Relevant bibliographies by topics / Photosystem II

Academic literature on the topic 'Photosystem II'

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Published: 4 June 2021
Last updated: 11 March 2023

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Journal articles on the topic "Photosystem II"

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Kumagai, Yuya, Yoshikatsu Miyabe, Tomoyuki Takeda, Kohsuke Adachi, Hajime Yasui, and Hideki Kishimura. "In Silico Analysis of Relationship between Proteins from Plastid Genome of Red Alga Palmaria sp. (Japan) and Angiotensin I Converting Enzyme Inhibitory Peptides." Marine Drugs 17, no. 3 (March 25, 2019): 190. http://dx.doi.org/10.3390/md17030190.

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Plastid proteins are one of the main components in red algae. In order to clarify the angiotensin I converting enzyme (ACE) inhibitory peptides from red alga Palmaria sp. (Japan), we determined the plastid genome sequence. The genome possesses 205 protein coding genes, which were classified as genetic systems, ribosomal proteins, photosystems, adenosine triphosphate (ATP) synthesis, metabolism, transport, or unknown. After comparing ACE inhibitory peptides between protein sequences and a database, photosystems (177 ACE inhibitory peptides) were found to be the major source of ACE inhibitory peptides (total of 751). Photosystems consist of phycobilisomes, photosystem I, photosystem II, cytochrome complex, and a redox system. Among them, photosystem I (53) and II (51) were the major source of ACE inhibitory peptides. We found that the amino acid sequence of apcE (14) in phycobilisomes, psaA (18) and psaB (13) in photosystem I, and psbB (11) and psbC (10) in photosystem II covered a majority of bioactive peptide sequences. These results are useful for evaluating the bioactive peptides from red algae.
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Barbato, R., G. Friso, F. Rigoni, F. Dalla Vecchia, and G. M. Giacometti. "Structural changes and lateral redistribution of photosystem II during donor side photoinhibition of thylakoids." Journal of Cell Biology 119, no. 2 (October 15, 1992): 325–35. http://dx.doi.org/10.1083/jcb.119.2.325.

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The structural and topological stability of thylakoid components under photoinhibitory conditions (4,500 microE.m-2.s-1 white light) was studied on Mn depleted thylakoids isolated from spinach leaves. After various exposures to photoinhibitory light, the chlorophyll-protein complexes of both photosystems I and II were separated by sucrose gradient centrifugation and analysed by Western blotting, using a set of polyclonals raised against various apoproteins of the photosynthetic apparatus. A series of events occurring during donor side photoinhibition are described for photosystem II, including: (a) lowering of the oligomerization state of the photosystem II core; (b) cleavage of 32-kD protein D1 at specific sites; (c) dissociation of chlorophyll-protein CP43 from the photosystem II core; and (d) migration of damaged photosystem II components from the grana to the stroma lamellae. A tentative scheme for the succession of these events is illustrated. Some effects of photoinhibition on photosystem I are also reported involving dissociation of antenna chlorophyll-proteins LHCI from the photosystem I reaction center.
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Hibino, T., BH Lee, AK Rai, H. Ishikawa, H. Kojima, M. Tawada, H. Shimoyama, and T. Takabe. "Salt Enhances Photosystem I Content and Cyclic Electron Flow via NAD(P)H Dehydrogenase in the Halotolerant Cyanobacterium Aphanothece halophytica." Functional Plant Biology 23, no. 3 (1996): 321. http://dx.doi.org/10.1071/pp9960321.

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To uncover the adaptation mechanisms of photosystems for halotolerance, changes in stoichiometry and activity of photosystems in response to changes of salinities were examined in a halotolerant cyanobacterium, Aphanothece halophytica. Photosynthetic O2 evolution was high even at high salinities. O2 evolution activity increased with increasing external concentration of NaCl, reached a maximum at 1.5 M NaCl, and then decreased. Similar salt dependence was observed for photosystem II activity. On the other hand, photosystem I activity increased concomitantly with increase in salinity. Photoacoustic measurements indicated that appreciable energy storage by photosystem I mediated cyclic electron flow at high salinities. Significant electron donation to photosystem I reaction centres through NAD(P)H-dehydrogenase complexes was observed in high salt media. The contents of cytochrome b6/f and photosystem II were almost constant under various salinity conditions, whereas the levels of chlorophyll α, photosystem I, soluble cytochrome c-553, and NAD(P)H-dehydrogenase increased in the cells grown with high salinities. These results indicate that salt specifically induces an increase of protein levels involving cyclic electron flow around photosystem I that may entail an important role for adaptation of Aphanothece halophytica cells to high salinities.
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Anderson, Jan M. "Lateral heterogeneity of plant thylakoid protein complexes: early reminiscences." Philosophical Transactions of the Royal Society B: Biological Sciences 367, no. 1608 (December 19, 2012): 3384–88. http://dx.doi.org/10.1098/rstb.2012.0060.

