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      Excitation of photosystem I by 760 nm femtosecond laser pulses: transient absorption spectra and intermediates

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          Crystal structure of oxygen-evolving photosystem II at a resolution of 1.9 Å.

          Photosystem II is the site of photosynthetic water oxidation and contains 20 subunits with a total molecular mass of 350 kDa. The structure of photosystem II has been reported at resolutions from 3.8 to 2.9 Å. These resolutions have provided much information on the arrangement of protein subunits and cofactors but are insufficient to reveal the detailed structure of the catalytic centre of water splitting. Here we report the crystal structure of photosystem II at a resolution of 1.9 Å. From our electron density map, we located all of the metal atoms of the Mn(4)CaO(5) cluster, together with all of their ligands. We found that five oxygen atoms served as oxo bridges linking the five metal atoms, and that four water molecules were bound to the Mn(4)CaO(5) cluster; some of them may therefore serve as substrates for dioxygen formation. We identified more than 1,300 water molecules in each photosystem II monomer. Some of them formed extensive hydrogen-bonding networks that may serve as channels for protons, water or oxygen molecules. The determination of the high-resolution structure of photosystem II will allow us to analyse and understand its functions in great detail. ©2011 Macmillan Publishers Limited. All rights reserved
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            Structure of the protein subunits in the photosynthetic reaction centre of Rhodopseudomonas viridis at 3Å resolution

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              Three-dimensional structure of cyanobacterial photosystem I at 2.5 A resolution.

              Life on Earth depends on photosynthesis, the conversion of light energy from the Sun to chemical energy. In plants, green algae and cyanobacteria, this process is driven by the cooperation of two large protein-cofactor complexes, photosystems I and II, which are located in the thylakoid photosynthetic membranes. The crystal structure of photosystem I from the thermophilic cyanobacterium Synechococcus elongatus described here provides a picture at atomic detail of 12 protein subunits and 127 cofactors comprising 96 chlorophylls, 2 phylloquinones, 3 Fe4S4 clusters, 22 carotenoids, 4 lipids, a putative Ca2+ ion and 201 water molecules. The structural information on the proteins and cofactors and their interactions provides a basis for understanding how the high efficiency of photosystem I in light capturing and electron transfer is achieved.
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                Author and article information

                Journal
                Journal of Physics B: Atomic, Molecular and Optical Physics
                J. Phys. B: At. Mol. Opt. Phys.
                IOP Publishing
                0953-4075
                1361-6455
                September 14 2017
                September 14 2017
                August 10 2017
                : 50
                : 17
                : 174001
                Article
                10.1088/1361-6455/aa824b
                fc0e9b41-0cef-4a1e-95a2-bdf782f7af69
                © 2017

                http://iopscience.iop.org/info/page/text-and-data-mining

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