scholarly journals Photosynthetic electron transport in thylakoid preparations from two marine red algae (Rhodophyta)

1983 ◽  
Vol 210 (2) ◽  
pp. 583-589 ◽  
Author(s):  
A C Stewart ◽  
A W D Larkum
Keyword(s):  
Electron Transport ◽  
Photosystem Ii ◽  
Red Algae ◽  
Higher Plants ◽  
Outer Part ◽  
Photosynthetic Electron Transport ◽  
O2 Evolution ◽  
Blue Green Algae ◽  
High Concentrations

Thylakoid membrane preparations active in photosynthetic electron transport have been obtained from two marine red algae, Griffithsia monilis and Anotrichium tenue. High concentrations (0.5-1.0 M) of salts such as phosphate, citrate, succinate and tartrate stabilized functional binding of phycobilisomes to the membrane and also stabilized Photosystem II-catalysed electron-transport activity. High concentrations (1.0 M) of chloride and nitrate, or 30 mM-Tricine/NaOH buffer (pH 7.2) in the absence of salts, detached phycobilisomes and inhibited electron transport through Photosystem II. The O2-evolving system was identified as the electron-transport chain component that was inhibited under these conditions. Washing membranes with buffers containing 1.0-1.5 M-sorbitol and 5-50 mM concentrations of various salts removed the outer part of the phycobilisome but retained 30-70% of the allophycocyanin ‘core’ of the phycobilisome. These preparations were 30-70% active in O2 evolution compared with unwashed membranes. In the sensitivity of their O2-evolving apparatus to the composition of the medium in vitro, the red algae resembled blue-green algae and differed from other eukaryotic algae and higher plants. It is suggested that an environment of structured water may be essential for the functional integrity of Photosystem II in biliprotein-containing algae.

scholarly journals The effects of high concentrations of salts on photosynthetic electron transport in spinach (Spinacia oleracea) chloroplasts

1982 ◽  
Vol 204 (3) ◽  
pp. 705-712 ◽  
Author(s):  
A C Stewart
Keyword(s):  
Electron Transport ◽  
Photosystem Ii ◽  
Photosystem I ◽  
Spinacia Oleracea ◽  
Photosynthetic Electron Transport ◽  
Potassium Citrate ◽  
O2 Evolution ◽  
Hofmeister Series ◽  
Reaction Centre ◽  
High Concentrations

1. Photosynthetic electron transport from water to lipophilic Photosystem II acceptors was stimulated 3-5-fold by high concentrations (greater than or equal to 1 M) of salts containing anions such as citrate, succinate and phosphate that are high in the Hofmeister series. 2. In trypsin-treated chloroplasts, K3Fe(CN)6 reduction insensitive to 3-(3,4-dichlorophenyl)-1,1-dimethylurea was strongly stimulated by high concentrations of potassium citrate, but there was much less stimulation of 2,6-dichloroindophenol reduction in Tris-treated chloroplasts supplied with 1,5-diphenylcarbazide as artificial donor. The results suggest that the main site of action of citrate was the O2-evolving complex of Photosystem II. 3. Photosystem I partial reactions were also stimulated by intermediate concentrations of citrate (up to 2-fold stimulation by 0.6-0.8 M-citrate), but were inhibited at the highest concentrations. The observed stimulation may have been caused by stabilizaton of plastocyanin that was complexed with the Photosystem I reaction centre, 4. At 1 M, potassium citrate protected O2 evolution against denaturation by heat or by the chaotropic agent NaNO3. 5. It is suggested that anions high in the Hofmeister series stimulated and stabilized electron transport by enhancing water structure around the protein complexes in the thylakoid membrane.

scholarly journals Plastocyanin is the long-range electron carrier between photosystem II and photosystem I in plants

2020 ◽  
Vol 117 (26) ◽  
pp. 15354-15362 ◽  
Author(s):  
Ricarda Höhner ◽  
Mathias Pribil ◽  
Miroslava Herbstová ◽  
Laura Susanna Lopez ◽  
Hans-Henning Kunz ◽  
...  
Keyword(s):  
Electron Transport ◽  
Photosystem Ii ◽  
Long Range ◽  
Narrow Range ◽  
Higher Plants ◽  
Regulatory Element ◽  
Photosynthetic Electron Transport ◽  
Electron Carrier ◽  
Mobile Electron ◽  
Electron Carriers

