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Journal articles on the topic 'Photosystem II'

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Published: 4 June 2021

Last updated: 11 March 2023

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1

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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2

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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3

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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4

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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5

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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6

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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7

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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8

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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9

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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10

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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11

Moustaka, Julietta, Georgia Ouzounidou, Ilektra Sperdouli, and Michael Moustakas. "Photosystem II Is More Sensitive than Photosystem I to Al3+ Induced Phytotoxicity." Materials 11, no. 9 (September 19, 2018): 1772. http://dx.doi.org/10.3390/ma11091772.

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Aluminium (Al) the most abundant metal in the earth’s crust is toxic in acid soils (pH < 5.5) mainly in the ionic form of Al3+ species. The ability of crops to overcome Al toxicity varies among crop species and cultivars. Here, we report for a first time the simultaneous responses of photosystem II (PSII) and photosystem I (PSI) to Al3+ phytotoxicity. The responses of PSII and PSI in the durum wheat (Triticum turgidum L. cv. ‘Appulo E’) and the triticale (X Triticosecale Witmark cv. ‘Dada’) were evaluated by chlorophyll fluorescence quenching analysis and reflection spectroscopy respectively, under control (−Al, pH 6.5) and 148 μM Al (+Al, pH 4.5) conditions. During control growth conditions the high activity of PSII in ‘Appulo E’ led to a rather higher electron flow to PSI, which induced a higher PSI excitation pressure in ‘Appulo E’ than in ‘Dada’ that presented a lower PSII activity. However, under 148 μM Al the triticale ‘Dada’ presented a lower PSII and PSI excitation pressure than ‘Appulo E’. In conclusion, both photosystems of ‘Dada’ displayed a superior performance than ‘Appulo E’ under Al exposure, while in both cultivars PSII was more affected than PSI from Al3+ phytotoxicity.

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12

Bednarz, J., A. Radunz, and G. H. Schmid. "Lipid Composition of Photosystem I and II in the Tobacco Mutant Nicotiana tabacum NC 95." Zeitschrift für Naturforschung C 43, no. 5-6 (June 1, 1988): 423–30. http://dx.doi.org/10.1515/znc-1988-5-617.

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The lipids of photosystem II particles, of chloroplasts and leaves are compared in the variegated tobacco mutant NC 95. The mutant differs from other N. tabacum mutants by the phenomenon that it has variegated leaves with green and with yellow-green leaf patches. Chloroplasts from the green leaf areas exhibit photosystem II and photosystem I reactions and have a normal lamellar system with grana and intergrana regions. Chloroplasts from the yellow-green leaf areas, however, yield only photosystem I reactions and have only single stranded isolated thylakoids. Hence, this mutant offers the unique possibility to compare without the use of detergents within the same plant the lipid composition of photosystem II particles with that in intact chloroplasts, exhibiting either photosystem II and I reactions or those exhibiting exclusively photosystem I reactions. The lipids of photosystem II particles are composed of 37 % glycolipids, 4 % phospholipids, 5 % carotenoids and 54 % chlorophyll. Lipids of chloroplasts with grana stacking are composed of 75% glycolipids, 7 % phospholipids, 2 % carotenoids and 16% chlorophyll. Chloroplasts with single isolated thylakoids have a lipid composition consisting of 8 3 % glycolipids, 14% phospholipids and only 0.5% carotenoids and 2 % chlorophyll. The chloroplast lipid mixture is characterized in comparison to the respective leaf lipid mixture by a 16-17% higher glycolipid portion and by a 13-70% lower phospholipid content. The main difference in the lipid composition of photosystem I and II consists in the observation that chloroplasts active in only photosystem I contain more than double the amount of glycolipids and the 4-fold amount of phospholipids in comparison to photosystem II active preparations. The amount of monogalactolipid is even 3 times higher in chloroplasts active only in photosystem I when compared to those in photosystem II particles. In photosystem II particles phosphatidylethanolamine is completely lacking and phosphatidylglycerol and phosphatidylinositol occur only in traces. The fatty acids of the sulfolipid are by 45 % more saturated in the photosystem II particles and the digalactolipids of the photosystem II particles are by 28 % more saturated than in chloroplasts exhibiting photosystem I and II activity.

