteins Cryoelectron Microscopy Light-Harvesting Protein Complexes

Classifications MeSH