The light reactions of oxygenic photosynthesis are performed by protein complexes embedded in the lipid bilayer of thylakoid membranes (TMs). Bilayers provide optimal conditions for the build-up of the proton motive force (pmf) and ATP synthesis. However, functional plant TMs, besides the bilayer, contain an inverted hexagonal (HII) phase and isotropic phases, a lipid polymorphism due to their major, non-bilayer lipid species, monogalactosyldiacylglycerol (MGDG). The lipid phase behavior of TMs is explained within the framework of the Dynamic Exchange Model (DEM), an extension of the fluid-mosaic model. DEM portrays the bilayer phase as inclusions between photosynthetic supercomplexes - characterized by compromised membrane impermeability and restricted sizes inflicted by the segregation propensity of lipid molecules, safe-guarding the high protein density of TMs. Isotropic phases mediate membrane fusions and are associated with the lumenal lipocalin-like enzyme, violaxanthin de-epoxidase. Stromal-side proteins surrounded by lipids give rise to the HII phase. These features instigate experimentally testable hypotheses: (i) non-bilayer phases mediate functional sub-compartmentalization of plant chloroplasts - a quasi-autonomous energization and ATP synthesis of each granum-stroma TM assembly; and (ii) the generation and utilization of pmf depend on hydrated protein networks and proton-conducting pathways along membrane surfaces - rather than on strict impermeability of the bilayer.

• MeSH
• Models, Biological MeSH
• Photosynthesis MeSH
• Galactolipids metabolism   MeSH
• Lipid Bilayers metabolism   MeSH
• Plants * metabolism   MeSH
• Thylakoids * metabolism   chemistry   MeSH
• Publication type
• Journal Article MeSH
• Review MeSH
• Names of Substances
• Galactolipids MeSH
• Lipid Bilayers MeSH

Light quality significantly influences plant metabolism, growth and development. Recently, we have demonstrated that leaves of barley and other plant species grown under monochromatic green light (500-590 nm) accumulated a large pool of chlorophyll a (Chl a) intermediates with incomplete hydrogenation of their phytyl chains. In this work, we studied accumulation of these geranylgeranylated Chls a and b in pigment-protein complexes (PPCs) of Arabidopsis plants acclimated to green light and their structural-functional consequences on the photosynthetic apparatus. We found that geranylgeranylated Chls are present in all major PPCs, although their presence was more pronounced in light-harvesting complex II (LHCII) and less prominent in supercomplexes of photosystem II (PSII). Accumulation of geranylgeranylated Chls hampered the formation of PSII and PSI super- and megacomplexes in the thylakoid membranes as well as their assembly into chiral macrodomains; it also lowered the temperature stability of the PPCs, especially that of LHCII trimers, which led to their monomerization and an anomaly in the photoprotective mechanism of non-photochemical quenching. Role of geranylgeranylated Chls in adverse effects on photosynthetic apparatus of plants acclimated to green light is discussed.

• Keywords
• Arabidopsis thaliana, Chlorophylls, Green light, Structure and function of photosystem II, Thermal stability, Thylakoid membrane,
• MeSH
• Adaptation, Ocular physiology   MeSH
• Arabidopsis metabolism   MeSH
• Chlorophyll metabolism   MeSH
• Photosystem II Protein Complex metabolism   MeSH
• Prenylation MeSH
• Light-Harvesting Protein Complexes metabolism   MeSH
• Publication type
• Journal Article MeSH
• Names of Substances
• Chlorophyll MeSH
• Photosystem II Protein Complex MeSH
• Light-Harvesting Protein Complexes MeSH