2019/07/09 by Peter R. Bos, Peter Bos, Anniek Oosterwijk +7 · 27 citations
Agricultural and Biological Sciences · Biochemistry, Genetics and Molecular Biology · Chemistry · Neuroscience · #Arabidopsis thaliana #Biochemistry #Biology #Biophysics #Botany #Chemistry #Chloroplast #Light effects on plants #Mutant #Photochemistry #Photoreceptor and optogenetics research #Photosynthesis #Photosynthetic Processes and Mechanisms #Photosystem #Photosystem I #Photosystem II #Thylakoid
paper · pdf · doi:10.1016/j.bbabio.2019.07.001
published in Biochimica et Biophysica Acta (BBA) - Bioenergetics 1860(8), 651-658 (Elsevier BV)
openalex publication_date 2019/07/09 · openalex created_date 2025/10/10 · openalex updated_date 2026/08/01
Light drives photosynthesis. In plants it is absorbed by light-harvesting antenna complexes associated with Photosystem I (PSI) and photosystem II (PSII). As PSI and PSII work in series, it is important that the excitation pressure on the two photosystems is balanced. When plants are exposed to illumination that overexcites PSII, a special pool of the major light-harvesting complex LHCII is phosphorylated and moves from PSII to PSI (state 2). If instead PSI is over-excited the LHCII complex is dephosphorylated and moves back to PSII (state 1). Recent findings have suggested that LHCII might also transfer energy to PSI in state 1. In this work we used a combination of biochemistry and (time-resolved) fluorescence spectroscopy to investigate the PSI antenna size in state 1 and state 2 for Arabidopsis thaliana. Our data shows that 0.7 ± 0.1 unphosphorylated LHCII trimers per PSI are present in the stroma lamellae of state-1 plants. Upon transition to state 2 the antenna size of PSI in the stroma membrane increases with phosphorylated LHCIIs to a total of 1.2 ± 0.1 LHCII trimers per PSI. Both phosphorylated and unphosphorylated LHCII function as highly efficient PSI antenna.