Here, we present data that fully characterize the structural and functional properties of PSII complexes in isolated PSII-enriched membranes from C. reinhardtii. The function of D1‐H332 in Photosystem II electron transport studied by thermoluminescence and chlorophyll fluorescence in site‐directed mutants of Synechocystis 6803 Yagut Allahverdiyeva Institute of Plant Biology, Biological Research Center, Szeged, Hungary Res. Loss-of-function of OsSTN8 suppresses the Photosystem II core protein phosphorylation and interferes with the Photosystem II repair mechanism in rice (Oryza sativa). Chlorophyll is the pigment involved in capturing light energy. Biochimica et Biophysica Acta (BBA) - Bioenergetics 2008 , 1777 (9) , 1184-1194. and a proton gradient subsequently used for ATP formation. PSI generates the most negative redox potential in nature and largely determines the global amount of enthalpy in living systems. Plant The semiquinone is thermodynamically stable and has a relatively high potential. The stripped protons contribute to a membrane electrochemical potential before combining with the stripped electrons to make chemical bonds and releasing O2 for powering respiratory metabolisms. In: Barber J., Malkin R. (eds) Techniques and New Developments in Photosynthesis Research. This minimizes back … The Plant Journal 2013 , 76 (4) , … Photosynth. High-light illumination of photosynthetic organisms stimulates the production of singlet oxygen by photosystem II (PSII) and causes photo-oxidative stress. Springer DOI www.annualreviews.org • Structure/Function of Oxygenic Photosystems 523 Annu. Photosystem I (PS I) and photosystem II (PS II) are two multi-subunit membrane-protein complexes involved in oxygenic photosynthesis. Biochemistry 52 , 6646 – 6652 ( 2013 ). Photosystem II is the first link in the chain of photosynthesis. 10.1111/tpj.12331 [] [] Nickelsen J. 72: 131 – 146. Front. Photosystem I and II are two types of reaction centers found in thylakoid membranes, which are the sites of protein synthesis located in the leaves of plants. Structure/Function/Dynamics of Photosystem II Plastoquinone Binding Sites Author(s): Maya D. Lambreva , Daniela Russo , Fabio Polticelli , Viviana Scognamiglio , Amina Antonacci , Veranika Zobnina , Gaetano Campi , Giuseppina Rea . Photosystem II Dimer Created by: Rebecca Babski Photosystem II (PDB ID: 3bz1) is a homodimer protein complex that is present in the thylakoid membrane of many photosynthesizing organisms including plants, green algae, and cyanobacteria (1). Core Composition in the PSI is made up of two subunits which are psaA and psaB, and PS II is made up of two subunits made up of D1 and D2. One of the components of the core complex of photosystem II (PSII). 2014 Mar;79(3):185-96. doi: 10.1134/S0006297914030031. In the PSII reaction centre, singlet oxygen is generated by the interaction of molecular oxygen with the excited triplet state of chlorophyll (Chl). HCF244 was identified by coexpression analysis of HCF173, which encodes a protein that is also necessary for psbA translational initiation and in addition for stabilization of this messenger RNA. Photosystem II (PSII)-enriched membranes retain the original PSII architecture in contrast to PSII cores or PSII supercomplexes, which are usually isolated from Chlamydomonas reinhardtii. Photosystem II (of cyanobacteria and green plants) is composed of around 20 subunits (depending on the organism) as well as other accessory, light-harvesting proteins. Downloaded from arjournals.annualreviews.org by TEL … 76, 675–686. The primary function of the photosystem I in NADPH synthesis, where it receives the electrons from PS II, and the photosystem II is in the hydrolysis of water and ATP synthesis. C-terminal processing of reaction center protein D1 is essential for the function and assembly of photosystem II in Arabidopsis. Photosystem II (PSII) is a membrane‐embedded protein–pigment complex, containing more than 20 subunits and approximately 100 cofactors. BERTIL ANDERSSON, STENBJÖRN STYRING, Photosystem II: Molecular Organization, Function, and Acclimation, Current Topics in Bioenergetics, 10.1016/B978-0-12-152516-3.50005-X, (1-81), (1991). , Crystal structure of Psb31, a novel extrinsic protein of photosystem II from a marine centric diatom and implications for its binding and function. Keywords: chloroplast, photosynthesis, structure, photosystem II protein complex, protein complex Citation: Gao J, Wang H, Yuan Q and Feng Y (2018) Structure and Function of the Photosystem Supercomplexes. 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