Steady State of Photosynthetic Electron Transport in Cells of the Cyanophyti Synechocystis PCC 6714 Having Different Stoichiometry between PS I and PS II: Analysis of Flash-Induced Oxidation-Reduction of Cytochrome f and P700 under Steady State of Photosynthesis

1991 ◽  
Vol 32 (2) ◽  
pp. 213-222 ◽  
Author(s):  
Akio Murakami ◽  
Yoshihiko Fujita
Keyword(s):  
Steady State ◽  
Electron Transport ◽  
Photosynthetic Electron Transport ◽  
Cytochrome F ◽  
Ps Ii ◽  
Ps I ◽  
Oxidation Reduction ◽  
Synechocystis Pcc 6714 ◽  
In Cells

Photoinactivation of Photosynthetic Electron Transport under Anaerobic and Aerobic Conditions in Isolated Thylakoids of Spinach

1992 ◽  
Vol 47 (1-2) ◽  
pp. 63-68 ◽  
Author(s):  
Rekha Chaturvedi ◽  
M. Singh ◽  
P. V. Sane
Keyword(s):  
Electron Transport ◽  
Photosynthetic Electron Transport ◽  
Oxygen Evolving Complex ◽  
Reaction Centre ◽  
Ps Ii ◽  
Ps I ◽  
S2 State ◽  
The Stability ◽  
Oxygen Evolving ◽  
Spinach Thylakoids

Abstract The effect of exposure to strong white light on photosynthetic electron transport reactions of PS I and PS II were investigated in spinach thylakoids in the absence or presence of oxygen. Irrespective of the conditions used for photoinactivation, the damage to PS II was always much more than to PS I. Photoinactivation was severe under anaerobic conditions compared to that in air for the same duration. This shows that the presence of oxygen is required for prevention of photoinactivation of thylakoids. The susceptibility of water-splitting complex in photoinactivation is indicated by our data from experiments with chloride-deficient chloroplast membranes wherein it was observed that the whole chain electron transport from DPC to MV was much less photoinhibited than that from water. The data from the photoinactivation experiments with the Tris-treated thylakoids indicate another photodam age site at or near reaction centre of PS II. DCMU-protected PS II and oxygen-evolving complex from photoinactivation. DCMU protection can also be interpreted in terms of the stability of the PS II complex when it is in S2 state.

Changes in Photosynthetic Apparatus in the Juvenile Rice Canopy and a Possible Function of Photosystem I in the Bottom Leaves

1999 ◽  
Vol 54 (11) ◽  
pp. 915-922 ◽  
Author(s):  
Jun-ya Yamazaki ◽  
Yasumaro Kamimura ◽  
Yasutomo Sugimura
Keyword(s):  
Electron Transport ◽  
Photosynthetic Apparatus ◽  
Photosynthetic Performance ◽  
Cytochrome F ◽  
Transport Capacity ◽  
Ps Ii ◽  
Electrochromic Shift ◽  
The Third ◽  
Ps I ◽  
Light Utilization

Abstract Changes in the photosynthetic apparatus and relative antenna sizes of photosystem (PS) I and PS II were measured in the rice canopy. We used juvenile rice seedlings to examine light utilization and its absorption in the bottom leaves and obtained the following results: (1) When referred to chlorophyll (Chl), levels of the electrochromic shift at 550 nm and cytochrome ƒ decreased from the sixth to the third leaves, but there was no loss of pigment (P)-700. As a consequence, the PS II/PS I ratio significantly decreased from 1.5 in the sixth leaves to 0.9 in the third leaves. (2) The electron transport capacity in the sixth leaves was 1.5-times larger than that in the third leaves. (3) The levels of cytochrome b6 referred to Chl were almost constant from top to bottom. (4) The photosynthetic performance of the leaf de­creased concomitant with the depth, whereas the respiration was slightly increased. From these results, we hypothesize that there are maintenance mechanisms when the imbalances of light absorption and electron transport capacity occur in the bottom leaves.