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The concept that the two photosystems of photosynthesis cooperate in series, immortalized in Hill and Bendall's Z scheme, was still a black box that defined neither the structural nor the molecular organization of the thylakoid membrane network into grana and stroma thylakoids. The differentiation of the continuous thylakoid membrane into stacked grana thylakoids interconnected by single stroma thylakoids is a morphological reflection of the non-random distribution of photosystem II/light-harvesting complex of photosystem II, photosystem I and ATP synthase, which became known as lateral heterogeneity.
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BARBER, J., and W. KUHLBRANDT. "Photosystem II." Current Opinion in Structural Biology 9, no. 4 (August 1999): 469–75. http://dx.doi.org/10.1016/s0959-440x(99)80066-9.

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Aro, Eva-Mari. "Photosystem II." Biochimica et Biophysica Acta (BBA) - Bioenergetics 1817, no. 1 (January 2012): 1. http://dx.doi.org/10.1016/j.bbabio.2011.09.015.

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Nürnberg, Dennis J., Jennifer Morton, Stefano Santabarbara, Alison Telfer, Pierre Joliot, Laura A. Antonaru, Alexander V. Ruban, et al. "Photochemistry beyond the red limit in chlorophyll f–containing photosystems." Science 360, no. 6394 (June 14, 2018): 1210–13. http://dx.doi.org/10.1126/science.aar8313.

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Photosystems I and II convert solar energy into the chemical energy that powers life. Chlorophyll a photochemistry, using red light (680 to 700 nm), is near universal and is considered to define the energy “red limit” of oxygenic photosynthesis. We present biophysical studies on the photosystems from a cyanobacterium grown in far-red light (750 nm). The few long-wavelength chlorophylls present are well resolved from each other and from the majority pigment, chlorophyll a. Charge separation in photosystem I and II uses chlorophyll f at 745 nm and chlorophyll f (or d) at 727 nm, respectively. Each photosystem has a few even longer-wavelength chlorophylls f that collect light and pass excitation energy uphill to the photochemically active pigments. These photosystems function beyond the red limit using far-red pigments in only a few key positions.
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Silva, Pedro J., Maria Osswald-Claro, and Rosário Castro Mendonça. "How to tune the absorption spectrum of chlorophylls to enable better use of the available solar spectrum." PeerJ Physical Chemistry 4 (December 19, 2022): e26. http://dx.doi.org/10.7717/peerj-pchem.26.

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Photon capture by chlorophylls and other chromophores in light-harvesting complexes and photosystems is the driving force behind the light reactions of photosynthesis. Excitation of photosystem II allows it to receive electrons from the water-oxidizing oxygen-evolution complex and to transfer them to an electron-transport chain that generates a transmembrane electrochemical gradient and ultimately reduces plastocyanin, which donates its electron to photosystem I. Subsequently, excitation of photosystem I leads to electron transfer to a ferredoxin which can either reduce plastocyanin again (in so-called “cyclical electron-flow”) and release energy for the maintenance of the electrochemical gradient, or reduce NADP+ to NADPH. Although photons in the far-red (700–750 nm) portion of the solar spectrum carry enough energy to enable the functioning of the photosynthetic electron-transfer chain, most extant photosystems cannot usually take advantage of them due to only absorbing light with shorter wavelengths. In this work, we used computational methods to characterize the spectral and redox properties of 49 chlorophyll derivatives, with the aim of finding suitable candidates for incorporation into synthetic organisms with increased ability to use far-red photons. The data offer a simple and elegant explanation for the evolutionary selection of chlorophylls a, b, c, and d among all easily-synthesized singly-substituted chlorophylls, and identified one novel candidate (2,12-diformyl chlorophyll a) with an absorption peak shifted 79 nm into the far-red (relative to chlorophyll a) with redox characteristics fully suitable to its possible incorporation into photosystem I (though not photosystem II). chlorophyll d is shown by our data to be the most suitable candidate for incorporation into far-red utilizing photosystem II, and several candidates were found with red-shifted Soret bands that allow the capture of larger amounts of blue and green light by light harvesting complexes.
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Allen, John F., and Thomas Pfannschmidt. "Balancing the two photosystems: photosynthetic electron transfer governs transcription of reaction centre genes in chloroplasts." Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences 355, no. 1402 (October 29, 2000): 1351–59. http://dx.doi.org/10.1098/rstb.2000.0697.

