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1.
Photosynth Res ; 147(2): 197-209, 2021 Feb.
Article in English | MEDLINE | ID: mdl-33389445

ABSTRACT

Chromatophores of purple non-sulfur bacteria (PNSB) are invaginations of the cytoplasmic membrane that contain a relatively simple system of light-harvesting protein-pigment complexes, a photosynthetic reaction center (RC), a cytochrome complex, and ATP synthase, which transform light energy into the energy of synthesized ATP. The high content of negatively charged phosphatidylglycerol (PG) and cardiolipin (CL) in PNSB chromatophore membranes makes these structures potential targets that bind cationic antiseptics. We used the methods of stationary and kinetic fluorescence spectroscopy to study the effect of some cationic antiseptics (chlorhexidine, picloxydine, miramistin, and octenidine at concentrations up to 100 µM) on the spectral and kinetic characteristics of the components of the photosynthetic apparatus of Rhodobacter sphaeroides chromatophores. Here we present the experimental data on the reduced efficiency of light energy conversion in the chromatophore membranes isolated from the photosynthetic bacterium Rb. sphaeroides in the presence of cationic antiseptics. The addition of antiseptics did not affect the energy transfer between the light-harvesting LH1 complex and reaction center (RC). However, it significantly reduced the efficiency of the interaction between the LH2 and LH1 complexes. The effect was maximal with 100 µM octenidine. It has been proved that molecules of cationic antiseptics, which apparently bind to the heads of negatively charged cardiolipin molecules located in the rings of light-harvesting pigments on the cytoplasmic surface of the chromatophores, can disturb the optimal conditions for efficient energy migration in chromatophore membranes.


Subject(s)
Anti-Infective Agents, Local/pharmacology , Bacterial Chromatophores/drug effects , Energy Transfer/drug effects , Photosynthetic Reaction Center Complex Proteins/drug effects , Rhodobacter sphaeroides/physiology , Cardiolipins/chemistry , Cell Membrane/drug effects , Kinetics , Light , Light-Harvesting Protein Complexes/drug effects , Phosphatidylglycerols/chemistry , Photosynthesis/drug effects , Rhodobacter sphaeroides/chemistry , Spectrometry, Fluorescence
2.
Aquat Toxicol ; 206: 54-60, 2019 Jan.
Article in English | MEDLINE | ID: mdl-30448745

ABSTRACT

The enantioselective toxic mechanisms of chiral herbicides in photosynthetic organisms are closely related to the production of reactive oxygen species (ROS) production, however, there are few reports on how the enantioselective production of ROS can be triggered. In suboptimal conditions, photosynthesis is one of the most important processes in the production of ROS, especially in the process of light utilization and electron transfer. In this study, we investigated the interactions between chiral herbicide dichlorprop (DCPP) enantiomers and the chiral macroaggregates of the photosynthetic light-harvesting chlorophyll a/b pigment-protein complexes (LHCII) in Scenedesmus obliquus, which is of great significance in capturing and utilizing sun light, and also in dissipating the excess excitation energy. The results of the circular dichroism indicated that DCPP induced the structural changes of the LHCII chiral macroaggregates in an enantioselective manner and that the (R)-DCPP treated-group showed a bigger change accompanied by a changed enantioselective dissipation of the excitation energy. The excitation energy was excessed in DCPP treated-groups and the degree of excess was enantioselective and the detrimental non-chemical energy triggered the enantioselective production of ROS, that induced the enantioselective toxicity to green algae S. obliquus. Overall, this study has identified that how the enantioselective production of ROS can be triggered in chloroplasts; this can help to reveal the enantioselective mechanisms of chiral herbicides to photosynthetic organisms.


Subject(s)
2,4-Dichlorophenoxyacetic Acid/analogs & derivatives , Chlorophyta/drug effects , 2,4-Dichlorophenoxyacetic Acid/toxicity , Chloroplasts/drug effects , Herbicides/toxicity , Photosynthesis/drug effects , Photosynthetic Reaction Center Complex Proteins/chemistry , Photosynthetic Reaction Center Complex Proteins/drug effects , Reactive Oxygen Species/metabolism , Stereoisomerism , Water Pollutants, Chemical/toxicity
3.
Photosynth Res ; 136(3): 379-392, 2018 Jun.
Article in English | MEDLINE | ID: mdl-29285578