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13

Mao, Haotian, Mengying Chen, Yanqiu Su, Nan Wu, Ming Yuan, Shu Yuan, Marian Brestic, Marek Zivcak, Huaiyu Zhang, and Yanger Chen. "Comparison on Photosynthesis and Antioxidant Defense Systems in Wheat with Different Ploidy Levels and Octoploid Triticale." International Journal of Molecular Sciences 19, no. 10 (October 2, 2018): 3006. http://dx.doi.org/10.3390/ijms19103006.

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To investigate the evolutionary differences of wheat with different ploidy levels and octoploid Triticale, photosynthetic capacity, and antioxidant defenses system were compared within and between diploid, tetraploid and hexaploid wheat, and octoploid Triticale seedlings. The results showed that seed germination rate, chlorophyll content, and photochemical activity of photosystems, and the activities of antioxidative enzymes in hexaploid wheat and octoploid Triticale were significantly higher than in diploid and tetraploid wheat. Compared to other two wheat species and octoploid Triticale, hexaploid wheat presented lower levels of reactive oxygen species (ROS). Furthermore, we found that the levels of photosystem II reaction center protein D1, light-harvesting complex II b4 (CP29), and D subunit of photosystem I (PsaD) in diploid wheat were significantly lower compared with hexaploid wheat and octoploid Triticale. Taken together, we concluded that hexaploid wheat and octoploid Triticale have higher photosynthetic capacities and better antioxidant systems. These findings indicate that different ploidy levels of chromosome probably play an important regulatory role in photosystems and antioxidative systems of plants.

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14

Fromme, Petra, Jan Kern, Bernhard Loll, Jaceck Biesiadka, Wolfram Saenger, Horst T. Witt, Norbert Krauss, and Athina Zouni. "Functional implications on the mechanism of the function of photosystem II including water oxidation based on the structure of photosystem II." Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences 357, no. 1426 (October 29, 2002): 1337–45. http://dx.doi.org/10.1098/rstb.2002.1143.

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The structure of photosystem I at 3.8 Å resolution illustrated the main structural elements of the water–oxidizing photosystem II complex, including the constituents of the electron transport chain. The location of the Mn cluster within the complex has been identified for the first time to our knowledge. At this resolution, no individual atoms are visible, however, the electron density of the Mn cluster can be used to discuss both the present models of the Mn cluster as revealed from various spectroscopic methods and the implications for the mechanisms of water oxidation. Twenty–six chlorophylls from the antenna system of photosystem II have been identified. They are arranged in two layers, one close to the stromal side and one close to the lumenal side. Comparing the structure of the antenna system of photosystem II with the chlorophyll arrangement in photosystem I, which was recently determined at 2.5 Å resolution shows that photosystem II lacks the central domain of the photosystem I antenna, which is discussed in respect of the repair cycle of photosystem II due to photoinhibition.

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15

Rutherford, A. W., and P. Faller. "Photosystem II: evolutionary perspectives." Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences 358, no. 1429 (January 29, 2003): 245–53. http://dx.doi.org/10.1098/rstb.2002.1186.

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Based on the current model of its structure and function, photosystem II (PSII) seems to have evolved from an ancestor that was homodimeric in terms of its protein core and contained a special pair of chlorophylls as the photo–oxidizable cofactor. It is proposed that the key event in the evolution of PSII was a mutation that resulted in the separation of the two pigments that made up the special chlorophyll pair, making them into two chlorophylls that were neither special nor paired. These ordinary chlorophylls, along with the two adjacent monomeric chlorophylls, were very oxidizing: a property proposed to be intrinsic to monomeric chlorophylls in the environment provided by reaction centre (RC) proteins. It seems likely that other (mainly electrostatic) changes in the environments of the pigments probably tuned their redox potentials further but these changes would have been minor compared with the redox jump imposed by splitting of the special pair. This sudden increase in redox potential allowed the development of oxygen evolution. The highly oxidizing homodimeric RC would probably have been not only inefficient in terms of photochemistry and charge storage but also wasteful in terms of protein or pigments undergoing damage due to the oxidative chemistry. These problems would have constituted selective pressures in favour of the lop–sided, heterodimeric system that exists as PSII today, in which the highly oxidized species are limited to only one side of the heterodimer: the sacrificial, rapidly turned–over D1 protein. It is also suggested that one reason for maintaining an oxidizable tyrosine, TyrD, on the D2 side of the RC, is that the proton associated with its tyrosyl radical, has an electrostatic role in confining P + to the expendable D1 side.

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16

Horton, P., and A. V. Ruban. "Regulation of Photosystem II." Photosynthesis Research 34, no. 3 (December 1992): 375–85. http://dx.doi.org/10.1007/bf00029812.