In photosynthetic electron transport, large multiprotein complexes are connected by small diffusible electron carriers, the mobility of which is challenged by macromolecular crowding. For thylakoid membranes of higher plants, a long-standing question has been which of the two mobile electron carriers, plastoquinone or plastocyanin, mediates electron transport from stacked grana thylakoids where photosystem II (PSII) is localized to distant unstacked regions of the thylakoids that harbor PSI. Here, we confirm that plastocyanin is the long-range electron carrier by employing mutants with different grana diameters. Furthermore, our results explain why higher plants have a narrow range of grana diameters since a larger diffusion distance for plastocyanin would jeopardize the efficiency of electron transport. In the light of recent findings that the lumen of thylakoids, which forms the diffusion space of plastocyanin, undergoes dynamic swelling/shrinkage, this study demonstrates that plastocyanin diffusion is a crucial regulatory element of plant photosynthetic electron transport.

Regulation of photosystem II by metabolic and environmental factors

1989 ◽  
Vol 323 (1216) ◽  
pp. 269-279 ◽  
Keyword(s):  
Electron Transport ◽  
Higher Plants ◽  
Photosynthetic Electron Transport ◽  
Thylakoid Membranes ◽  
Internal Factors ◽  
Regulatory Processes ◽  
Quenching Analysis ◽  
Intact Chloroplasts ◽  
Rate Of Dissipation

The thylakoid membranes of higher plants possess several mechanisms that control both the distribution and rate of dissipation of absorbed light. These mechanisms, which allow regulation of photosynthetic electron transport in response to alteration in external and internal factors, can be observed as the various processes that quench chlorophyll fluorescence. By using the 'light-doubling techniques’, together with analysis of quenching relaxation, it is possible to assess quantitatively the extents of these regulatory processes and to allow their interrelations to be studied. These techniques can be applied to in vitro systems or to leaves, and can be particularly useful when applied with electron-transport measurements and when models are used to aid interpretation. Results of quenching analysis at different light intensities in isolated thylakoids, intact chloroplasts, protoplasts, algae and leaves of a variety of species are presented.

scholarly journals The effects of oxygen solubility and high concentrations of salts on photosynthetic electron transport in chloroplast membranes

1984 ◽  
Vol 218 (2) ◽  
pp. 539-545 ◽  
Author(s):  
B Thomasset ◽  
J N Barbotin ◽  
D Thomas
Keyword(s):  
Electron Transport ◽  
Photosynthetic Electron Transport ◽  
Potassium Citrate ◽  
Potassium Ferricyanide ◽  
O2 Evolution ◽  
Oxygen Solubility ◽  
Chloroplast Membranes ◽  
Ferricyanide Reduction ◽  
High Concentrations ◽  
Stimulation Of

Chloroplast membranes were isolated in different media containing Hepes [4-(2-hydroxyethyl)-1-piperazine-ethanesulphonic acid] and high concentrations of sorbitol (0.33 M), potassium citrate (0.75 M) or Na2SO4 (1.0 M). Due to the complexity of the media, the oxygen solubility is strongly modified by high concentrations of salts (oxygen solubility for 0.33 M-sorbitol, 0.21 mmol/litre; for 0.75 M-potassium citrate, 0.121 mmol/litre; and for 1.0 M-Na2SO4, 0.112 mmol/litre). The knowledge of these values is necessary to interpret the rate of O2 evolution. For thylakoids isolated in ‘sorbitol buffer’ and then tested in high concentrations of potassium citrate, a slight stimulation of O2 evolution is observed (143-173 mumol of O2/h per mg of chlorophyll a) with potassium ferricyanide as electron acceptor. When we monitor the potassium ferricyanide reduction, no stimulation of electron transport is obtained even if the observed phenomenon is identical with the Photosystem-II oxygen evolution. In the same experiments no stimulation of the photophosphorylation was recorded, but when thylakoids are directly isolated in 0.75 M-potassium citrate, O2 evolution, ferricyanide reduction and photophosphorylation are inhibited by high concentrations of salts. The behaviour of thylakoids seems to be influenced by their initial treatment.

