PROTEIN-PHOSPHORYLATION AND MG-2+ INFLUENCE LIGHT HARVESTING AND ELECTRON-TRANSPORT IN CHLOROPLAST THYLAKOID MEMBRANE MATERIAL CONTAINING ONLY THE CHLOROPHYLL-A/B-BINDING LIGHT-HARVESTING COMPLEX OF PHOTOSYSTEM-II AND PHOTOSYSTEM-I

A material containing only photosystem I (PSI) and the chlorophyll-a/b-binding light-harvesting complex of PSII (LHC-II) has been isolated from the chloroplast thylakoid membrane by solubilization with Triton X-100. Fluorescence spectroscopy shows that, within the material, LHC-II is coupled to PSI for excitation-energy transfer and that this coupling is decreased by the presence of Mg2+, which also decreased PSI electron transport specifically at limiting light intensity. Inclusion of phosphorylated LHC-II within the material did not alter its structure, but gave decreased energy transfer to PSI and inhibition of electron transport which was independent of light intensity, implying effects of phosphorylation on both light harvesting and directly on electron transport. Inclusion of Mg2+ within the phosphorylated material gave decreased energy transfer, but slightly increased PSI electron transport. A cation-induced direct promotion of PSI electron transport was also observed in isolated PSI particles. The PSI/LHC-II material represents a model system for examining protein interactions during light-state adaptations and the possibility that LHC-II can contribute to the antenna of PSI in light state 2 in vivo is discussed.