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17

Ort, Donald R., and John Whitmarsh. "Inactive photosystem II centers: A resolution of discrepencies in photosystem II quantitation." Photosynthesis Research 23, no. 1 (January 1990): 101–4. http://dx.doi.org/10.1007/bf00030069.

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18

Manodori, Annamaria, and Anastasios Melis. "Cyanobacterial Acclimation to Photosystem I or Photosystem II Light." Plant Physiology 82, no. 1 (September 1, 1986): 185–89. http://dx.doi.org/10.1104/pp.82.1.185.

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19

Morales, Fermín, Anunciación Abadía, and Javier Abadía. "Photosynthesis, quenching of chlorophyll fluorescence and thermal energy dissipation in iron-deficient sugar beet leaves." Functional Plant Biology 25, no. 4 (1998): 403. http://dx.doi.org/10.1071/pp97130.

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In sugar beet (Beta vulgaris L.) iron deficiency decreased not only the photosynthetic rate but also the actual photosystem II efficiency at steady-state photosynthesis. In moderate iron deficiency, the decrease in actual photosystem II efficiency under illumination was related to closure of photosystem II reaction centers, whereas in severe iron deficiency it was associated to decreases of intrinsic photosystem II efficiency. The O2 evolution, on an absorbed light basis, decreased more than the actual photosystem II efficiency, suggesting the presence of a significant fraction of electron transport to molecular oxygen or the existence of some form of cyclic electron flow. Iron-deficient leaves reduced the excess of light absorbed that cannot be used in photosynthesis not only by decreasing absorptance, but also by dissipating a large part of the light absorbed by the photosystem II antenna. This mechanism, that protects the photosystem II reaction centers through the enhancement of energy dissipation, was related to the de-epoxidation of violaxanthin (V) to antheraxanthin (A) and zeaxanthin (Z) in iron-deficient leaves. These data provide additional support for a role of Z+A in photoprotection under conditions of excess photosynthetic light absorption.

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20

Giardi, Maria Teresa. "Significance of Photosystem II Core Phosphorylation Heterogeneity for the Herbicide-Binding Domain." Zeitschrift für Naturforschung C 48, no. 3-4 (April 1, 1993): 241–45. http://dx.doi.org/10.1515/znc-1993-3-420.

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Abstract In recent papers the heterogeneous nature of photosystem (PS) II core phosphorylation has been revealed (Giardi et al., BBRC 176, 1298 -1305 (1991); Plant Physiol. 100, 1948 -1954 (1992)). In this paper the action of endogenous and exogenous phosphatases both on the distribution of phosphorylated PS II core populations and on herbicide-binding activity in photosystem II preparations from Spinacia oleracea L. has been investigated. The results indicate that these phosphatases modify the photosystem II core phosphorylation heterogeneity at a different level. Dark incubation causes a partial dephosphorylation of D1 and D2 proteins by endogenous phosphatase(s) and changes the relative distribution of phosphorylated photosystem II core populations, while the action of the alkaline phosphatase leads to extensive dephosphorylation and to the detachment of PsbH protein from the photosystem II core. Dephosphorylation by the two alternative methods results in a differential modification of herbicide-binding activity. It is suggested that photosystem II heterogeneity with respect to the herbicide action, observed in vivo, could be a consequence of PS II core phosphorylation heterogeneity.

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21

Iwai, Masakazu, Makio Yokono, Noriko Inada, and Jun Minagawa. "Live-cell imaging of photosystem II antenna dissociation during state transitions." Proceedings of the National Academy of Sciences 107, no. 5 (December 22, 2009): 2337–42. http://dx.doi.org/10.1073/pnas.0908808107.

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Plants and green algae maintain efficient photosynthesis under changing light environments by adjusting their light-harvesting capacity. It has been suggested that energy redistribution is brought about by shuttling the light-harvesting antenna complex II (LHCII) between photosystem II (PSII) and photosystem I (PSI) (state transitions), but such molecular remodeling has never been demonstrated in vivo. Here, using chlorophyll fluorescence lifetime imaging microscopy, we visualized phospho-LHCII dissociation from PSII in live cells of the green alga Chlamydomonas reinhardtii. Induction of energy redistribution in wild-type cells led to an increase in, and spreading of, a 250-ps lifetime chlorophyll fluorescence component, which was not observed in the stt7 mutant incapable of state transitions. The 250-ps component was also the dominant component in a mutant containing the light-harvesting antenna complexes but no photosystems. The appearance of the 250-ps component was accompanied by activation of LHCII phosphorylation, supporting the visualization of phospho-LHCII dissociation. Possible implications of the unbound phospho-LHCII on energy dissipation are discussed.