Interactions of Herbicides with Photosynthetic Electron Transport

Weed Science ◽  
1991 ◽  
Vol 39 (3) ◽  
pp. 458-464 ◽  
Author(s):  
E. Patrick Fuerst ◽  
Michael A. Norman
Keyword(s):  
Electron Transport ◽  
Membrane Lipids ◽  
Electron Flow ◽  
Membrane Integrity ◽  
D1 Protein ◽  
Photosynthetic Electron Transport ◽  
Peroxidation Of Lipids ◽  
Ps Ii ◽  
Ps I ◽  
Sulfur Protein

The two primary sites of herbicide action in photosynthetic electron transport are the inhibition of photosystem II (PS II) electron transport and diversion of electron flow through photosystem I (PS I). PS II electron transport inhibitors bind to the D1 protein of the PS II reaction center, thus blocking electron transfer to plastoquinone. Inhibition of PS II electron transport prevents the conversion of absorbed light energy into electrochemical energy and results in the production of triplet chlorophyll and singlet oxygen which induce the peroxidation of membrane lipids. PS I electron acceptors probably accept electrons from the iron-sulfur protein, Fa/Fb. The free radical form of the herbicide leads to the production of hydroxyl radicals which cause the peroxidation of lipids. Herbicide-induced lipid peroxidation destroys membrane integrity, leading to cellular disorganization and phototoxicity.

Die Wirkung 2.3-substituierter Naphthochinone auf einzellige Algen und isolierte Spinatchloroplasten/ The Effect of 2,3-Substituted Naphthoquinones on Unicellular Algae and Isolated Spinach Chloroplasts

1979 ◽  
Vol 34 (11) ◽  
pp. 961-963 ◽  
Author(s):  
Klaus Bauer ◽  
Helmu Kodier
Keyword(s):  
Electron Transport ◽  
Dark Respiration ◽  
Electron Flow ◽  
Photosynthetic Electron Transport ◽  
Flow Mode ◽  
Ps Ii ◽  
Spinach Chloroplasts ◽  
Ps I ◽  
Low Concentrations ◽  
Strong Stimulation

Abstract Short term effects of 2-(C-dichloro-acetylamino)-3-chloro-1,4-naphthoquinone (Hoe 13465, quinonamid*) and 2-amino-3-chloro-1,4-naphthoquinone (Hoe 17399, 06K-quinone) on cell suspensions of Chlorella vulgaris, Anabaena flos aquae, Porphyridium cruentum, and on isolated spinach chloroplasts were studied. The results clearly show that both substances inhibit the photosynthetic O2 production of algal suspensions as well as the electron transport of PS II in spinach chloroplasts. PS I is not inhibited by the action of the two algicides. At low concentrations quinonamid acts as a photosynthetic electron transport blocker, whereas Hoe 17399 is a weak inhibitor of photosynthetic electron flow. Mode of action of the two naphthoquinones is discussed. Both naphthoquinone derivatives can operate as an electron acceptor for PS I at low concentra­tions (10-5-10-6м). In addition there is observed a strong stimulation of dark respiration in algal cells induced by both of the compounds, Hoe 17399 causes a much higher stimulation rate than quinonamid does.

scholarly journals Photosynthetic performance of Salvinia natans exposed to chromium and zinc rich wastewater

2008 ◽  
Vol 20 (1) ◽  
pp. 61-70 ◽  
Author(s):  
Bhupinder Dhir ◽  
P. Sharmila ◽  
P. Pardha Saradhi
Keyword(s):  
Electron Transport ◽  
Assimilation Efficiency ◽  
Carbon Assimilation ◽  
Photosynthetic Electron Transport ◽  
Redox Status ◽  
Photosynthetic Performance ◽  
Pyridine Nucleotides ◽  
Ps Ii ◽  
Ps I ◽  
Salvinia Natans