ABSTRACT

Mercuric contamination of aqueous cultures results in impairment of viability of photosynthetic bacteria primarily by inhibition of the photochemistry of the reaction center (RC) protein. Isolated reaction centers (RCs) from Rhodobacter sphaeroides were exposed to Hg2+ ions up to saturation concentration (~ 103 [Hg2+]/[RC]) and the gradual time- and concentration-dependent loss of the photochemical activity was monitored. The vast majority of Hg2+ ions (about 500 [Hg2+]/[RC]) had low affinity for the RC [binding constant Kb ~ 5 mM-1] and only a few (~ 1 [Hg2+]/[RC]) exhibited strong binding (Kb ~ 50 µM-1). Neither type of binding site had specific and harmful effects on the photochemistry of the RC. The primary charge separation was preserved even at saturation mercury(II) concentration, but essential further steps of stabilization and utilization were blocked already in the 5 < [Hg2+]/[RC] < 50 range whose locations were revealed. (1) The proton gate at the cytoplasmic site had the highest affinity for Hg2+ binding (Kb ~ 0.2 µM-1) and blocked the proton uptake. (2) Reduced affinity (Kb ~ 0.05 µM-1) was measured for the mercury(II)-binding site close to the secondary quinone that resulted in inhibition of the interquinone electron transfer. (3) A similar affinity was observed close to the bacteriochlorophyll dimer causing slight energetic changes as evidenced by a ~ 30 nm blue shift of the red absorption band, a 47 meV increase in the redox midpoint potential, and a ~ 20 meV drop in free energy gap of the primary charge pair. The primary quinone was not perturbed upon mercury(II) treatment. Although the Hg2+ ions attack the RC in large number, the exertion of the harmful effect on photochemistry is not through mass action but rather a couple of well-defined targets. Bound to these sites, the Hg2+ ions can destroy H-bond structures, inhibit protein dynamics, block conformational gating mechanisms, and modify electrostatic profiles essential for electron and proton transfer.


Subject(s)
Electron Transport/radiation effects , Mercury/pharmacology , Photosynthetic Reaction Center Complex Proteins/drug effects , Photosynthetic Reaction Center Complex Proteins/radiation effects , Protons , Rhodobacter sphaeroides/drug effects , Bacteriochlorophylls/metabolism , Benzoquinones/metabolism , Binding Sites , Photochemistry , Photosynthesis/drug effects , Rhodobacter sphaeroides/physiology , Rhodobacter sphaeroides/radiation effects , Water/metabolism
4.
Dokl Biochem Biophys ; 477(1): 368-371, 2017 Nov.
Article in English | MEDLINE | ID: mdl-29297127

ABSTRACT

The effect of heating at 65°C for 20 min on the absorption spectra and kinetics of the dark recombination of charges separated between photoactive bacteriochlorophyll and quinone acceptors was studied in dry films of bacterial photosynthetic reaction centers (RCs), RC films in polyvinyl alcohol, and trehalose. A pronounced protective effect of trehalose against pheophytinizaiton of molecules bacteriochlorophylls in RC structure and in maintaining their higher photochemical activity was found.


Subject(s)
Hot Temperature , Photosynthetic Reaction Center Complex Proteins/drug effects , Photosynthetic Reaction Center Complex Proteins/metabolism , Trehalose/pharmacology , Kinetics , Rhodobacter sphaeroides/cytology , Rhodobacter sphaeroides/enzymology
5.
Photochem Photobiol ; 92(3): 436-45, 2016 05.
Article in English | MEDLINE | ID: mdl-26888623

ABSTRACT

The high light-induced bleaching of photosynthetic pigments and the degradation of proteins of light-harvesting complexes of PSI and PSII were investigated in isolated thylakoid membranes of Arabidopsis thaliana, wt and lutein-deficient mutant lut2, with the aim of unraveling the role of lutein for the degree of bleaching and degradation. By the means of absorption spectroscopy and western blot analysis, we show that the lack of lutein leads to a higher extent of pigment photobleaching and protein degradation in mutant thylakoid membranes in comparison with wt. The highest extent of bleaching is suffered by chlorophyll a and carotenoids, while chlorophyll b is bleached in lut2 thylakoids during long periods at high illumination. The high light-induced degradation of Lhca1, Lhcb2 proteins and PsbS was followed and it is shown that Lhca1 is more damaged than Lhcb2. The degradation of analyzed proteins is more pronounced in lut2 mutant thylakoid membranes. The lack of lutein influences the high light-induced alterations in organization of pigment-protein complexes as revealed by 77 K fluorescence.