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22

Bader, Klaus P., and Susanne Höper. "Stimulatory Effects of an Ammonium Salt Biocide on Photosynthetic Electron Transport Reactions." Zeitschrift für Naturforschung C 49, no. 1-2 (February 1, 1994): 87–94. http://dx.doi.org/10.1515/znc-1994-1-214.

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Alkylbenzyldimethylammonium chloride (ABDAC, zephirol) has been shown to improve the functioning of the photosynthetic apparatus of the filamentous cyanobacterium Oscillatoria chalybea (Bader, K. P. (1989) Biochim. Biophys. Acta 975, 399-402). This biocide exerts stimulatory effects on various electron transport reactions in Oscillatoria chalybea and chloroplasts from higher plants. By means of oxygen evolution measurements and of repetitive flash-induced absorption spectroscopy we were able to demonstrate an impact of the drug on the major complexes of photosynthetic membranes, i.e. the water splitting complex, photosystem II and photosystem I. Both, P820- and X320-absorption change signals were enhanced by the addition of ABDAC. Along with the quantitative analysis we investigated the relaxation kinetics of the signals and observed a substantial stabilization of the oxidized states of the respective redox components in the presence of the ammonium salt. Under appropriate conditions the relaxation kinetics of the absorption signals were significantly slowed down. ABDAC also affects photosystem I in Oscillatoria chalybea, but only under conditions, where a donor/acceptor system i.e. an isolated photosystem I reaction with photosystem II being disconnected was measured. Electron transport through the whole chain i.e. with water as the electron donor yielded no effect of the quaternary ammonium salt. It is suggested that this is due to an extremely bad linkage between the two photosystem, each of which, however, shows good reaction rates, when separately measured. The described interactions of the biocide with photosynthetic membranes are not restricted to Oscillatoria chalybea but are also observed with higher plant chloroplasts. In these systems, ABDAC enhances X320- and P700-signals to a comparable extent. In this case the P700-signal is stimulated in assays with electrons which are furnished from water which hints at good coupling between the two photosystems in our tobacco chloroplast preparations.

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23

Boekema, Egbert J., Henny van Roon, and Jan P. Dekker. "Specific association of photosystem II and light-harvesting complex II in partially solubilized photosystem II membranes." FEBS Letters 424, no. 1-2 (March 6, 1998): 95–99. http://dx.doi.org/10.1016/s0014-5793(98)00147-1.

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24

Schiphorst, Christo, Luuk Achterberg, Rodrigo Gómez, Rob Koehorst, Roberto Bassi, Herbert van Amerongen, Luca Dall’Osto, and Emilie Wientjes. "The role of light-harvesting complex I in excitation energy transfer from LHCII to photosystem I in Arabidopsis." Plant Physiology 188, no. 4 (December 6, 2021): 2241–52. http://dx.doi.org/10.1093/plphys/kiab579.

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Abstract Photosynthesis powers nearly all life on Earth. Light absorbed by photosystems drives the conversion of water and carbon dioxide into sugars. In plants, photosystem I (PSI) and photosystem II (PSII) work in series to drive the electron transport from water to NADP+. As both photosystems largely work in series, a balanced excitation pressure is required for optimal photosynthetic performance. Both photosystems are composed of a core and light-harvesting complexes (LHCI) for PSI and LHCII for PSII. When the light conditions favor the excitation of one photosystem over the other, a mobile pool of trimeric LHCII moves between both photosystems thus tuning their antenna cross-section in a process called state transitions. When PSII is overexcited multiple LHCIIs can associate with PSI. A trimeric LHCII binds to PSI at the PsaH/L/O site to form a well-characterized PSI–LHCI–LHCII supercomplex. The binding site(s) of the “additional” LHCII is still unclear, although a mediating role for LHCI has been proposed. In this work, we measured the PSI antenna size and trapping kinetics of photosynthetic membranes from Arabidopsis (Arabidopsis thaliana) plants. Membranes from wild-type (WT) plants were compared to those of the ΔLhca mutant that completely lacks the LHCI antenna. The results showed that “additional” LHCII complexes can transfer energy directly to the PSI core in the absence of LHCI. However, the transfer is about two times faster and therefore more efficient, when LHCI is present. This suggests LHCI mediates excitation energy transfer from loosely bound LHCII to PSI in WT plants.

