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DENSITY FUNCTIONAL THEORY --- PHOTOSYSTEM II --- OXYGENASES (MESH) --- DENSITY FUNCTIONAL THEORY --- PHOTOSYSTEM II --- OXYGENASES (MESH)
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Phytochemistry. Phytobiochemistry --- PLANT BIOCHEMISTRY --- AMINO ACIDS --- PROTEINS --- NUCLEIC ACIDS --- THYLAKOIDS --- PHOTOSYSTEM I --- PHOTOSYSTEM II --- ALGAE --- CHROMOPROTEINS --- PHYTOCHROME --- CYTOKININS --- PURINES --- PYRIMIDINES --- NUCLEOSIDES --- NUCLEOTIDES --- SEED PROTEINS --- CELL WALLS
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CELL WALLS --- CYTOCHEMISTRY --- ENZYMES --- HANDBOOKS --- PLANTS --- CALCIUM --- POTASSIUM --- SODIUM --- PLANT TISSUES --- IMMUNOCYTOCHEMISTRY --- LECTINS --- PHOTOSYSTEM II --- PHOTOSYSTEM I --- CYTOCHEMISTRY --- PLANTS --- CYTOCHEMISTRY --- CYTOCHEMISTRY --- CYTOCHEMISTRY --- IMMUNOCYTOCHEMISTRY --- CYTOCHEMISTRY --- CYTOCHEMISTRY --- CYTOCHEMISTRY --- CELL WALLS --- CYTOCHEMISTRY --- ENZYMES --- HANDBOOKS --- PLANTS --- CALCIUM --- POTASSIUM --- SODIUM --- PLANT TISSUES --- IMMUNOCYTOCHEMISTRY --- LECTINS --- PHOTOSYSTEM II --- PHOTOSYSTEM I --- CYTOCHEMISTRY --- PLANTS --- CYTOCHEMISTRY --- CYTOCHEMISTRY --- CYTOCHEMISTRY --- IMMUNOCYTOCHEMISTRY --- CYTOCHEMISTRY --- CYTOCHEMISTRY --- CYTOCHEMISTRY
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PHOTOSYSTEM I --- CYTOCHEMISTRY --- ENZYMES --- HANDBOOKS --- PLANTS --- CALCIUM --- POTASSIUM --- SODIUM --- PLANT TISSUES --- IMMUNOCYTOCHEMISTRY --- LECTINS --- PHOTOSYSTEM II --- CYTOCHEMISTRY --- PLANTS --- CYTOCHEMISTRY --- CYTOCHEMISTRY --- CYTOCHEMISTRY --- IMMUNOCYTOCHEMISTRY --- CYTOCHEMISTRY --- CYTOCHEMISTRY --- PHOTOSYSTEM I --- CYTOCHEMISTRY --- ENZYMES --- HANDBOOKS --- PLANTS --- CALCIUM --- POTASSIUM --- SODIUM --- PLANT TISSUES --- IMMUNOCYTOCHEMISTRY --- LECTINS --- PHOTOSYSTEM II --- CYTOCHEMISTRY --- PLANTS --- CYTOCHEMISTRY --- CYTOCHEMISTRY --- CYTOCHEMISTRY --- IMMUNOCYTOCHEMISTRY --- CYTOCHEMISTRY --- CYTOCHEMISTRY
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Photosystem II is a 700-kDa membrane-protein super-complex responsible for the light-driven splitting of water in oxygenic photosynthesis. The photosystem is comprised of two 350-kDa complexes each made of 20 different polypeptides and over 80 co-factors. While there have been major advances in understanding the mature structure of this photosystem many key protein factors involved in the assembly of the complex do not appear in the holoenzyme. The mechanism for assembling this super-complex is a very active area of research with newly discovered assembly factors and subcomplexes requiring characterization. Additionally the ability to split water is inseparable from light-induced photodamage that arises from radicals and reactive O2 species generated by Photosystem II chemistry. Consequently, to sustain water splitting, a “self repair” cycle has evolved whereby damaged protein is removed and replaced so as to extend the working life of the complex. Understanding how the biogenesis and repair processes are coordinated is among several important questions that remain to be answered. Other questions include: how and when are the inorganic cofactors inserted during the assembly and repair processes and how are the subcomplexes protected from photodamage during assembly? Evidence has also been obtained for Photosystem II biogenesis centers in cyanobacteria but do these also exist in plants? Do the molecular mechanisms associated with Photosystem II assembly shed fresh light on the assembly of other major energy-transducing complexes such as Photosystem I or the cytochrome b6/f complex or indeed other respiratory complexes? The contributions to this Frontiers in Plant Science Research Topic are likely to reveal new details applicable to the assembly of a range of membrane-protein complexes, including aspects of self-assembly and solar energy conversion that may be applied to artificial photosynthetic systems. In addition, a deeper understanding of Photosystem II assembly — particularly in response to changing environmental conditions — will provide new knowledge underpinning photosynthetic yields which may contribute to improved food production and long-term food security.