Subject(s)
Arabidopsis/physiology , Light , Lutein/pharmacology , Photosynthetic Reaction Center Complex Proteins/radiation effects , Thylakoids/physiology , Arabidopsis/radiation effects , Dose-Response Relationship, Radiation , Photosynthetic Reaction Center Complex Proteins/drug effects , Proteolysis , Spectrum Analysis
6.
Biochemistry (Mosc) ; 80(4): 417-23, 2015 Apr.
Article in English | MEDLINE | ID: mdl-25869358

ABSTRACT

Plastoquinone bound with decyltriphenylphosphonium cation (SkQ1) penetrating through the membrane in nanomolar concentrations inhibited H2O2 generation in cells of epidermis of pea seedling leaves that was detected by the fluorescence of 2',7'-dichlorofluorescein. Photosynthetic electron transfer in chloroplasts isolated from pea leaves is suppressed by SkQ1 at micromolar concentrations: the electron transfer in chloroplasts under the action of photosystem II or I (with silicomolybdate or methyl viologen as electron acceptors, respectively) is more sensitive to SkQ1 than under the action of photosystem II + I (with ferricyanide or p-benzoquinone as electron acceptors). SkQ1 reduced by borohydride is oxidized by ferricyanide, p-benzoquinone, and, to a lesser extent, by silicomolybdate, but not by methyl viologen. SkQ1 is not effective as an electron acceptor supporting O2 evolution from water in illuminated chloroplasts. The data on suppression of photosynthetic O2 evolution or consumption show that SkQ1, similarly to phenazine methosulfate, causes conversion of the chloroplast redox-chain from non-cyclic electron transfer mode to the cyclic mode without O2 evolution. Oxidation of NADH or succinate in mitochondria isolated from pea roots is stimulated by SkQ1.


Subject(s)
Chloroplasts/drug effects , Mitochondria/drug effects , Pisum sativum/drug effects , Plastoquinone/analogs & derivatives , Seedlings/drug effects , Cell Respiration/drug effects , Chloroplasts/metabolism , Electron Transport/drug effects , Mitochondria/metabolism , Pisum sativum/metabolism , Photosynthetic Reaction Center Complex Proteins/drug effects , Plastoquinone/pharmacology , Seedlings/metabolism
7.
Plant Physiol Biochem ; 84: 10-21, 2014 Nov.
Article in English | MEDLINE | ID: mdl-25240106

ABSTRACT

Tenuazonic acid (TeA), a phytotoxin produced by the fungus Alternaria alternata isolated from diseased croftonweed (Ageratina adenophora), exhibits a strong inhibition in photosystem II (PSII) activity. In vivo chlorophyll fluorescence transients of the host plant croftonweed, show that the dominant effect of TeA is not on the primary photochemical reaction but on the biochemical reaction after QA. The most important action site of TeA is the QB site on the PSII electron-acceptor side, blocking electron transport beyond QA(-) by occupying the QB site in the D1 protein. However, TeA does not affect the antenna pigments, the energy transfer from antenna pigment molecules to reaction centers (RCs), and the oxygen-evolving complex (OEC) at the donor side of PSII. TeA severely inactivated PSII RCs. The fraction of non-QA reducing centers and non-QB reducing centers show a time- and concentration-dependent linear increase. Conversely, the amount of active QA or QB reducing centers declined sharply in a linear way. The fraction of non-QB reducing centers calculated from data of fluorescence transients is close to the number of PSII RCs with their QB site filled by TeA. An increase of the step-J level (VJ) in the OJIP fluorescence transients attributed to QA(-) accumulation due to TeA bound to the QB site is a typical characteristic response of the plants leaf with respect to TeA penetration.


Subject(s)
Photosystem II Protein Complex/metabolism , Tenuazonic Acid/pharmacology , Chlorophyll/metabolism , Electron Transport/drug effects , Photosynthetic Reaction Center Complex Proteins/drug effects , Photosynthetic Reaction Center Complex Proteins/metabolism , Photosystem II Protein Complex/drug effects
8.
Tree Physiol ; 30(11): 1415-32, 2010 Nov.
Article in English | MEDLINE | ID: mdl-21030406

ABSTRACT

Populus tremula L. × Populus alba L. (Populus ×c anescens (Aiton) Smith) - clone INRA 717-1-B4 saplings (50 cm apex to base and carrying 19 leaves on average) - were followed for 28 days. Half of the trees were grown in charcoal-filtered air while the other half were exposed to 120 ppb ozone for 11 h a day during the light period. The expanding leaf number 4 was tagged at the beginning of the experiment and finished expansion between 7 and 14 days. These leaves were harvested weekly for biochemical and proteome analyses using quantitative bidimensional electrophoresis (DiGE). Independent of the ozone treatment, all the analyses allowed a distinction between expanding and adult leaves. The results indicate that during the expansion phase (Days 0-7) the enzymatic machinery of the leaves is set up, and remains dynamically stable in the adult leaves (Days 14-28). Although ozone had no apparent effect on expanding leaves, the metabolic stability in fully expanded leaves observed in ozone-free plants was disturbed after 2 weeks of exposure and a stress-induced response became apparent.


