5.B.4 The Plant Photosystem I Supercomplex (PSI) Family
Oxygenic photosynthesis is the principal producer of both oxygen and organic matter on Earth. Water, the electron donor for this process, is oxidized to O2 and four protons by PSII. The electrons that have been extracted from water are shuttled through a quinone pool and the cytochrome b6f complex to plastocyanin&151;a small, soluble, copper-containing protein. Solar energy that has been absorbed by PSI induces the translocation of an electron from plastocyanin at the inner face of the membrane (thylakoid lumen) to ferredoxin on the opposite side (stroma). PSI generates the most negative redox potential in nature (-1 V), and thus largely determines the global amount of enthalpy in living systems. The structures of three of the four complexes that catalyse oxygenic photosynthesis in cyanobacteria have been solved at relatively high resolution, and the position of most of their amino acids and prosthetic groups has been defined. Thus, the architecture of oxygenic photosynthesis in cyanobacteria has largely been determined. The structure of the cytochrome b6f complex from chloroplasts of the algae Chlamydomonas reinhardtii has also been solved at high resolution, and has remarkable similarity to the cyanobacterial complex. Two high-resolution structures of light-harvesting complexes of PSII from higher plants have also been published.
All higher organisms on Earth receive energy directly or indirectly from oxygenic photosynthesis performed by plants, green algae and cyanobacteria. Photosystem I (PSI) is a supercomplex of reaction centre and light-harvesting complexes. It generates the most negative redox potential in nature. The structure of plant PSI has been solved at 3.4 Å resolution, revealing 17 protein subunits. The crystal structure of PSI provides a picture at near atomic detail of 11 out of 12 protein subunits of the reaction centre. At this level, 168 chlorophylls (65 assigned with orientations for Qx and Qy transition dipole moments), 2 phylloquinones, 3 Fe4S4 clusters and 5 carotenoids are described. This structural information extends the understanding of the most efficient nano-photochemical machine in nature. (Amunts et al., 2007).
Photosystem I (PSI) is a highly efficient natural light-energy converter, and has diverse light-harvesting antennas associated with its core. In green algae, an extremely large light-harvesting complex I (LHCI) captures and transfers energy to the PSI core. Qin et al. 2019 reported the structure of PSI-LHCI from a green alga Bryopsis corticulans at 3.49 Å resolution, obtained by single-particle cryo-electron microscopy, which revealed 13 core subunits including subunits characteristic of both prokaryotes and eukaryotes, and 10 light-harvesting complex a (Lhca) antennas that form a double semi-ring and an additional Lhca dimer, including a novel 4 TMS Lhca. In total, 244 chlorophylls were identified, some of which were located at key positions for the fast energy transfer.
The plant photosystem I (PSI) supercomplex at 3.4 Å resolution (Amunts et al., 2007). It contains 4 light harvesting chlorophyll a/b binding proteins as well as 13 additional constituents. One helix (TMS) proteins, OHP1 (O81208) amd OHP2 (Q9FEC1) play an essential role in the assembly or stabilization of photosynthetic pigment-protein complexes, especially photosystem reaction centers, in the thylakoid membrane (Beck et al. 2017). PSI consists of two complexes, a reaction center and light-harvesting complex (LHC), which together form the PSI-LHC supercomplex. The crystal structure of plant PSI has been solved with two distinct crystal forms. The first, crystallized at pH 6.5, exhibited P21 symmetry; the second, crystallized at pH 8.5, exhibited P212121 symmetry. The surfaces involved in binding plastocyanin and ferredoxin were identical in both forms. The crystal structure at 2.6 Å resolution revealed 16 subunits, 45 transmembrane helices, and 232 prosthetic groups, including 143 chlorophyll a, 13 chlorophyll b, 27 beta-carotene, 7 lutein, 2 xanthophyll, 1 zeaxanthin, 20 monogalactosyl diglyceride, 7 phosphatidyl diglyceride, 5 digalactosyl diglyceride, 2 calcium ions, 2 phylloquinone, and 3 iron sulfur clusters (Caspy and Nelson 2018). The model revealed detailed interactions, providing mechanisms for excitation energy transfer and its modulation in one of nature's most efficient photochemical machine. The photoexcitation response of cyanobacterial Photosystem I has been studied following reconstitution in proteoliposomes (Niroomand et al. 2017).
Photosystem I of Arabidopsis thaliana
(PsaA-L; Lhca 1-4)
PsaA (chlorophyll a apoprotein; 750 aas; 7 TMSs) (P56766)
PsaB (chlorophyll a apoprotein; 734 aas; 11-12 TMSs) (P56767)
PsaC (iron sulfur center protein) (P62090)
PsaD (Reaction Center Subunit II) (Q9SA56)
PsaE (Reaction Center Subunit IV) (Q9S714)
PsaF (Reaction Center Subunit III) (Q9SUI8)
PsaG (Reaction Center Subunit V) (Q9S7N7)
PsaH (Reaction Center Subunit VI) (Q9SUI6)
PsaI (Reaction Center Subunit VIII) (P56768)
PsaJ (Reaction Center Subunit IX) (P56769)
PsaK (Reaction Center Subunit X) (Q9SUI5)
PsaL (Reaction Center Subunit XI) (Q9SUI4)
Lhca1 (225 aas; 1-2 TMSs) (ABD37878)
Lhca2 (257 aas; 1-2 TMSs) (Q9SYW8)
Lhca3 (273 aas; 1-2 TMSs) (Q43381)
Lhca4 (244 aas; 2-4 TMSs) (Q6YWJ7)