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      STRUCTURE AND MEMBRANE ORGANIZATION OF PHOTOSYSTEM II IN GREEN PLANTS

      1 , 1 , 2
      Annual Review of Plant Physiology and Plant Molecular Biology
      Annual Reviews

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          Abstract

          Photosystem II (PSII) is the pigment protein complex embedded in the thylakoid membrane of higher plants, algae, and cyanobacteria that uses solar energy to drive the photosynthetic water-splitting reaction. This chapter reviews the primary, secondary, tertiary, and quaternary structures of PSII as well as the function of its constituent subunits. The understanding of in vivo organization of PSII is based in part on freeze-etched and freeze-fracture images of thylakoid membranes. These images show a resolution of about 40-50 A and so provide information mainly on the localization, heterogeneity, dimensions, and shapes of membrane-embedded PSII complexes. Higher resolution of about 15-40 A has been obtained from single particle images of isolated PSII complexes of defined and differing subunit composition and from electron crystallography of 2-D crystals. Observations are discussed in terms of the oligomeric state and subunit organization of PSII and its antenna components.

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          Crystal structure of an integral membrane light-harvesting complex from photosynthetic bacteria

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            REGULATION OF LIGHT HARVESTING IN GREEN PLANTS.

            When plants are exposed to light intensities in excess of those that can be utilized in photosynthetic electron transport, nonphotochemical dissipation of excitation energy is induced as a mechanism for photoprotection of photosystem II. The features of this process are reviewed, particularly with respect to the molecular mechanisms involved. It is shown how the dynamic properties of the proteins and pigments of the chlorophyll a/b light-harvesting complexes of photosystem II first enable the level of excitation energy to be sensed via the thylakoid proton gradient and subsequently allow excess energy to be dissipated as heat by formation of a nonphotochemical quencher. The nature of this quencher is discussed, together with a consideration of how the variation in capacity for energy dissipation depends on specific features of the composition of the light-harvesting system. Finally, the prospects for future progress in understanding the regulation of light harvesting are assessed.
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              The potential and limitations of neutrons, electrons and X-rays for atomic resolution microscopy of unstained biological molecules.

              Radiation damage is the main problem which prevents the determination of the structure of a single biological macromolecule at atomic resolution using any kind of microscopy. This is true whether neutrons, electrons or X-rays are used as the illumination. For neutrons, the cross-section for nuclear capture and the associated energy deposition and radiation damage could be reduced by using samples that are fully deuterated and 15N-labelled and by using fast neutrons, but single molecule biological microscopy is still not feasible. For naturally occurring biological material, electrons at present provide the most information for a given amount of radiation damage. Using phase contrast electron microscopy on biological molecules and macromolecular assemblies of approximately 10(5) molecular weight and above, there is in theory enough information present in the image to allow determination of the position and orientation of individual particles: the application of averaging methods can then be used to provide an atomic resolution structure. The images of approximately 10,000 particles are required. Below 10(5) molecular weight, some kind of crystal or other geometrically ordered aggregate is necessary to provide a sufficiently high combined molecular weight to allow for the alignment. In practice, the present quality of the best images still falls short of that attainable in theory and this means that a greater number of particles must be averaged and that the molecular weight limitation is somewhat larger than the predicted limit. For X-rays, the amount of damage per useful elastic scattering event is several hundred times greater than for electrons at all wavelengths and energies and therefore the requirements on specimen size and number of particles are correspondingly larger. Because of the lack of sufficiently bright neutron sources in the foreseeable future, electron microscopy in practice provides the greatest potential for immediate progress.
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                Author and article information

                Journal
                Annual Review of Plant Physiology and Plant Molecular Biology
                Annu. Rev. Plant. Physiol. Plant. Mol. Biol.
                Annual Reviews
                1040-2519
                June 1997
                June 1997
                : 48
                : 1
                : 641-671
                Affiliations
                [1 ]Wolfson Laboratories, Department of Biochemistry, Imperial College of Science, Technology and Medicine, London SW7 2AY, United Kingdom
                [2 ]Biophysical Chemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, Groningen, NL-9747 AG The Netherlands
                Article
                10.1146/annurev.arplant.48.1.641
                15012277
                3bd68fdc-24af-4e8b-bbee-afc2797e9ac7
                © 1997
                History

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