Subject(s)
Air Pollutants/toxicity , Ecosystem , Ozone/adverse effects , Plant Leaves/drug effects , Populus/drug effects , Seedlings/drug effects , Chlorophyll/metabolism , Electrophoresis , Photosynthesis/drug effects , Photosynthetic Reaction Center Complex Proteins/drug effects , Photosynthetic Reaction Center Complex Proteins/metabolism , Plant Leaves/enzymology , Plant Leaves/growth & development , Plant Proteins/metabolism , Populus/enzymology , Populus/growth & development , Proteomics/methods , Seedlings/enzymology , Seedlings/growth & development , Stress, Physiological/drug effects , Time Factors
9.
Biochim Biophys Acta ; 1804(1): 137-46, 2010 Jan.
Article in English | MEDLINE | ID: mdl-19786126

ABSTRACT

We report on the response of reaction center (RC) from Rhodobacter sphaeroides (an archetype of membrane proteins) to the exposure at high temperature. The RCs have been solubilized in aqueous solution of the detergent N,N-dimethyldodecylamine-N-oxide (LDAO). Changes in the protein conformation have been probed by monitoring the variation in the absorbance of the bacteriochlorine cofactors and modification in the efficiency of energy transfer from tryptophans to cofactors and among the cofactors (through fluorescence measurements). The RC aggregation taking place at high temperature has been investigated by means of dynamic light scattering. Two experimental protocols have been used: (i) isothermal kinetics, in which the time evolution of RC after a sudden increase of the temperature is probed, and (ii) T-scans, in which the RCs are heated at constant rate. The analysis of the results coming from both the experiments indicates that the minimal kinetic scheme requires an equilibrium step and an irreversible process. The irreversible step is characterized by a activation energy of 205+/-14 kJ/mol and is independent from the detergent concentration. Since the temperature dependence of the aggregation rate was found to obey to the same law, the aggregation process is unfolding-limited. On the other hand, the equilibrium process between the native and a partially unfolded conformations was found to be strongly dependent on the detergent concentration. Increasing the LDAO content from 0.025 to 0.5 wt.% decreases the melting temperature from 49 to 42 degrees C. This corresponds to a sizeable (22 kJ/mol at 25 degrees C) destabilization of the native conformation induced by the detergent. The nature of the aggregates formed by the denatured RCs depends on the temperature. For temperature below 60 degrees C compact aggregates are formed while at 60 degrees C the clusters are less dense with a scaling relation between mass and size close to that expected for diffusion-limited aggregation. The aggregate final sizes formed at different temperatures indicate the presence of an even number of proteins suggesting that these clusters are formed by aggregation of dimers.


Subject(s)
Detergents/pharmacology , Dimethylamines/pharmacology , Membrane Proteins/drug effects , Photosynthetic Reaction Center Complex Proteins/drug effects , Hot Temperature , Kinetics , Protein Denaturation/drug effects , Protein Stability/drug effects , Rhodobacter sphaeroides/metabolism
10.
Ecotoxicology ; 18(7): 929-38, 2009 Oct.
Article in English | MEDLINE | ID: mdl-19562482

ABSTRACT

The effects of long-term (33 months) sun/shade acclimation and short-term (within 10 h) HSO(3) (-) treatment on leaf photosynthetic apparatus were investigated in three subtropical forest plants, Pinus massoniana, Schima superba, and Acmena acuminatissima. After 33 months' growth in two light environments (100 and 12% sunlight), rapid light curves (RLC), chlorophyll fluorescence imaging and chloroplast ultrastructures of three tested species were changed to different degrees. When leaf sections were immersed in 50 mM NaHSO(3) for 10 h, all the RLCs were lowered; chlorophyll fluorescence imaging was inclined to present warmer colors and imaging areas were decreased. However, changes in chloroplast ultrastructures differed from three species. Our results showed that the photosynthetic apparatus of a dominant species, A. acuminatissima, in the late succession stage of a subtropical forest in South China, was less sensitive to NaHSO(3) under both growing light intensities. Conversely, the chloroplasts of P. massoniana, the pioneer heliophyte species, were most susceptible to NaHSO(3). It is deduced that, SO(2) pollution may become as a factor to accelerate the succession of subtropical forest.


