The Presence of Malate Dehydrogenase in Thylakoids of Anabaena cylindrical Nostoc muscorum and Chlorogloeopsis fritschii

1990 ◽  
Vol 45 (3-4) ◽  
pp. 249-252
Author(s):  
A.-K. J. Sallal ◽  
N. A. Nimer

Abstract The location of malate dehydrogenase in the cyanobacteria, Anabaena cylindrica, Nostoc muscorum and Chlorogloeopsis fritschii was investigated by the fractionation of cell-free extracts. The bulk of the enzyme activity was associated with the thylakoid membrane fraction, which also exhibited complete photosynthetic electron transport reactions. Malate dehydrogenase activity and photosystem II activities were inhibited by homologous antisera raised against isolated thylakoid membranes.

Isolated heterocysts of the N 2 -fixing Anabaena cylindrica , prepared by a combination of lysozyme and Yeda press treatments, are metabolically active with over 90% of the measurable nitrogenase activity being located in the heterocyst preparations after disruption of the intact filaments. The photosynthetic activities of such isolated heterocysts are characterized by an inability to carry out the photolysis of water or to fix CO 2 . The lack of O 2 evolution appears to be due in part to the deple­tion during heterocyst differentiation of Mn, a central component of the photosystem II reaction centre in O 2 -evolving algae. There is evidence that components of the photosynthetic electron transport chain on the reducing side of the photosystem II reaction centre are present and functional in heterocysts. These include cytochrome c 554 , plastocyanin, plastoquinone, cytochrome b 559 , P700, cytochrome b 563 , and iron-sulphur proteins which appear to correspond to centre A and centre B of higher plant chloroplasts. Soluble, or loosely bound ferredoxin is also present and involved in electron transport from ferredoxin to NADP. Isolated heterocysts photoreduce methylviologen when reduced 2,6-dichlorophenolindophenol and diphenylcarbazide serve as electron donors. They show P700 photo-oxidation and photoreduction, photosyn­thetic electron transport which is inhibited by 2,5-dibromo-3-methyl-6-isopropyl- p -benzoquinone an antagonist of plastoquinone, photophos­phorylation, oxidative phosphorylation and ferredoxin-NADP oxido-reductase mediated reactions. The photosynthetic modifications of the heterocyst are such that electron transport and the generation of ATP for nitrogenase can occur without concomitant O 2 evolution and with­out nitrogenase having to compete with CO 2 fixation for ATP and reductant.


1993 ◽  
Vol 48 (3-4) ◽  
pp. 163-167
Author(s):  
Koichi Yoneyama ◽  
Yoshihiro Nakajima ◽  
Masaru Ogasawara ◽  
Hitoshi Kuramochi ◽  
Makoto Konnai ◽  
...  

Abstract Through the studies on structure-activity relationships of 5-acyl-3-(1-aminoalkylidene)-4-hydroxy-2 H-pyran-2,6(3 H)-dione derivatives in photosystem II (PS II) inhibition, overall lipophilicity of the molecule was found to be a major determinant for the activity. In the substituted N -benzyl derivatives, not only the lipophilicity but also the electronic and steric characters of the substituents greatly affected the activity. Their mode of PS II inhibition seemed to be similar to that of DCMU , whereas pyran-enamine derivatives needed to be highly lipophilic to block the electron transport in thylakoid membranes, which in turn diminished the permeability through biomembranes.


1984 ◽  
Vol 39 (5) ◽  
pp. 374-377 ◽  
Author(s):  
J. J. S. van Rensen

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.


1991 ◽  
Vol 46 (1-2) ◽  
pp. 93-98 ◽  
Author(s):  
Helen G. McFadden ◽  
Donald C. Craig ◽  
John L. Huppatz ◽  
John N. Phillips

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.


2020 ◽  
Vol 117 (26) ◽  
pp. 15354-15362 ◽  
Author(s):  
Ricarda Höhner ◽  
Mathias Pribil ◽  
Miroslava Herbstová ◽  
Laura Susanna Lopez ◽  
Hans-Henning Kunz ◽  
...  

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.


1980 ◽  
Vol 35 (3-4) ◽  
pp. 293-297 ◽  
Author(s):  
P. V. Sane ◽  
Udo Johanningmeier

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.


1981 ◽  
Vol 36 (9-10) ◽  
pp. 848-852 ◽  
Author(s):  
W. Draber ◽  
H. J. Knops ◽  
A. Trebst

Abstract Several substituted diphenylethers were found to be effective inhibitors of photosynthetic electron flow in isolated thylakoid membranes from spinach chloroplasts. T heir site of inhibition was localized with artificial acceptor and donor systems. The phenylether of an alkyl substituted nitrophenol is prim arely inhibiting electron flow after plastoquinone function whereas a dinitro-phenylether of a phenyl substituted nitrophenol is inhibiting before plastoquinone function. Therefore certain diphenylethers interfere with plastoquinone function at the oxidation or reduction site, depending on the substitution.


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