Inhibition of Photosystem II-Reactions in Blue-Green Algae by the Antisera to Lutein and Neoxanthin

1977 ◽  
Vol 32 (1-2) ◽  
pp. 118-124 ◽  
Author(s):  
Georg H. Schmid ◽  
Helga List ◽  
Alfons Radunz
Keyword(s):  
Electron Transport ◽  
Photosystem Ii ◽  
Green Algae ◽  
Higher Plants ◽  
Algal Species ◽  
Nostoc Muscorum ◽  
Blue Green Algae ◽  
Oscillatoria Chalybea ◽  
Electron Donation ◽  
Tetramethyl Benzidine

An antiserum to lutein agglutinates thylakoids of Nostoc muscorum and Oscillatoria chalybea. From this it follows that lutein is located in the outer surface of the thylakoid membrane of these blue-green algae. The same result is obtained for an antiserum to neoxanthin. As neoxanthin is supposed not to occur in blue-green algae it follows that in this case the antibody action should be directed towards a carotenoid with allenic structure. The antisera to lutein and neoxanthin inhibit in both investigated algal species photosynthetic electron transport on the oxygen-evolving side of photosystem II. Moreover, the inhibition sites of both antisera are identical in Nostoc muscorum and are located between the sites of electron donation of the artificial electron donors tetramethyl benzidene and diphenylcarbazide. In the case of the blue-green alga Oscillatoria chalybea the inhibition sites of both antisera differ. Whereas the inhibition site of the antiserum to neoxanthin lies again between the sites of electron donation of tetramethyl benzidine and di­phenylcarbazide, the inhibition site of the antiserum to lutein appears to be situated at least partially beyond the site of electron donation of tetramethyl benzidine. The degree of inhibition of electron transport reactions with Nostoc muscorum is for both antisera 50 - 60 per cent and is pH-dependent. The pH-optimum lies at pH 7.2 for the antiserum to neoxanthin and at 7.8 for the antiserum to lutein. In comparison to this data the same antisera inhibit electron transport in chloroplasts from higher plants only by 20%. This low degree of inhibition in higher plants is apparently due to the fact that the surfaces of the thylakoids are not accessible to antibodies within the grana. In contrast to this the thylakoid surfaces of blue-green algae are fully accessible because the thylakoids are unstacked. The thylakoids of Oscillatoria chalybea have the tendency towards aggregation. Therefore, the results concerning the accessibility of the carotenoids to antibodies are not so clear cut as with Nostoc muscorum.

Inhibition of Photosynthetic Electron Transport by Halogenated 4-Hydroxy-pyridines

1985 ◽  
Vol 40 (5-6) ◽  
pp. 391-399 ◽  
Author(s):  
A. Trebst ◽  
B. Depka ◽  
S. M. Ridley ◽  
A. F. Hawkins
Keyword(s):  
Electron Transport ◽  
Photosystem Ii ◽  
Photosystem I ◽  
Electron Flow ◽  
Essential Element ◽  
Photosynthetic Electron Transport ◽  
Cyclic Electron Flow ◽  
Acceptor Side

Abstract Herbicidal halogen substituted 4-hydroxypyridines are inhibitors of photosynthetic electron flow in isolated thylakoid membranes by interfering with the acceptor side of photosystem II. Tetrabromo-4-hydroxypyridine, the most active compound found, has a pI50-value of 7.6 in the inhibition of oxygen evolution in both the reduction of an acceptor of photosystem I and an acceptor of photosystem II. The new inhibitors displace both metribuzin and ioxynil from the membrane. The 4-hydroxypyridines, like ioxynil, have unimpaired inhibitor potency in Tristreated chloroplasts, whereas the DCMU-type family of herbicides does not. It is suggested that 4-hydroxypyridines are complementary to phenol-type inhibitors, and a common essential element is proposed. The 4-hydroxypyridines do not inhibit photosystem I or non-cyclic electron flow through the cytochrome b/f complex. But they do have a second inhibition site in photosynthetic electron transport since they inhibit ferredoxin-catalyzed cyclic electron flow, indicating an antimycin-like property. A comparison of the in vitro potency of the compounds with the in vivo potency shows no correlation. A major herbicidal mode of action of the group is related to the inhibition of carotenoid synthesis, and access to the chloroplast lamellae in vivo for inhibition of electron transport may be restricted.

scholarly journals LOW PHOTOSYNTHETIC EFFICIENCY 1 is required for light-regulated photosystem II biogenesis inArabidopsis

2018 ◽  
Vol 115 (26) ◽  
pp. E6075-E6084 ◽  
Author(s):  
Honglei Jin ◽  
Mei Fu ◽  
Zhikun Duan ◽  
Sujuan Duan ◽  
Mengshu Li ◽  
...  
Keyword(s):  
Electron Transport ◽  
Photosystem Ii ◽  
Photosynthetic Efficiency ◽  
Higher Plants ◽  
D1 Protein ◽  
Mrna Translation ◽  
Photosynthetic Electron Transport ◽  
Dependent Manner ◽  
Pentatricopeptide Repeat ◽  
Ppr Protein