Investigations were carried out to evaluate alterations in photosynthetic performance of Salvinia natans (L.) exposed to chromium (Cr) and zinc (Zn) rich wastewater. Accumulation of high levels of Cr and Zn in plants affected photosynthetic electron transport. Photosystem- (PS) II-mediated electron transport was enhanced in plants exposed to Cr rich wastewater while a decline was observed in Zn-exposed plants. Photosystem-I-mediated electron transport increased in plants exposed to Cr and Zn rich wastewater. Efficiency of photosystem II (Fv/Fm) measured by fluorescence did not show any significant change in Cr-exposed plants but a decrease was observed in Zn-exposed plants as compared to the control. The enhancement in PS I-induced cyclic electron transport in Cr and Zn exposed plants led to a build up of the transthylakoidal proton gradient (DpH) which subsequently helped in maintaining the photophosphorylation potential to meet the additional requirement of ATP under stress. The carbon assimilation potential was adversely affected as evident from the decrease in Rubisco (EC 4.1.1.39) activity. The alterations in photosynthetic electron transport affected stromal redox status and induced variations in the level of stromal components such as pyridine nucleotides in plants exposed to Cr and Zn rich wastewater. The present investigations revealed that alteration in the photosynthetic efficiency of Salvinia exposed to Cr could primarily be the result of a decline in carbon assimilation efficiency relative to light-mediated photosynthetic electron transport, though in the case of Zn-exposed plants both these factors were affected equally.

Reinvestigation of the Effects of Disalicylidenepropanediamine (DSPD) and 2-Hepty-4-hydroxyquinoline-N-oxide (HQNO) on Photosynthetic Electron Transport

1981 ◽  
Vol 36 (1-2) ◽  
pp. 109-114 ◽  
Keyword(s):  
Electron Transport ◽  
Electron Flow ◽  
Photosynthetic Electron Transport ◽  
Reduced Form ◽  
Similar Extent ◽  
Ps Ii ◽  
Ps I ◽  
Inhibitory Site ◽  
High Concentrations ◽  
Dark Decay

Abstract The effects of disalicylidenepropanediamine (DSPD) and 2-heptyl-4-hydroxyquinoline-Noxide (HQNO) on photosynthetic electron transport have been reexamined. The results confirm earlier observations that lower concentrations of DSPD (< 100μᴍ) block electron transport at the levels of ferredoxin and plastocyanin. High concentrations of DSPD even inhibit electron transport from H2O → pBQ, suggesting that DSPD has an inhibitory site in PS II as well. Thermoluminescence curves of DSPD and DCMU treated chloroplasts were very similar, showing that the third inhibitory site of DSPD is similar to that of DCMU. Both oxidized and reduced HQNO, (0.6-6 μᴍ) blocked electron transport from H2O → pBQ, H2O → MV/FeCy to a similar extent. The effect of HQNO on thermoluminescence showed that its inhibitory site is probably located before that of DCMU. At higher concentration (> 6 μᴍ), the H2O → MV/FeCy reactions were more strongly inhibited by oxidized HQNO than those occuring from H2O → pBQ, suggesting that a new site of inhibition must also be considered. The dark decay of the P 700 signal was not influenced by the addition of oxidized HQNO which shows that the new inhibitory site of HQNO is located between plastoquinone and P 700. The reduced form of HQNO did not inhibit non-cyclic electron transport around PS I. Indeed, at higher concentrations, reduced HQNO even accelerates electron flow from DCIP → MV and the dark reduction of P 700, thus suggesting that this compound has a “donor-mediator” function in PS I.