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Chloroplasts are cytoplasmic organelles whose primary function is photosynthesis, but which also contain small, specialized and quasi–autonomous genetic systems. In photosynthesis, two energy converting photosystems are connected, electrochemically, in series. The connecting electron carriers are oxidized by photosystem I (PS I) and reduced by photosystem II (PS II). It has recently been shown that the oxidation–reduction state of one connecting electron carrier, plastoquinone, controls transcription of chloroplast genes for reaction centre proteins of the two photosystems. The control counteracts the imbalance in electron transport that causes it: oxidized plastoquinone induces PS II and represses PS I; reduced plastoquinone induces PS I and represses PS II. This complementarity is observed both in vivo , using light favouring one or other photosystem, and in vitro , when site–specific electron transport inhibitors are added to transcriptionally and photosynthetically active chloroplasts. There is thus a transcriptional level of control that has a regulatory function similar to that of purely post–translational ‘state transitions’ in which the redistribution of absorbed excitation energy between photosystems is mediated by thylakoid membrane protein phosphorylation. The changes in rates of transcription that are induced by spectral changes in vivo can be detected even before the corresponding state transitions are complete, suggesting the operation of a branched pathway of redox signal transduction. These findings suggest a mechanism for adjustment of photosystem stoichiometry in which initial events involve a sensor of the redox state of plastoquinone, and may thus be the same as the initial events of state transitions. Redox control of chloroplast transcription is also consistent with the proposal that a direct regulatory coupling between electron transport and gene expression determines the function and composition of the chloroplast's extra–nuclear genetic system.
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Bednarz, J., S. Höper, M. Bockstette, K. P. Bader, and G. H. Schmid. "Interrelationship of Oxygen and Nitrogen Metabolism in the Filamentous Cyanobacterium Oscillatoria chalybea." Zeitschrift für Naturforschung C 44, no. 11-12 (December 1, 1989): 946–54. http://dx.doi.org/10.1515/znc-1989-11-1212.

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Abstract Filamentous Cyanobacteria. Hydrogen Peroxide, Photosystem II. Nitrogen Metabolism By means of mass spectrometric analysis we have been able to demonstrate H 20 2-production and its decomposition by photosystem II in thylakoids of the filamentous cyanobacterium Oscil­ latoria chalybea. This H2O2-production and its quasi simultaneous decomposition by the S-state system can be readily demonstrated in flash light illumination (K. P. Bader and G. H. Schmid, Biochim. Biophys. Acta 936, 179-186 (1988)) or as shown in the present paper in continuous light at low light intensities. These light conditions correspond essentially to the culturing condition of the organism on nitrate as the sole nitrogen source. Under these conditions, however, electron transport between the two photosystems seems to be mostly disconnected and respiratory activity practically non existent. Under these conditions, on the other hand, nitrate reductase is induced and nitrate reduced. The present paper addresses the question how this organism might solve the metabolic problems of nitrate reduction with such an electron transport system. Tested under high light intensities under which the organism would not grow at all, electron transport between the two photosystems is optimally linked and the system funnels part of its photosynthetically pro­duced electrons into a conventional cyanide-sensitive respiratory electron transport chain and even into an alternative Sham-sensitive (cyanide-insensitive) respiratory chain. This is made possible by the overweight of photosystem II capacity in comparison to photosystem I activity as reported in this paper. Under the conditions described, the cyanobacterium grows also on ar­ginine as the sole nitrogen source. Most interestingly under these conditions nitrate reductase induction is not shut off as is the case with other aminoacids like ornithine or alanine in the medium. Nitrite reductase is not induced in these bacteria, if grown on arginine as the sole nitrogen source. This observation is discussed in context with the fact that arginine is a major storage product (cyanophycin) in this organism and that the observed photosystem II mediated H2O2-production might be correlated with arginine metabolism.
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Dissertations / Theses on the topic "Photosystem II"