Arabidopsis thaliana --- photoactivation --- photosynthesis --- Chlamydomonas reinhardtii --- cyanobacteria --- biogenesis --- Photosystem II --- photodamage --- Nicotiana tabacum --- Synechocystis sp. PCC 6803 --- Arabidopsis thaliana --- photoactivation --- photosynthesis --- Chlamydomonas reinhardtii --- cyanobacteria --- biogenesis --- Photosystem II --- photodamage --- Nicotiana tabacum --- Synechocystis sp. PCC 6803
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Photosystem II is a 700-kDa membrane-protein super-complex responsible for the light-driven splitting of water in oxygenic photosynthesis. The photosystem is comprised of two 350-kDa complexes each made of 20 different polypeptides and over 80 co-factors. While there have been major advances in understanding the mature structure of this photosystem many key protein factors involved in the assembly of the complex do not appear in the holoenzyme. The mechanism for assembling this super-complex is a very active area of research with newly discovered assembly factors and subcomplexes requiring characterization. Additionally the ability to split water is inseparable from light-induced photodamage that arises from radicals and reactive O2 species generated by Photosystem II chemistry. Consequently, to sustain water splitting, a “self repair” cycle has evolved whereby damaged protein is removed and replaced so as to extend the working life of the complex. Understanding how the biogenesis and repair processes are coordinated is among several important questions that remain to be answered. Other questions include: how and when are the inorganic cofactors inserted during the assembly and repair processes and how are the subcomplexes protected from photodamage during assembly? Evidence has also been obtained for Photosystem II biogenesis centers in cyanobacteria but do these also exist in plants? Do the molecular mechanisms associated with Photosystem II assembly shed fresh light on the assembly of other major energy-transducing complexes such as Photosystem I or the cytochrome b6/f complex or indeed other respiratory complexes? The contributions to this Frontiers in Plant Science Research Topic are likely to reveal new details applicable to the assembly of a range of membrane-protein complexes, including aspects of self-assembly and solar energy conversion that may be applied to artificial photosynthetic systems. In addition, a deeper understanding of Photosystem II assembly — particularly in response to changing environmental conditions — will provide new knowledge underpinning photosynthetic yields which may contribute to improved food production and long-term food security.
Arabidopsis thaliana --- photoactivation --- photosynthesis --- Chlamydomonas reinhardtii --- cyanobacteria --- biogenesis --- Photosystem II --- photodamage --- Nicotiana tabacum --- Synechocystis sp. PCC 6803
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Photosystem II is a 700-kDa membrane-protein super-complex responsible for the light-driven splitting of water in oxygenic photosynthesis. The photosystem is comprised of two 350-kDa complexes each made of 20 different polypeptides and over 80 co-factors. While there have been major advances in understanding the mature structure of this photosystem many key protein factors involved in the assembly of the complex do not appear in the holoenzyme. The mechanism for assembling this super-complex is a very active area of research with newly discovered assembly factors and subcomplexes requiring characterization. Additionally the ability to split water is inseparable from light-induced photodamage that arises from radicals and reactive O2 species generated by Photosystem II chemistry. Consequently, to sustain water splitting, a “self repair” cycle has evolved whereby damaged protein is removed and replaced so as to extend the working life of the complex. Understanding how the biogenesis and repair processes are coordinated is among several important questions that remain to be answered. Other questions include: how and when are the inorganic cofactors inserted during the assembly and repair processes and how are the subcomplexes protected from photodamage during assembly? Evidence has also been obtained for Photosystem II biogenesis centers in cyanobacteria but do these also exist in plants? Do the molecular mechanisms associated with Photosystem II assembly shed fresh light on the assembly of other major energy-transducing complexes such as Photosystem I or the cytochrome b6/f complex or indeed other respiratory complexes? The contributions to this Frontiers in Plant Science Research Topic are likely to reveal new details applicable to the assembly of a range of membrane-protein complexes, including aspects of self-assembly and solar energy conversion that may be applied to artificial photosynthetic systems. In addition, a deeper understanding of Photosystem II assembly — particularly in response to changing environmental conditions — will provide new knowledge underpinning photosynthetic yields which may contribute to improved food production and long-term food security.
