Evolution and function of light harvesting proteins

被引:99
作者
Buechel, Claudia [1 ]
机构
[1] Goethe Univ Frankfurt, Inst Mol Biosci, Max von Laue Str 9, D-60438 Frankfurt, Germany
关键词
Chlorophyll c; Chromalveolatae; Lhcx; Non-photochemical quenching; Thylakoid structure; DIATOM PHAEODACTYLUM-TRICORNUTUM; FUCOXANTHIN-CHLOROPHYLL-PROTEINS; PHOTOSYSTEM-II ANTENNA; CHARGE-TRANSFER STATE; CYCLOTELLA-CRYPTICA BACILLARIOPHYCEAE; RESONANCE RAMAN-SPECTROSCOPY; EXCITATION-ENERGY TRANSFER; A/C-BINDING POLYPEPTIDES; CHLAMYDOMONAS-REINHARDTII; PERIDININ-CHLOROPHYLL;
D O I
10.1016/j.jplph.2014.04.018
中图分类号
Q94 [植物学];
学科分类号
071001 ;
摘要
Photosynthetic eukaryotes exhibit very different light-harvesting proteins, but all contain membrane-intrinsic light-harvesting complexes (Lhcs), either as additional or sole antennae. Lhcs non-covalently bind chlorophyll a and in most cases another Chl, as well as very different carotenoids, depending on the taxon. The proteins fall into two major groups: The well-defined Lhca/b group of proteins binds typically Chl b and lutein, and the group is present in the 'green lineage'. The other group consists of Lhcr/Lhcf, Lhcz and Lhcx/LhcSR proteins. The former are found in the so-called Chromalveolates, where they mostly bind Chl c and carotenoids very efficient in excitation energy transfer, and in their red algae ancestors. Lhcx/LhcSR are present in most Chromalveolates and in some members of the green lineage as well. Lhcs function in light harvesting, but also in photoprotection, and they influence the organisation of the thylakoid membrane. The different functions of the Lhc subfamilies are discussed in the light of their evolution. (C) 2014 Elsevier GmbH. All rights reserved.
引用
收藏
页码:62 / 75
页数:14
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