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Liebisch, Peter. "Der Mangankomplex der Photosynthese im katalytischen Zyklus neue röntgenspektroskopische Ansätze zur Untersuchung von Struktur und Mechanismus /." [S.l. : s.n.], 2005. http://www.diss.fu-berlin.de/2005/63/index.html.

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Grabolle, Markus. "Die Donorseite des Photosystems II der Pflanzen Rekombinationsfluoreszenz- und Röntgenabsorptionsstudien /." [S.l. : s.n.], 2005. http://www.diss.fu-berlin.de/2005/174/index.html.

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Zehetner, Andrea. "Modifikationen am Photosystem II-Reaktionszentrum." Diss., lmu, 2003. http://nbn-resolving.de/urn:nbn:de:bvb:19-12133.

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Sharma, Jyoti. "Structural characterisation of photosystem II." Thesis, Imperial College London, 1995. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.309267.

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Protocols were developed to fractionate each of the five protein components present in the PSII reaction centre complex, isolated from the thylakoid membrane of pea plants. The precise molecular weights of all the purified components were then successfully determined, for the first time by electrospray and fast atom bombardment mass spectrometry. Discrepancies between the molecular weights assigned and those calculated from the respective cDNA sequences were observed for all of the reaction centre component proteins. Application of novel mapping and sequencing strategies on these proteins has assured the elucidation of full primary structures of and subunits of cytochrome b559 and the majority of the structures of the D1 and D2 proteins. In the case of the subunit to cytochrome b559 an N-terminal processing event, involving the removal of the initiating formyl-methionine residue was found. The transformations on the subunit of cytochrome b559 were characterised as a N-terminal modification, entailing the processing of the formyl-methionine residue followed by an acetylation of the amino terminus of the mature protein, and a sequence change at residue twenty six, were a serine has been replaced by a phenylalanine residue. This was presumed to be due to an error in the gene sequence, but is more probably a result of the recently described phenomenon of mRNA editing. Currently, the nucleotide sequence of the pshI gene from pea plants is not available. Using a combination of mass spectrometric techniques and automated gas phase sequencing the primary structure of this component has been obtained in these studies. In contrast to the smaller subunits, data obtained on the D1 and D2 proteins indicated that both these components exist in heterogeneous forms. Mapping studies on these subunits have identified phosphorylation and oxidation, as at least two sources of this microheterogeneity.
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Nield, Jonathan Michael. "Structural characterisation of photosystem II." Thesis, Imperial College London, 1997. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.268032.

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Photosystem II (PSII) is the multi-subunit pigment-protein complex which catalyses water oxidation in higher plants, algae and cyanobacteria. Its atomic structure and protein cofactor organisation has not yet been determined. Elucidation of the structure would aid our understanding of PSII function and regulation, and may provide us with the knowledge to design new solar driven catalysts for the production of renewable energy. This thesis details the biochemical and structural studies on PSII complexes differing in subunit composition that have been isolated in order to enhance our current understanding of PSII structure. The largest of several novel PSII complexes isolated was a 725 kDa PSII-LHCII complex from the higher plant, spinach (Spinacea oleracea), consisting of the light harvesting proteins Lhcb1, 2, 4 and 5 bound to a dimeric oxygen evolving PSII core. The Lhcb proteins, 33 kDa and 23 kDa extrinsic proteins were sequentially removed, allowing their positions to be determined at a resolution of 25 Å by producing enhanced images from electron micrographs of negatively stained particles. A three-dimensional reconstruction was also achieved with these images at a resolution of 30 Å. The results suggest that the dimeric 725 kDa particle bound one LHCII trimer per reaction centre, connected to a centrally located PSII core dimer by one copy of Lhcb4 and 5. It is further concluded that CP43 is located to the outer side of the central dimer core and that there is a single copy of the 33 kDa and 23 kDa proteins per reaction centre. The significance of the dimeric organisation is discussed in terms of the in vivo structure. A similar complex of the PSII-LHCII type was also isolated from the green alga, Chlamydomonas reinhardtii and enhanced images obtained to enable comparison with the higher plant data. A smaller spinach CP47-RC dimeric PSII complex (390 kDa), was subjected to single particle image averaging with the view to more closely identifying the position of the reaction centre proteins within the PSII-LHCII complex.
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Hankamer, Benjamin David. "Structural studies on photosystem II." Thesis, Imperial College London, 1994. http://hdl.handle.net/10044/1/11392.

