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.

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 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.

Electron Transport to Assimilatory Nitrate Reductase in A zotobacter vinelandii

1981 ◽  
Vol 36 (11-12) ◽  
pp. 1030-1035 ◽  
Author(s):  
Hermann Bothe ◽  
Klaus-Peter Häger
Keyword(s):  
Electron Transport ◽  
Nitrate Reductase ◽  
Nitrate Reduction ◽  
Azotobacter Vinelandii ◽  
Additive Effects ◽  
Electron Carrier ◽  
Transport Chain ◽  
Solubilized Enzyme ◽  
Electron Carriers ◽  
Bound Electron

Abstract Assimilatory nitrate reductase was particle-bound in extracts from Azotobacter vinelandii. Nitrate reduction by particle fractions was dependent on NADPH and a particle-bound electron carrier. When the enzyme was solubilized from the particles by treatment with detergents, the particle-bound electron carrier could be substituted by ferredoxin or flavodoxin. Flavodoxin reduced at the expense of photoreduced deazaflavin was much more efficient than ferredoxin in transferring electrons to nitrate reductase. The addition of both ferredoxin and flavodoxin to the assays with photoreduced deazaflavin gave additive effects. With the solubilized enzyme, NADPH only poorly supported nitrate reduction even after the addition of electron carriers. The experiments indicate that A. vinelandii utilizes an electron transport chain between NADPH and nitrate reductase with some properties similar to those described for the generation of reductants to nitrogenase.

Studies about the Mechanism of Herbicidal Interaction with Photosystem II in Isolated Chloroplasts

1979 ◽  
Vol 34 (11) ◽  
pp. 1010-1014 ◽  
Author(s):  
Gernot Renger
Keyword(s):  
Electron Transport ◽  
Photosystem Ii ◽  
Excitation Energy ◽  
Electron Acceptor ◽  
Functional Organization ◽  
Regulatory Element ◽  
Release Kinetics ◽  
Acceptor Side ◽  
Receptor Sites ◽  
Isolated Chloroplasts

Abstract Based on the functional organization scheme of system-II-electron transport and its modification by different procedures a proteinaceous component enwrapping the redox components (plastoquinone molecules) of the acceptor side (thereby acting as regulatory element) is inferred to be the unique target for herbicidal interaction with system II. This proteinaceous component, which is attacked by trypsin, provides the receptor sites for the herbicides. Studies of the release kinetics in trypsinated chloroplasts of the inhibition of oxygen evolution with K3 [Fe (CN)6] as electron acceptor indicates, that there exists a binding area with different specific subreceptor sites rather than a unique binding site for the various types of inhibitors. Furthermore, trypsination of the proteinaceous component enhances the efficiency of the plastoquinone pool to act as a non-photochemical quencher for excitation energy.

Inhibition by Tetranitromethane of Photosynthetic Electron Transport from Water to Photosystem II in Chloroplasts

1980 ◽  
Vol 35 (3-4) ◽  
pp. 293-297 ◽  
Author(s):  
P. V. Sane ◽  
Udo Johanningmeier
Keyword(s):  
Electron Transport ◽  
Photosystem Ii ◽  
Electron Flow ◽  
Ph Dependence ◽  
Photosynthetic Electron Transport ◽  
Donor Side ◽  
Ps Ii ◽  
Diphenyl Carbazide ◽  
Low Concentrations ◽  
Sh Group

Abstract Low concentrations (10 µM) of tetranitromethane inhibit noncyclic electron transport in spinach chloroplasts. A study of different partial electron transport reactions shows that tetranitromethane primarily interferes with the electron flow from water to PS II. At higher concentrations the oxidation of plastohydroquinone is also inhibited. Because diphenyl carbazide but not Mn2+ ions can donate electrons efficiently to PS II in the presence of tetranitromethane it is suggested that it blocks the donor side of PS II prior to donation of electrons by diphenyl carbazide. The pH dependence of the inhibition by this protein modifying reagent may indicate that a functional-SH group is essential for a protein, which mediates electron transport between the water splitting complex and the reaction center of PS II.

Hydrophilic Photosystem II Inhibitors: Cyanoacrylate Thiolate Salts

1990 ◽  
Vol 45 (5) ◽  
pp. 343-347 ◽  
Author(s):  
John N. Phillips
Keyword(s):  
Brassica Napus ◽  
Electron Transport ◽  
Photosystem Ii ◽  
Sodium Salt ◽  
Slow Rate ◽  
Membrane Lipids ◽  
Photosynthetic Electron Transport

Cyanoacrylate thiolate salts such as the sodium salt of ethoxyethyl-3-p-chlorobenzylthio-2-cyano-3-mercapto acrylate have been shown to be relatively slow binding, potent inhibitors of photosynthetic electron transport, that are equally active against thylakoids isolated from atrazine-susceptible and atrazine-resistant Brassica napus seedlings. It has been suggested that their mode of binding involves the substituted benzyl group interacting with the membrane lipids and the thiolate ion interacting in the region of the histidine215 residue of the D1 peptide, close to the non-heme Fe centre. This, together with their slow rate of binding, has led to the thiolate salts being classified as phenol type inhibitors.

2-Anilino-1.3.4-thiadiazole, Hemmstoffe der oxidativen und photosynthetischen Phosphorylierung

1975 ◽  
Vol 30 (3-4) ◽  
pp. 183-189 ◽  
Author(s):  
G. Schäfer ◽  
A. Trebst ◽  
K. H. Büchel
Keyword(s):  
Electron Transport ◽  
Photosystem Ii ◽  
Oxidative Phosphorylation ◽  
Benzene Ring ◽  
Inhibitory Action ◽  
Substituent Effects ◽  
Photosynthetic Electron Transport ◽  
Liver Mitochondria ◽  
Rat Liver Mitochondria ◽  
Mitochondrial Oxidative Phosphorylation

Abstract 2-anilino-1,3,4-thiadiazoles carrying various substituents in the 5-position as well as in the benzene-ring were synthesized. The compounds were tested with rat-liver-mitochondria and with spinach-chloroplasts and revealed to be potent uncouplers of both, oxidative and photosynthetic phosphorylation, with p I50-values rangeing from 6.79 to 4.05. At higher concentration all compounds are inhibitors of the Hillreaction. In mitochondria a fair correlation exists between pKa of the acidic NH-group and the uncoupling activity; a maximum is obtained around pKa= 6 .8 , whereas in chloroplasts activity is shifted to more acid pKa-values. The compounds meet the requirements for uncouplers according to the chemi-osmotic theory, being lipophilic weak acids. N-methylation causes total loss of activity in mitochondrial oxidative phosphorylation. The inhibitory action on photosynthetic electron transport is located within photosystem II. This latter activity is almost independent of substituent effects in contrast to uncoupling of either respiratory- or photo-phosphorylation

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