Photosystem II (PSII), a multisubunit protein complex of the photosynthetic electron transport chain, functions as a water-plastoquinone oxidoreductase, which is vital to the initiation of photosynthesis and electron transport. Although the structure, composition, and function of PSII are well understood, the mechanism of PSII biogenesis remains largely elusive. Here, we identified a nuclear-encoded pentatricopeptide repeat (PPR) protein LOW PHOTOSYNTHETIC EFFICIENCY 1 (LPE1; encoded by At3g46610) inArabidopsis, which plays a crucial role in PSII biogenesis. LPE1 is exclusively targeted to chloroplasts and directly binds to the 5′ UTR ofpsbAmRNA which encodes the PSII reaction center protein D1. The loss ofLPE1results in less efficient loading of ribosome on thepsbAmRNA and great synthesis defects in D1 protein. We further found that LPE1 interacts with a known regulator ofpsbAmRNA translation HIGH CHLOROPHYLL FLUORESCENCE 173 (HCF173) and facilitates the association of HCF173 withpsbAmRNA. More interestingly, our results indicate that LPE1 associates withpsbAmRNA in a light-dependent manner through a redox-based mechanism. This study enhances our understanding of the mechanism of light-regulated D1 synthesis, providing important insight into PSII biogenesis and the functional maintenance of efficient photosynthesis in higher plants.

Interaction of Photosystem II Herbicides with Bicarbonate and Formate in Their Effects on Photosynthetic Electron Flow

1984 ◽  
Vol 39 (5) ◽  
pp. 374-377 ◽  
Author(s):  
J. J. S. van Rensen
Keyword(s):  
Electron Transport ◽  
Photosystem Ii ◽  
Electron Flow ◽  
Photosynthetic Electron Transport ◽  
Hill Reaction ◽  
Amaranthus Hybridus ◽  
Apparent Affinity ◽  
Photosynthetic Electron Flow ◽  
Different Characteristics ◽  
The Hill

The reactivation of the Hill reaction in CO2-depleted broken chloroplasts by various concentrations of bicarbonate was measured in the absence and in the presence of photosystem II herbicides. It appears that these herbicides decrease the apparent affinity of the thylakoid membrane for bicarbonate. Different characteristics of bicarbonate binding were observed in chloroplasts of triazine-resistant Amaranthus hybridus compared to the triazine-sensitive biotype. It is concluded that photosystem II herbicides, bicarbonate and formate interact with each other in their binding to the Qв-protein and their interference with photosynthetic electron transport.

X-Ray Structure Analysis of a Cyanoacrylate Inhibitor of Photosystem II Electron Transport

1991 ◽  
Vol 46 (1-2) ◽  
pp. 93-98 ◽  
Author(s):  
Helen G. McFadden ◽  
Donald C. Craig ◽  
John L. Huppatz ◽  
John N. Phillips
Keyword(s):  
Electron Transport ◽  
Photosystem Ii ◽  
Chlorophyll Concentration ◽  
Photosynthetic Electron Transport ◽  
Hill Reaction ◽  
Ps Ii ◽  
X Ray ◽  
High Affinity ◽  
Modelling Studies ◽  
Intramolecular Hydrogen

Abstract X-ray crystallographic data for the highly potent cyanoacrylate photosynthetic electron transport inhibitor, (Z)-ethoxyethyl 3-(4-chlorobenzylamino)-2-cyano-4-methylpent-2-enoate, are presented. This compound has a particularly high affinity for the photosystem II (PS II) herbicide receptor with a p I50 value of 9.5 (in the Hill reaction under uncoupled condi­tions with a chlorophyll concentration of 0.1 μg/ml). Data regarding the structure of small li­gands, such as this potent cyanoacrylate, which bind to the site with high affinity may be used to provide the basis for modelling studies of PS II/herbicide complexes. The X-ray data presented confirm the Z-stereochemistry of active cyanoacrylates and demonstrate the pres­ence of a planar core stabilized by an intramolecular hydrogen bond between the ester car­bonyl oxygen and a benzylamino hydrogen atom. In order to assess the importance of the benzylamino -NH -group in this type of cyanoacrylate, analogues containing a methylene group in its place were synthesized and found to be 100-and 1000-fold less active as Hill inhibitors.

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