Localization and Function of Cytochrome f in the Thylakoid Membrane

1977 ◽  
Vol 32 (3-4) ◽  
pp. 271-280 ◽  
Author(s):  
Georg H. Schmid ◽  
Alfons Radunz ◽  
Wilhelm Menke
Keyword(s):  
Electron Transport ◽  
Outer Surface ◽  
Thylakoid Membrane ◽  
Time Lag ◽  
Photosynthetic Electron Transport ◽  
Cytochrome F ◽  
Antigenic Determinants ◽  
Light Reaction ◽  
Transport Reaction ◽  
Cyclic Photophosphorylation

Abstract A monospecific antiserum to cytochrome f agglutinates stroma-free swellable chloroplasts from tobacco and Antirrhinum. Consequently, antigenic determinants towards which the antiserum is directed are located in the outer surface of the thylakoid membrane. The antiserum inhibits linear photosynthetic electron transport. Just as described earlier for the antiserum to polypeptide 11000 this inhibition develops in the course of the light reaction. Ultrasonication in the presence of anti­ serum abolishes the light requirement and the maximal inhibition of the electron transport reaction is immediately observed. Electron transport in chloroplasts from a tobacco mutant which ex­ hibits only photosystem I-reactions is also inhibited by the antiserum. No time lag in the light for the onset of inhibition is observed with these chloroplasts. As chloroplasts of this mutant have only single unfolded thylakoids it appears that light might preponderantly open up partitions. If the light effect is interpreted in this way, cytochrome f should be located in the partition regions but nevertheless in the outer surface of the thylakoid membrane. However, a rearrangement of molecules in the membrane in the light by which the accessibility of cytochrome f is changed can­ not be excluded. The inhibition of linear electron transport by the antiserum is approximately 50 per cent and can only be increased to 75% upon the addition of antibodies to plastocyanin. The inhibition by the antiserum to cytochrome f as well as the combined inhibition by the antisera to cytochrome f and plastocyanin can be by-passed by DCPiP. It appears that cytochrome f and plastocyanin cannot be connected in series in the electron transport chain but are both closely associated in the thylakoid membrane. PMS-mediated cyclic photophosphorylation in chloroplasts from wild type tobacco and the tobacco mutant NC95 is only inhibited if the chloroplasts are sonicated in the presence of anti­ serum. If one disregards, that ultrasonication might cause reaction artifacts, it is thinkable that the cytochrome f, involved in the PMS-mediated cyclic photophosphorylation reaction, might be located inside the membrane.

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.

Glyphosate Does Not Inhibit Photosynthetic Electron Transport and Phosphorylation in Pea (Pisum sativum) Chloroplasts

Weed Science ◽  
1979 ◽  
Vol 27 (6) ◽  
pp. 684-688 ◽  
Author(s):  
E. P. Richard ◽  
J. R. Goss ◽  
C. J. Arntzen
Keyword(s):  
Electron Transport ◽  
Pisum Sativum ◽  
Photosynthetic Electron Transport ◽  
Photochemical Reactions ◽  
Transport Processes ◽  
Ps Ii ◽  
Dark Incubation ◽  
Fluorescence Studies ◽  
Mixture Prior

The activity of glyphosate [N-(phosphonomethyl)glycine], formulated as the isopropylamine salt, on in vitro photosynthesis was investigated. When pH 4.7 glyphosate solutions were titrated to a pH equal to that of the reaction media (pH 7.8), glyphosate additions had no effect on whole chain electron transport between coupled photosystem II (PS II) and photosystem I (PS I) in stroma-free chloroplast thylakoids from peas (Pisum sativumL. ‘Morse's Progress No. 9′). Inhibition did not occur even after a 2-h dark incubation of lamellae in a 5-mM solution of glyphosate. Fluorescence studies failed to detect an effect of glyphosate on PS-II mediated electron transport processes or upon light harvesting properties of PS II even after a 2-h glyphosate/chloroplast preincubation. Glyphosate had no effect on cyclic and noncyclic photophosphorylation even after a 100-min dark incubation of chloroplast membranes in a 5-mM solution of glyphosate. Based on these assays it is concluded that glyphosate has no direct effect on the photochemical reactions of photosynthesis when the pH of the active compound is adjusted to that of the reaction mixture prior to addition to a chloroplast suspension.

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