Arabidopsis thaliana --- photoactivation --- photosynthesis --- Chlamydomonas reinhardtii --- cyanobacteria --- biogenesis --- Photosystem II --- photodamage --- Nicotiana tabacum --- Synechocystis sp. PCC 6803
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chloroplasts --- genes --- Enzymes --- DNA. --- DNA --- Photosynthesis --- Molecular biology --- genetics --- Rubisco --- Plastids --- Amyloplast --- Carotenoids --- Cytochromes --- cells --- Plastide --- Adaptation chromatique --- PHOTOSYNTHETIC APPARATUS --- PHOTOSYSTEM I --- PHOTOSYSTEM II --- PHOTOSYNTHETIC BACTERIA --- CYTOCHROMES --- COOPLING FACTOR --- CYANOBACTERIA --- PHYCOBILISOMES --- CHLOROPHILLS --- CAROTENES AND CAROTENOIDS --- RUBISCO --- CHLOROPLASTS --- PHOTOREGULATION --- PLASTIDS --- ADAPTATION --- NUCLEO-CYTOPLASMIC INTERACTION --- CHLOROPLAST GENETIC --- MOLECULAR BIOLOGY --- FUNCTIONS --- SYNTHESIS --- PREPARATION --- DIFFERENTIATION
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The Molecular Biology of Cyanobacteria summarizes more than a decade of progress in analyzing the taxonomy, biochemistry, physiology, cellular differentiation and developmental biology of cyanobacteria by modern molecular methods, especially molecular genetics. During this period cyanobacterial molecular biologists have been 'studying those things that cyanobacteria do well', and they have made cyanobacteria the organisms of choice for detailed molecular analyses of oxygenic photosynthesis. Part 1 contains chapters describing the molecular evolution and taxonomy of the cyanobacteria, as well as chapters describing cyanelles and the origins of algal and higher plant chloroplasts. Also included are chapters describing the picoplanktonic, oceanic cyanobacteria and prochlorophytes, 'the other cyanobacteria'. Part 2 is devoted to a detailed description of structural and functional aspects of the cyanobacterial photosynthetic apparatus. Included are chapters on thylakoid membrane organization, phycobiliproteins, and phycobilisomes, Photosystem I, Photosystem II, the cytochrome b6f complex, ATP synthase, and soluble electron carriers associated with photosynthetic electron transport. Structure, as it relates to biological function, is heavily emphasized in this portion of the book. Part 3 describes other important biochemical processes, including respiration, carbon metabolism, inorganic carbon uptake and concentration, nitrogen metabolism, tetrapyrrole biosynthesis, and carotenoid biosynthesis. Part 4 describes the cyanobacterial genetic systems and gene regulatory phenomena in these organisms. Emphasis is placed on responses to environmental stimuli, such as light intensity, light wavelength, temperature, and nutrient availability. Cellular differentiation and development phenomena, including the formation of heterocysts for nitrogen fixation and hormogonia for dispersal of organisms in the environment, are described. The book comprises 28 chapters written by lead
Prochlorophytes --- carotenoids --- cytochrome --- gene regulation --- genetic analysis --- heterocysts --- hormogonia --- photosystem --- pigments --- respiration --- Plant physiology. Plant biophysics --- Cyanobacteria --- Molecular aspects. --- CYANOBACTERIA --- PHOTOSYNTHETIC APPARATUS --- MOLECULAR EVOLUTION --- MARINE AREAS --- PICOPLANKTON --- PHYTOSYNTHESIS --- PROCHLOROPHYTA --- CYANELLES --- PHOTOSYNTHESIS --- RESPIRATION --- NITROGEN --- GENETIC ANALYSIS --- ECOPHYSIOLOGY --- HEAT-SHOCK --- HETEROCYSTS --- HORMOGONIA --- MOLECULAR BIOLOGY --- TAXONOMY --- REGULATION --- MECHANISMS --- METABOLISM
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Immunocytochemistry of Plant Cells is the first book exclusively dedicated to this topic. The first and largest portion of the book is concerned with a group of proven protocols and variations on these protocols that might prove useful, many developend or modified in the author's laboratory. The second portion of the book covers the studies that have been published previously on each of the plant organelles. Numerous state of the art micrographs from researchers around the world are included to demonstrate typical results.
Photosystem. --- Plant cells. --- Polymerization. --- Plant cytochemistry --- Immunocytochemistry --- Botany --- Earth & Environmental Sciences --- Plant Anatomy --- Plant Physiology --- Immunocytochemistry. --- Plant cells and tissues. --- Plant tissues --- Life sciences. --- Antibodies. --- Cell biology. --- Plant anatomy. --- Plant development. --- Biology --- Life Sciences. --- Plant Anatomy/Development. --- Cell Biology. --- Biological Techniques. --- Technique. --- Cells --- Plant anatomy --- Tissues --- Cytochemistry --- Immunochemistry --- Immunofluorescence --- Monoclonal antibodies. --- Cytology. --- Cytology --- Research --- Methodology. --- Cell biology --- Cellular biology --- Cytologists --- Antibodies, Monoclonal --- Monoclonal immunoglobulins --- Immunoglobulins --- Molecular cloning --- Plant structure --- Plants --- Structural botany --- Vegetable anatomy --- Anatomy --- Structure --- Biology—Technique. --- Antibodies --- Immune globulins --- Immune serum globulin --- Blood proteins --- Globulins --- Plasma cells --- Antibody diversity --- Antigens --- Bacterial immunoglobulin-binding proteins --- Development of plants --- Plant development --- Developmental biology --- Growth (Plants) --- Ontogeny
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