Oxygen-exchange studies in Chlamydomonas mutants deficient in photosynthetic electron transport: Evidence for a Photosystem II-dependent oxygen uptake in vivo

1988 ◽  
Vol 936 (3) ◽  
pp. 319-324 ◽  
Author(s):  
Gilles Peltier ◽  
Pierre Thibault
Keyword(s):  
Electron Transport ◽  
Photosystem Ii ◽  
Oxygen Uptake ◽  
Photosynthetic Electron Transport ◽  
Oxygen Exchange ◽  
Chlamydomonas Mutants

Research note: Energy partitioning in photosystem II complexes subjected to photoinhibitory treatment

2007 ◽  
Vol 34 (3) ◽  
pp. 214 ◽  
Author(s):  
Dmytro Kornyeyev ◽  
Luke Hendrickson
Keyword(s):  
Electron Transport ◽  
Photosystem Ii ◽  
Excitation Energy ◽  
Chlorophyll A ◽  
Chlorophyll A Fluorescence ◽  
Photosynthetic Electron Transport ◽  
Energy Partitioning ◽  
Simple Equations

Chlorophyll a fluorescence measured in vivo is frequently used to study the role of different processes influencing the distribution of excitation energy in PSII complexes. Such studies are important for understanding the regulation of photosynthetic electron transport. However, at the present time, there is no unified methodology to analyse the energy partitioning in PSII. In this article, we critically assess several approaches recently developed in this area of research and propose new simple equations, which can be used for de-convolution of non-photochemical energy quenching in PSII complexes.

Irreversibly Binding Photosynthetic Electron Transport Inhibitors II. Halogen-Substituted 1,4-Naphthoquinones and Halogenmethyl-1,4-quinones

1987 ◽  
Vol 42 (6) ◽  
pp. 693-697 ◽  
Author(s):  
Walter Oettmeier ◽  
Ralf Dostatni ◽  
Hans-Joachim Santel
Keyword(s):  
Electron Transport ◽  
Photosystem Ii ◽  
Binding Affinity ◽  
Alkylating Agents ◽  
Photosynthetic Electron Transport ◽  
Hydrogen Halide ◽  
Covalent Linkage ◽  
Transport Inhibitors ◽  
Preincubation Time

Several halogen-substituted 1,4-naphthoquinones have been synthesized and found to be effective photosystem II inhibitors. Due to their properties as vinylogous acid halides they can react with nucleophiles under formation of a covalent linkage. In their presence other photosystem II herbicides show a decreased binding affinity. This decrease is dependent from the preincubation time. Halogenmethyl-1,4-quinones also turned out to be efficient photosystem II inhibitors and. in addition, possessed herbicidal in vivo activity. They function as “bioreductive alkylating agents” in a way that after reduction they can split off hydrogen halide under formation of a o-quinonemethide. This quinonemethide can react with nucleophilic groups in proteins.

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.

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.

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.

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.

The Phycobihproteids in Cyanophora paradoxa as Accessoric Pigments and Nitrogen Storage Proteins

1983 ◽  
Vol 38 (11-12) ◽  
pp. 972-977 ◽  
Author(s):  
Hainfried E. A. Schenk ◽  
Jürgen Hanf ◽  
Margarete Neu-Müller
Keyword(s):  
Electron Transport ◽  
Stress Proteins ◽  
Nitrogen Starvation ◽  
Storage Proteins ◽  
Photosynthetic Electron Transport ◽  
Lower Degree ◽  
Nitrogen Storage ◽  
Cyanophora Paradoxa ◽  
Free Living

The phycobiliproteids of cyanobacteria have two functions. They are accessoric pigments for the light-dependent photosynthetic electron transport, and, secondly, they are storage proteins. Cyanocyta korschikoffiana, the endocyanelle of Cyanophora paradoxa, a hardly adapted endocytobiotic cyanobacterium, is responsible for the photoautotrophy of the host flagellate. The biosynthesis of the phycobiliproteids takes place in the endocyanelles and is reversible. Under nitrogen starvation the phycobiliproteids were disintegrated again, in contrast to the carotenoids (and in a lower degree to chlorophyll), whose contents rem ain more constant in the cells, as shown by in vivo measurements. Therefore, it is concluded that sim ilar to the function in free living cyanobacteria the phycobiliproteids of C. paradoxa also serve as storage substances (“stress proteins”). This opinion is supported by experiments with chloramphenicol

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