The site of electron transport inhibition by bentazon (3-isopropyl-1H-2,1,3-benzothiadiazin-(4)3H-one 2,2-dioxide) in isolated chloroplasts

1982 ◽  
Vol 60 (4) ◽  
pp. 409-412 ◽  
Author(s):  
Rungsit Suwanketnikom ◽  
Kriton K. Hatzios ◽  
Donald Penner ◽  
Duncan Bell

The effect of bentazon (3-isopropyl-1H-2,1,3-benzathiadiazin-(4)3H-one 2,2-dioxide) on various photochemical reactions of isolated spinach (Spinacea oleracea L.) chloroplasts was studied at concentrations 0, 5, 15, 45, and 135 μM. Bentazon at a concentration of 135 μM strongly inhibited uncoupled electron transport from water to ferricyanide or to methylviologen with inhibition percentages greater than 90%. Photosystem II mediated electron transport from water to oxidized diaminodurene, with 2,5-dibromo-3-methyl-6-isopropyl-p-benzoquinone (DBMIB) blocking photosystem I, was also strongly inhibited by bentazon at 135 μM but less with lower concentrations of bentazon. Photosystem I mediated transfer of electrons from diaminodurene to methylviologen, with 3,4-dichlorophenyl-1,1-dimethylurea (DCMU) blocking photosystem II, was not inhibited by bentazon at any concentration examined. Transfer of electrons from catechol to methylviologen in hydroxylamine-treated chloroplasts was inhibited by bentazon, and the inhibition percentages were again concentration dependent. The data indicate that the site of bentazon inhibition of the photosynthetic electron transport is at the reducing side of photosystem II, between the primary electron acceptor Q and plastoquinone.


1978 ◽  
Vol 170 (2) ◽  
pp. 373-378 ◽  
Author(s):  
P Heathcote ◽  
D L Williams-Smith ◽  
M C W Evans

An e.p.r. spectrum of the reduced form of the electron-transport component (X), thought to be the primary electron acceptor of Photosystem I, was obtained. By using line-shape simulations of this component and the free-radical e.p.r. signal I of the oxidized reaction-centre chlorophyll (P700), it was possible to determine the ratio of the number of electron spins to which these signals correspond in Photosystem-I particles under a variety of conditions. On illumination at cryogenic temperatures of Photosystem-I preparations, in which both bound iron-sulphur centres A and B were reduced, the measured ratio of free radical to component X varied between 1.04 and 2.23, with an average value of 1.54 +/- 0.18 where a Gaussian line-shape is assumed for the component-X signal in the simulation. The error in this measurement is estimated to be up to 50%. In a similar way component X and centre A of the bound iron-sulphur protein were quantified, the ratio between these two components varying between 1.26 and 0.61 with an average value of 0.75 +/- 0.06. These results indicate that the quantitative relationship, in terms of net electron spins, between centre A, component X and P700 is of the order to be expected if component X is indeed the primary electron acceptor in Photosystem I and a component of the photosynthetic electron-transport chain.



Weed Science ◽  
1979 ◽  
Vol 27 (3) ◽  
pp. 300-308 ◽  
Author(s):  
P. E. Brewer ◽  
C. J. Arntzen ◽  
F. W. Slife

The effects of atrazine [2-chloro-4-(ethylamino)-6-(isopropylamino)-s-triazine], cyanazine {2-[[4-chloro-6-(ethylamino)-s-triazin-2-yl] amino]-2-methylpropionitrile}, and procyazine {2-[[4-chloro-6-(cyclopropylamino)-1,3,5-triazine-2-yl] amino]-2-methylpropanenitrile} on the photochemical reactions of isolated pea (Pisum sativum L. ‘Progress #9 Dwarf’) chloroplasts were studied. Atrazine, cyanazine, and procyazine inhibited electron transport but did not uncouple photophosphorylation. The primary site of inhibition for all three herbicides was on the reducing side of photosystem II; the electron transfer step between the primary electron acceptor (Q) and the plastoquinone pool of the electron transport chain is suggested as the site of action of all three herbicides. The amount of inhibition of electron transport observed after addition of herbicide to isolated chloroplasts was time-dependent for cyanazine and procyazine but not for atrazine. This was apparently due to a slower partitioning of cyanazine and procyazine from the aqueous phase of the reaction solution into the highly hydrophobic environment within the chloroplast membrane. Treatment of the thylakoid membranes with detergent reduced the time-dependent inhibitory nature of cyanazine and procyazine, and the ability of atrazine to block electron transport. A photosystem II-dependent electron transport assay and a chlorophyll fluorescence induction assay were used to determine the inhibitory potentials of atrazine, cyanazine, and procyazine. After allowing for differences in the rate of membrane penetration, I50 values of approximately 2 × 10−7 M were determined for each of the three herbicides.