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25

Johnson, Virginia M., and Himadri B. Pakrasi. "Advances in the Understanding of the Lifecycle of Photosystem II." Microorganisms 10, no. 5 (April 19, 2022): 836. http://dx.doi.org/10.3390/microorganisms10050836.

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Photosystem II is a light-driven water-plastoquinone oxidoreductase present in cyanobacteria, algae and plants. It produces molecular oxygen and protons to drive ATP synthesis, fueling life on Earth. As a multi-subunit membrane-protein-pigment complex, Photosystem II undergoes a dynamic cycle of synthesis, damage, and repair known as the Photosystem II lifecycle, to maintain a high level of photosynthetic activity at the cellular level. Cyanobacteria, oxygenic photosynthetic bacteria, are frequently used as model organisms to study oxygenic photosynthetic processes due to their ease of growth and genetic manipulation. The cyanobacterial PSII structure and function have been well-characterized, but its lifecycle is under active investigation. In this review, advances in studying the lifecycle of Photosystem II in cyanobacteria will be discussed, with a particular emphasis on new structural findings enabled by cryo-electron microscopy. These structural findings complement a rich and growing body of biochemical and molecular biology research into Photosystem II assembly and repair.

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26

Kato, Masaru, Jenny Z. Zhang, Nicholas Paul, and Erwin Reisner. "Protein film photoelectrochemistry of the water oxidation enzyme photosystem II." Chem. Soc. Rev. 43, no. 18 (2014): 6485–97. http://dx.doi.org/10.1039/c4cs00031e.

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27

Nugent, Jonathan H. A. "Oxygenic Photosynthesis. Electron Transfer in Photosystem I and Photosystem II." European Journal of Biochemistry 237, no. 3 (May 1996): 519–31. http://dx.doi.org/10.1111/j.1432-1033.1996.00519.x.

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28

Chow, W. S., Jan M. Anderson, and A. B. Hope. "Variable stoichiometries of photosystem II to photosystem I reaction centres." Photosynthesis Research 17, no. 3 (September 1988): 277–81. http://dx.doi.org/10.1007/bf00035454.

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29

Zharmukhamedov, S. K., and S. I. Allakhverdiev. "Chemical Inhibitors of Photosystem II." Russian Journal of Plant Physiology 68, no. 2 (March 2021): 212–27. http://dx.doi.org/10.1134/s1021443721020229.

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30

Khatoon, Mahbuba, Kayo Inagawa, Pavel Pospíšil, Amu Yamashita, Miho Yoshioka, Björn Lundin, Junko Horie, et al. "Quality Control of Photosystem II." Journal of Biological Chemistry 284, no. 37 (July 17, 2009): 25343–52. http://dx.doi.org/10.1074/jbc.m109.007740.

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31

Ohta, Hisataka, Takehiro Suzuki, Masaji Ueno, Akinori Okumura, Shizue Yoshihara, Jian-Ren Shen, and Isao Enami. "Extrinsic proteins of photosystem II." European Journal of Biochemistry 270, no. 20 (September 26, 2003): 4156–63. http://dx.doi.org/10.1046/j.1432-1033.2003.03810.x.

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32

Yoshioka, Miho, Suguru Uchida, Hiroki Mori, Keisuke Komayama, Satoshi Ohira, Noriko Morita, Tohru Nakanishi, and Yasusi Yamamoto. "Quality Control of Photosystem II." Journal of Biological Chemistry 281, no. 31 (May 30, 2006): 21660–69. http://dx.doi.org/10.1074/jbc.m602896200.

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33

Mulo, Paula, Susana Laakso, Pirkko Mäenpää, and Eva-Mari Aro. "Stepwise Photoinhibition of Photosystem II." Plant Physiology 117, no. 2 (June 1, 1998): 483–90. http://dx.doi.org/10.1104/pp.117.2.483.

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34

Hanley, J., Y. Deligiannakis, A. Pascal, P. Faller, and A. W. Rutherford. "Carotenoid Oxidation in Photosystem II†." Biochemistry 38, no. 26 (June 1999): 8189–95. http://dx.doi.org/10.1021/bi990633u.

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35

Coleman, William F. "Photosystem II Oxygen-Evolving Complex." Journal of Chemical Education 82, no. 5 (May 2005): 800. http://dx.doi.org/10.1021/ed082p800.