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Rolfe, Stephen Alexander. "Electron transport in cyanobacterial photosystem II." Thesis, University of Cambridge, 1988. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.258430.

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Sarcina, Maria. "Pigment-protein interactions within photosystem II." Thesis, Imperial College London, 1999. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.313030.

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Reinsberg, Dirk. "Zeitaufgelöste Fluoreszenzmessungen zur Faltung und Pigmentbindung des Lichtsammlerproteins LHC II aus Photosystem II." [S.l. : s.n.], 2000. http://ArchiMeD.uni-mainz.de/pub/2000/0082/diss.pdf.

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Lo, Wen-Feng. "Mimicking Photosystem II With Synthetic Manganese Complexes." Thesis, Boston College, 2008. http://hdl.handle.net/2345/1367.

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Thesis advisor: William H. Armstrong
The Oxygen-Evolving Complex (OEC) of Photosystem II (PSII) utilizes a Mn4Ca cluster to catalyze the conversion of water to dioxygen within plant chloroplasts. The active site of the water oxidase is found on the lumenal side of the thylakoid membrane. For many years, the nature of this convoluted system, including the unresolved structural arrangement of the OEC manganese-oxo aggregate, stimulated on-going research projects in a diverse set of scientific fields. A tetranuclear oxo-bridged manganese complex associated with calcium [Ca] and chloride [Cl], along with a redox active tyrosine (Tyr), is thought to be the center of this remarkable and unique biological machinery. An illustrious catalytic cycle, known as the Kok cycle, progresses through a series of five intermediate states (Si, i = 0-4) to conduct water oxidation and dioxygen evolution. A tentative structural proposal based on the single crystal X-ray diffraction (XRD) crystallographic measurements introduced a CaMn3 cubane cluster and an appended fourth manganese atom. It was proposed that water binds between the “dangling” Mn atom and the Ca atom, and that is where the O-O bond formation is proposed to occur, followed by O2 release without structural rearrangement of the cubane core. The plausible manganyl (MnV=O) species was also suggested as an intermediate in the S4 state for the O-O bond formation and release O2. We have examined plausible reactive manganyl species as are proposed to exist at the OEC S4 state. The existence of manganyl in synthetic model systems will be presented in Chapter 2. In this study, we utilized stopped-flow UV-vis spectroscopy and mass spectrometry to investigate the formation and the nature of the intermediate in the reaction between mononuclear Schiff base manganese complexes and a reagent that is often used for O atom transfer reactions. Chapter 3 involves establishment of a logical synthetic method to prepare the related complexes, Mn2O2(bpy/dmb)2(ArRCOO)2 [R = 2,6-diphenyl, 2,6-ditolyl]. The dimanganese-oxo center is considered as a basic unit on the path toward the construction of higher nuclearity of Mn aggregates, preferably Mn4 clusters to be used for OEC catalytic cycle mimicry. Controlled ligand exchange synthesis of this type of carboxylate-rich/bridged {Mn2O2} dimers will provide an alternate pathway toward obtaining the Mn aggregates that are not attainable by direct ‘self-assembly’ synthetic methods. In Chapter 4, we will describe a novel mixed-ligand tetranuclear Mn cluster of the adamantane core type, [Mn4(μ-O6)(bpy)4(py)4](ClO4)4. This cluster was synthesized by using a simple reaction and its spectroscopic characterization will be discussed. We will also demonstrate chromatographic behavior of the Mn clusters that we encountered in this work (see Appendix A)
Thesis (PhD) — Boston College, 2008
Submitted to: Boston College. Graduate School of Arts and Sciences
Discipline: Chemistry
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Books on the topic "Photosystem II"

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Wydrzynski, Thomas J., Kimiyuki Satoh, and Joel A. Freeman, eds. Photosystem II. Dordrecht: Springer Netherlands, 2005. http://dx.doi.org/10.1007/1-4020-4254-x.

