Structural analysis and comparison of light-harvesting complexes I and II

• Published in: Biochimica et biophysica acta. Bioenergetics 2020-04, Vol.1861 (4), p.148038-148038, Article 148038
• Main Authors: Pan, Xiaowei, Cao, Peng, Su, Xiaodong, Liu, Zhenfeng, Li, Mei
• Format: Article
• Language: English
• Subjects: Alga; Amino Acid Sequence; Apoproteins - chemistry; Apoproteins - metabolism; Chlamydomonas reinhardtii - metabolism; Chlorophyll - metabolism; Light-harvesting complex; Light-Harvesting Protein Complexes - chemistry; Light-Harvesting Protein Complexes - metabolism; Models, Molecular; Photosystem I; Photosystem I Protein Complex - metabolism; Photosystem II; Photosystem II Protein Complex - chemistry; Photosystem II Protein Complex - metabolism; Plant; Protein Subunits - chemistry; Protein Subunits - metabolism; Rhodophyta - metabolism; Structure
• ISSN: 0005-2728; 1879-2650
• DOI: 10.1016/j.bbabio.2019.06.010

Photosynthesis is a fundamental biological process involving the conversion of solar energy into chemical energy. The initial photochemical and photophysical events of photosynthesis are mediated by photosystem II (PSII) and photosystem I (PSI). Both PSII and PSI are multi-subunit supramolecular machineries composed of a core complex and a peripheral antenna system. The antenna system serves to capture light energy and transfer it to the core efficiently. Both PSII and PSI in the green lineage (plants and green algae) and PSI in red algae have an antenna system comprising a series of chlorophyll- and carotenoid-binding membrane proteins belonging to the light-harvesting complex (LHC) superfamily, including LHCII and LHCI. However, the antenna size and subunit composition vary considerably in the two photosystems from diverse organisms. On the basis of the plant and algal LHCII and LHCI structures that have been solved by X-ray crystallography and single-particle cryo-electron microscopy we review the detailed structural features and characteristic pigment properties of these LHCs in PSII and PSI. This article is part of a Special Issue entitled Light harvesting, edited by Dr. Roberta Croce. •Structures and locations of light-harvesting complexes in plant PSII are described.•Architectures, locations and the interactions of light-harvesting complexes in plant and algal PSI are reviewed.•Structural comparison of apoproteins of the light-harvesting complexes from PSII and PSI are summarized.•Arrangement of pigments in the light-harvesting complexes from PSII and PSI are compared.