1970 ◽  
Vol 25 (10) ◽  
pp. 1157-1159 ◽  
Author(s):  
A. Trebst ◽  
E. Harth ◽  
W. Draber

A halogenated benzoquinone has been found to inhibit the photosynthetic electron transport system in isolated chloroplasts. 2·10-6ᴍ of dibromo-thymoquinone inhibit the Hill- reaction with NADP, methylviologen or anthraquinone to 100%, but do not effect the photoreduction of NADP at the expense of an artificial electron donor. The Hill - reaction with ferricyanide is inhibited even at the high concentration of 2·10-5ᴍ of dibromo-thymoquinone to only 60%. The remaining reduction in the presence of the inhibitor reflects the rate of ferricyanide reduction by photosystem II. It is concluded that the inhibition of electron transport by the quinone occurs between photosystem I and II and close to or at the functional site of plastoquinone.



1987 ◽  
Vol 42 (11-12) ◽  
pp. 1265-1268
Author(s):  
B. Lotina-Hennsen ◽  
A . Garcia ◽  
M. Aguilar ◽  
M. Albores

The midpoint potential of BFO, the sensitivity of its photoreduction to DCM, DBMIB and KCN, and the photosystem I activity, suggest that the photoreduction of BFO in the chloroplast is at the primary electron acceptor x of photosystem I. and is irreversible. Rates of electron transport are similar in basal phosphorylating or uncoupled conditions al­though electron transport is coupled to photophosphorylation.



1975 ◽  
Vol 30 (7-8) ◽  
pp. 489-498 ◽  
Author(s):  
Christian Holzapfel ◽  
Robert Bauer

Abstract A computer model describing the “Z-scheme” of photosynthetic electron transport in terms of reduction and oxydation of coupled redox pools was built up. Starting from a certain initial state corresponding to the dark adapted state of the photosynthetic system the reduction and reoxidation levels of the pools were calculated during adaptation of the system to a steady state in the light. The changes of calculated redox levels were compared with experimental results of fluorescence and oxygen evolution induction curves. It is shown that the transients in prompt fluorescence and oxygen evolution can be described by reduction and reoxidation of the primary electron acceptor pool and the electron donor pool of photosystem II due to reduction and oxidation of the other pools during adaptation to light. The first depression D in the fluorescence induction curve is explained by the existence of a redox pool X between the primary electron acceptor pool Q of photosystem II and plastoquinone. It is shown that DCMU blocks the electron flow between Q and X. Furthermore, it is shown that the inhibitor DBMIB probably not only blocks the electron flow but also causes a successive disconnection of the plastoquinone pool from the electron transport chain.





1972 ◽  
Vol 27 (4) ◽  
pp. 445-455 ◽  
Author(s):  
Heinrich Strotmann ◽  
Christa Von Gösseln

Photosystem I related phosphorylation of isolated chloroplasts was investigated with special reference to the stoichiometry between ATP production and electron transprt (ATP: 2e⊖). The system studied contained DCMU to inhibit electron flow from photosystem II, ascorbate and DPIP to supply electrons to photosystem I, and methylviologen as electron acceptor. The following results were obtained:1. Basal electron transport is stimulated by the addition of the phosphorylating system, indicating that phosphorylation is really coupled to non-cyclic electron flow. The ratio ATP: 2e⊖ is 1, when the increase of electron flow obtained by the addition of ADP and phosphate is correlated to phosphorylation. This ratio is constant upon varying several parameters including DPIP concentration and light intensity.2. In the absence of methylviologen a DPIP catalyzed cyclic phosphorylation takes place (cf. I. c.7, 11, 12). Phosphorylation is not increased by the addition of methylviologen, indicating that both, the cyclic DPIP mediated and the non-cyclic system are coupled to the same phosphorylation site and limited by the same reaction step.3. In the absence of oxygen a methylviologen supported cyclic phosphorylation occurs. Comparing optimum rates, phosphorylation under these conditions is about twice as high as in the noncyclic system. Therefore we conclude that two phosphorylation sites are involved in methylviologen catalyzed cyclic electron transport. This system is sensitive against trypsin treatment of the chloroplasts, whereas the linear system is not.4. The two cyclic systems as well as the non-cyclic system are coupled to reversible proton uptake. Furthermore the linear system exhibits an irreversible uptake of hydrogen ions, which is stoichiometric to electron flow. From the reversible and the irreversible components of the pH changes the ratio of the proton pump to electron transprt can be calculated. Under steady state conditions the ration H⨁ : e⊖ approaches 1.



1979 ◽  
Vol 34 (11) ◽  
pp. 1021-1023 ◽  
Author(s):  
J. J. S. van Rensen ◽  
J. H. Hobé

Abstract The herbicide 4,6-dinitro-o-cresol inhibits electron transport to ferricyanide and non-cyclic photophosphorylation for 50% at about 15 μm. At higher concentrations the photosystem I depen­dent Mehler reaction ascorbate/dichlorophenolindophenol to methyl viologen is stimulated, while cyclic photophosphorylation is inhibited. The herbicide thus is an inhibitory uncoupler. Although the chemical structure of 4,6-dinitro-o-cresol is different from that of the diuron-type herbicides, its site and mechanism of action is similar. Both 4,6-dinitro-o-cresol and diuron inhibit electron transport between the primary electron acceptor of Photosystem II and the plastoquinone pool. This causes a closing of the reaction centers of Photosystem II. The interaction with the inhibited molecule however is different for the two herbicides.



1979 ◽  
Vol 34 (11) ◽  
pp. 1010-1014 ◽  
Author(s):  
Gernot Renger

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.



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