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Nicholson, W. V. Structural studies of photosystem II. Manchester: UMIST, 1995.

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Rutherford, A. W. Photosystem II, the water-splitting enzyme. Amsterdam: Elsevier, 1989.

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Sparrow, Raymond Walter. Studies on photosystem II in higher plant chloroplasts. Preston: Lancashire Polytechnic, 1987.

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Nakamura, Shin. Molecular Mechanisms of Proton-coupled Electron Transfer and Water Oxidation in Photosystem II. Singapore: Springer Singapore, 2020. http://dx.doi.org/10.1007/978-981-15-1584-2.

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Nongnuj, J. X-ray diffraction studies of inorganic co-ordination complexes related to photosystem-II. Manchester: UMIST, 1998.

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Collins, R. F. Investigations of spinacia oleracea photosystem II architechture using the zero length bi-functional crosslinker 1-ethyl-3(3-dimethylaminoipropyl)-carbodi-imide(EDC). Manchester: UMIST, 1997.

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Nieuwenhuis, Saskia Apollonia Maria. Investigation of the oxygenic photosynthetic reaction centre photosystem II with specific isotope labelling: Synthesis and incorporation of stable-isotope labelled (S)-phenylalanine and (S)-tyrosine. [Leiden: S.A.M. Nieuwenhuis, 1998.

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Al-Hazmi, Abdul Aziz. An investigation into the functional role of the D1:1 and D1:2 polypeptides in photosystem II in cyanobacteria: The effect of changing PSI/PSII ratio on photoinhibition in Synechococcus sp. PCC7942. St. Catharines, Ont: Brock University, Dept. of Biological Sciences, 1999.

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Wydrzynski, T., Joel A. Freeman, and Kimiyuki Satoh. Photosystem II : The Light-Driven Water: Plastoquinone Oxidoreductase. Springer, 2006.

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Book chapters on the topic "Photosystem II"

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McConnell, Iain L., and Gary W. Brudvig. "Photosystem II." In Encyclopedia of Biophysics, 1879–82. Berlin, Heidelberg: Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-16712-6_23.

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Sibbald, Peter R., and Beverley R. Green. "Copper in Photosystem II." In Progress in Photosynthesis Research, 573–76. Dordrecht: Springer Netherlands, 1987. http://dx.doi.org/10.1007/978-94-009-3535-8_136.

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Cai, Peng, Guangle Li, Jiao Li, Yi Jia, Zhongfeng Zhang, and Junbai Li. "Photosystem II Based Multilayers." In Supramolecular Chemistry of Biomimetic Systems, 109–33. Singapore: Springer Singapore, 2017. http://dx.doi.org/10.1007/978-981-10-6059-5_6.

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Ford, Robert C., Richard P. Collins, Toby D. Flint, Ashraf Kitmitto, William V. Nicholson, Mark F. Rosenberg, Fiona H. Shepherd, Svetla Stoylova, and Andreas Holzenburg. "Photosystem II 3D Architecture." In Photosynthesis: from Light to Biosphere, 2153–58. Dordrecht: Springer Netherlands, 1995. http://dx.doi.org/10.1007/978-94-009-0173-5_506.

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Kouřil, Roman, Lukáš Nosek, Dmitry Semchonok, Egbert J. Boekema, and Petr Ilík. "Organization of Plant Photosystem II and Photosystem I Supercomplexes." In Subcellular Biochemistry, 259–86. Singapore: Springer Singapore, 2018. http://dx.doi.org/10.1007/978-981-10-7757-9_9.

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Sauer, Kenneth. "Photosystem II and Water Oxidation." In Current Research in Photosynthesis, 675–84. Dordrecht: Springer Netherlands, 1990. http://dx.doi.org/10.1007/978-94-009-0511-5_157.