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36

Allen, John F., and Jon Nield. "Redox Tuning in Photosystem II." Trends in Plant Science 22, no. 2 (February 2017): 97–99. http://dx.doi.org/10.1016/j.tplants.2016.11.011.

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37

Camilleri, Patrick, David P. Astles, Michael W. Kerr, and John E. Spencer. "Aminopyrazolones: novel photosystem II inhibitors." Journal of Agricultural and Food Chemistry 38, no. 7 (July 1990): 1601–3. http://dx.doi.org/10.1021/jf00097a036.

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38

Wydrzynski, Thomas, Jonas ngström, and Tore Vänngård. "H2O2 formation by Photosystem II." Biochimica et Biophysica Acta (BBA) - Bioenergetics 973, no. 1 (January 1989): 23–28. http://dx.doi.org/10.1016/s0005-2728(89)80397-4.

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39

Stewart, David H., and Gary W. Brudvig. "Cytochrome b559 of photosystem II." Biochimica et Biophysica Acta (BBA) - Bioenergetics 1367, no. 1-3 (October 1998): 63–87. http://dx.doi.org/10.1016/s0005-2728(98)00139-x.

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40

Lubitz, Wolfgang, Maria Chrysina, and Nicholas Cox. "Water oxidation in photosystem II." Photosynthesis Research 142, no. 1 (June 11, 2019): 105–25. http://dx.doi.org/10.1007/s11120-019-00648-3.

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41

Yoshioka, Miho, Yosuke Nakayama, Mari Yoshida, Kensuke Ohashi, Noriko Morita, Hideki Kobayashi, and Yasusi Yamamoto. "Quality Control of Photosystem II." Journal of Biological Chemistry 285, no. 53 (October 4, 2010): 41972–81. http://dx.doi.org/10.1074/jbc.m110.117432.

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42

Yamamoto, Yasusi. "Quality Control of Photosystem II." Plant and Cell Physiology 42, no. 2 (February 15, 2001): 121–28. http://dx.doi.org/10.1093/pcp/pce022.

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43

Yamashita, Amu, Nobuyoshi Nijo, Pavel Pospíšil, Noriko Morita, Daichi Takenaka, Ryota Aminaka, Yoko Yamamoto, and Yasusi Yamamoto. "Quality Control of Photosystem II." Journal of Biological Chemistry 283, no. 42 (July 29, 2008): 28380–91. http://dx.doi.org/10.1074/jbc.m710465200.

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44

Pujols-Ayala, Idelisa, and Bridgette A. Barry. "Tyrosyl radicals in Photosystem II." Biochimica et Biophysica Acta (BBA) - Bioenergetics 1655 (April 2004): 205–16. http://dx.doi.org/10.1016/j.bbabio.2003.07.010.

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45

Ikeuchi, Masahiko. "Subunit proteins of photosystem II." Botanical Magazine Tokyo 105, no. 2 (June 1992): 327–73. http://dx.doi.org/10.1007/bf02489425.

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46

van Amerongen, Herbert, and Roberta Croce. "Light harvesting in photosystem II." Photosynthesis Research 116, no. 2-3 (April 18, 2013): 251–63. http://dx.doi.org/10.1007/s11120-013-9824-3.

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47

Nugent, Jonathan H. A., Christalla Demetriou, and Christopher J. Lockett. "Electron donation in Photosystem II." Biochimica et Biophysica Acta (BBA) - Bioenergetics 894, no. 3 (December 1987): 534–42. http://dx.doi.org/10.1016/0005-2728(87)90133-2.

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48

Thompson, Lynmarie K., Anne-Frances Miller, Julio C. De Paula, and Gary W. Brudvig. "Electron Donation in Photosystem II." Israel Journal of Chemistry 28, no. 2-3 (1988): 121–28. http://dx.doi.org/10.1002/ijch.198800021.

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49

Tracewell, Cara A., John S. Vrettos, James A. Bautista, Harry A. Frank, and Gary W. Brudvig. "Carotenoid Photooxidation in Photosystem II." Archives of Biochemistry and Biophysics 385, no. 1 (January 2001): 61–69. http://dx.doi.org/10.1006/abbi.2000.2150.

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50

Hansson, �rjan, and Tom Wydrzynski. "Current perceptions of Photosystem II." Photosynthesis Research 23, no. 2 (February 1990): 131–62. http://dx.doi.org/10.1007/bf00035006.

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