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Gray, J. C., A. N. Webber, S. M. Hird, D. L. Willey, and T. A. Dyer. "Genes for Photosystem II Polypeptides." In Current Research in Photosynthesis, 2367–74. Dordrecht: Springer Netherlands, 1990. http://dx.doi.org/10.1007/978-94-009-0511-5_538.

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Murata, Norio, Sho-Ichi Higashi, and Yoko Fujimura. "Lipids in Spinach Photosystem II." In Current Research in Photosynthesis, 403–6. Dordrecht: Springer Netherlands, 1990. http://dx.doi.org/10.1007/978-94-009-0511-5_89.

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Hubbard, Julia A. M., and Michael C. W. Evans. "Electron Acceptors in Photosystem II." In Techniques and New Developments in Photosynthesis Research, 237–39. Boston, MA: Springer US, 1989. http://dx.doi.org/10.1007/978-1-4684-8571-4_27.

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Feyziyev, Yashar. "Photosystem II Function and Bicarbonate." In Photosynthesis. Energy from the Sun, 397–400. Dordrecht: Springer Netherlands, 2008. http://dx.doi.org/10.1007/978-1-4020-6709-9_89.

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Conference papers on the topic "Photosystem II"

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Hayes, John M., D. Tang, Ryszard Jankowiak, and Gerald J. Small. "Transient and persistent hole-burning of photosystem II preparations." In Optics, Electro-Optics, and Laser Applications in Science and Engineering, edited by Bryan L. Fearey. SPIE, 1991. http://dx.doi.org/10.1117/12.44249.

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Nguyen, Hoang H., Yin Song, Elizabeth L. Maret, Yogita Silori, and Jennifer P. Ogilvie. "Multispectral Two-Dimensional Electronic Spectroscopy of the Photosystem II Reaction Center." In International Conference on Ultrafast Phenomena. Washington, D.C.: Optica Publishing Group, 2022. http://dx.doi.org/10.1364/up.2022.m1a.2.

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We present two-dimensional electronic spectroscopy of the photosystem II reaction center at 77K, exciting the spectrally-congested Qy region and probing multiple spectral regions spanning the visible to the mid-IR to extract broadband charge separation signatures.
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Myers, J. A., K. L. M. Lewis, F. Fuller, P. F. Tekavec, and J. P. Ogilvie. "Two-dimensional electronic spectroscopy of the photosystem II reaction center." In Laser Science. Washington, D.C.: OSA, 2010. http://dx.doi.org/10.1364/ls.2010.ltha2.

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MALY, J., M. ILIE, E. CIANCI, V. FOGLIETTI, L. DELLA SETA, M. R. MONTEREALI, K. PUNAKIVI, W. VASTARELLA, and R. PILLOTON. "DIRECT ELECTRON TRANSPORT BETWEEN PHOTOSYSTEM II AND MODIFIED GOLD ELECTRODES." In Proceedings of the 10th Italian Conference. WORLD SCIENTIFIC, 2008. http://dx.doi.org/10.1142/9789812833532_0003.

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Vacha, M., F. Adamec, M. Ambroz, J. Dian, L. Nedbal, and J. Hala. "Persistent Hole Burning Study of Core Antenna of Photosystem II." In Persistent Spectral Hole Burning: Science and Applications. Washington, D.C.: Optica Publishing Group, 1991. http://dx.doi.org/10.1364/pshb.1991.the2.

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The application of hole burning spectroscopy (HB) in the study of photosynthetic systems offers an independent method for determining excited state lifetimes of particular chromophores. The rate constants of excitation energy transfer (EET) in photosynthetic antennae can be directly determined by time resolved fluorescence spectroscopy. For most bacterial and higher plants antennae is of the order of 10-12 s–1 [1]. Efficient EET in pigment-protein complexes causes significant shortening (three orders of magnitude) of the excited state lifetimes T1 in comparison with isolated pigments.
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Yang, Shiun-Jr, Eric A. Arsenault, Kaydren Orcutt, Cristina Leonardo, Masakazu Iwai, Yusuke Yoneda, and Graham R. Fleming. "Ultrafast Energy Transfer and Charge Separation Pathways in the Photosystem II Supercomplex." In International Conference on Ultrafast Phenomena. Washington, D.C.: Optica Publishing Group, 2022. http://dx.doi.org/10.1364/up.2022.th5a.5.

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Spectral congestion challenges spectroscopic studies of the Photosystem II (PSII) light harvesting antenna dynamics. The higher resolution of two-dimensional electronic-vibrational spectroscopy provides new insights into the PSII supercomplex dynamics.
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Giardi, M. T., P. Ragni, D. Esposito, A. Alessandrelli, E. Pace, and G. Angelini. "Realization of a Photosystem II-based biosensor for gamma radiation detection." In Proceedings of the 5th Italian Conference — Extended to Mediterranean Countries. WORLD SCIENTIFIC, 2000. http://dx.doi.org/10.1142/9789812792013_0011.

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Freiberg, Arvi, Kou Timpmann, and Andrei A. Moskalenko. "Energy transfer in photosystem II core complexes: comparison with bacterial systems." In Laser Spectroscopy of Biomolecules: 4th International Conference on Laser Applications in Life Sciences, edited by Jouko E. Korppi-Tommola. SPIE, 1993. http://dx.doi.org/10.1117/12.146159.

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Lovyagina, E. R., and B. K. Semin. "MECHANISM OF PHOTOSYSTEM II OXYGEN EVOLUTION ACTIVITY DECREASE AT ACIDIC pH." In The All-Russian Scientific Conference with International Participation and Schools of Young Scientists "Mechanisms of resistance of plants and microorganisms to unfavorable environmental". SIPPB SB RAS, 2018. http://dx.doi.org/10.31255/978-5-94797-319-8-471-474.

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Loktyushkin, A. V., E. R. Lovyagina, and B. K. Semin. "TOXIC EFFECT OF TERBIUM ON THE HIGH PLANT PHOTOSYSTEM II FUNCTION." In The All-Russian Scientific Conference with International Participation and Schools of Young Scientists "Mechanisms of resistance of plants and microorganisms to unfavorable environmental". SIPPB SB RAS, 2018. http://dx.doi.org/10.31255/978-5-94797-319-8-475-478.

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Reports on the topic "Photosystem II"

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Chang, Hai Chou. Spectral hole burning studies of photosystem II. Office of Scientific and Technical Information (OSTI), September 1995. http://dx.doi.org/10.2172/130613.

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Luan, Sheng. Immunophilins and their function in photosystem II assembly. Office of Scientific and Technical Information (OSTI), November 2012. http://dx.doi.org/10.2172/1055782.

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Vermaas, W. F. J. The chlorophyll-binding protein CP47 in photosystem II. Progress report. Office of Scientific and Technical Information (OSTI), June 1994. http://dx.doi.org/10.2172/10155644.

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Vermaas, W. F. J. The chlorophyll-binding protein CP47 in photosystem II. Final report. Office of Scientific and Technical Information (OSTI), December 1995. http://dx.doi.org/10.2172/207435.

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Bogorad, L. Unraveling Photosystem II: Progress report, February 1, 1988--January 31, 1989. Office of Scientific and Technical Information (OSTI), January 1989. http://dx.doi.org/10.2172/6128988.

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Latimer, Matthew John. The role of calcium in the oxygen evolving center of photosystem II. Office of Scientific and Technical Information (OSTI), May 1995. http://dx.doi.org/10.2172/199108.

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Dismukes, Gerard Charles, Gennady Ananyev, and Colin Gates. Photosystem II Water Oxidation: Mechanism, Efficiency and Flux in Diverse Oxygenic Phototrophs. Office of Scientific and Technical Information (OSTI), January 2018. http://dx.doi.org/10.2172/1418262.

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Robblee, John Henry. XANES, EXAFS and Kbeta spectroscopic studies of the oxygen-evolving complex in Photosystem II. Office of Scientific and Technical Information (OSTI), December 2000. http://dx.doi.org/10.2172/773946.

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Woodbury, Neal. Combinatorial Development of Water Splitting Catalysts Based on the Oxygen Evolving Complex of Photosystem II. Office of Scientific and Technical Information (OSTI), March 2010. http://dx.doi.org/10.2172/1080011.

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Ogilvie, Jennifer P. Two-Dimensional Electronic Spectroscopies for Probing Electronic Structure and Charge Transfer: Applications to Photosystem II. Office of Scientific and Technical Information (OSTI), November 2016. http://dx.doi.org/10.2172/1333164.

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