Subject(s)
Adaptation, Physiological/physiology , Photosynthetic Reaction Center Complex Proteins/drug effects , Sulfites/toxicity , Chlorophyll/metabolism , Chloroplasts/drug effects , Chloroplasts/metabolism , Chloroplasts/ultrastructure , Plant Leaves/drug effects , Species Specificity , Sunlight
11.
J Hazard Mater ; 166(2-3): 1332-8, 2009 Jul 30.
Article in English | MEDLINE | ID: mdl-19157705

ABSTRACT

This article discusses the applicability of the Charophyte, Nitella pseudoflabellata in the remediation of Cr (VI) contaminated waters at different calcifying potentials. Its growth was found to be positively correlated with Ca in water (CaW), but marginally significant in the presence of Cr (VI) in water (CrW). High CaW resulted in calcite encrustation on the plant cell wall. CaW was found to be aiding Cr (VI) fixation in the long run, as this correlated positively with both CaW and CrW. However, Ca interfered with passive Cr (VI) accumulation in live plant matter at low CrW concentrations (1mg/g Cr dry weight of plant. Cr (VI) concentrations greater than 0.4 mg/L were too toxic, showing maximum quantum efficiency of PSII photochemistry (F(v)/F(m)) values<0.63. The opposite was noticed (F(v)/F(m)>0.76) when Cr (VI) was less than 0.2mg/L. Elongation curve patterns based on shoot lengths showed similar scenarios. In all cases high CaW units with calcite encrustation found to be least affected by Cr (VI) toxicity. Optimum remediation was obtained using a combination of high Ca and Cr (VI) in the case of passive (short-term) operation and low Ca and Cr (VI) for active (long-term) operation. Under the passive scenario, plants accumulated above 1.2mg/g Cr dry weight whereas in the active case, accumulation was 0.8 mg/g Cr dry weight. We conclude that Nitella-mediated Cr (VI) remediation is a promising technique within the range and conditions investigated.


Subject(s)
Biodegradation, Environmental , Calcium/chemistry , Chromium/metabolism , Nitella/metabolism , Calcium Carbonate , Chromium/toxicity , Minerals , Nitella/physiology , Photosynthetic Reaction Center Complex Proteins/drug effects , Photosystem II Protein Complex/drug effects , Water Pollutants, Chemical/metabolism
12.
Photochem Photobiol Sci ; 7(8): 973-8, 2008 Aug.
Article in English | MEDLINE | ID: mdl-18688505

ABSTRACT

Photophysical properties of tetramethyl-1,4-benzoquinone (TMBQ) and 2,6-dimethoxy-1,4-benzoquinone (DMOBQ) in solution and their interactions with the photosynthetic reaction centre (RC) isolated from the photosynthetic bacterium Rhodobacter sphaeroides have been investigated in this work. For these two benzoquinone derivatives an efficient ISC process which leads to the population of the lowest triplet state of the molecules upon direct excitation was observed. The presence of RC does not alter the properties of the triplet state of DMOBQ suggesting that interactions are negligible; on the other side RC efficiently quenched the T1 state of TMBQ. The behavior is rationalized in terms of redox potentials of quinones and kinetic characteristics of their transients.


Subject(s)
Light , Photosynthetic Reaction Center Complex Proteins/drug effects , Quinones/pharmacology , Crystallography, X-Ray , Photosynthetic Reaction Center Complex Proteins/chemistry , Photosynthetic Reaction Center Complex Proteins/radiation effects , Protein Conformation , Quinones/chemistry , Rhodobacter sphaeroides/drug effects , Rhodobacter sphaeroides/radiation effects
13.
Biofizika ; 52(2): 277-86, 2007.
Article in Russian | MEDLINE | ID: mdl-17477055

ABSTRACT

The damaging effect of oxidative stress inductors: methyl viologen, benzyl viologen, cumene hydroperoxide, H2O2, menadion, and high irradiance on the photosynthetic apparatus of cyanobacterium Synechocystis sp. PCC 6803 in cells of the wild type strain and the methyl viologen-resistant Prq20 mutant with the disrupted function of the regulatory gene prqR has been investigated by measuring the delayed fluorescence of chlorophyll a and the rate of CO2dependent -O2 gas exchange. It has been shown that the damage to the photosynthetic apparatus in the Prq20 mutant as compared with the wild type was less in the presence of methyl viologen and benzyl viologen. Reasons for the enhanced resistance of the photosynthetic apparatus in the mutant Prq20 to methyl viologen and benzyl viologen are discussed.


Subject(s)
Drug Resistance/genetics , Oxidants/pharmacology , Oxidative Stress , Photosynthetic Reaction Center Complex Proteins/drug effects , Synechocystis/drug effects , Bacterial Proteins/genetics , Benzyl Viologen/metabolism , Benzyl Viologen/pharmacology , Herbicides/pharmacology , Mutation , Oxidants/metabolism , Paraquat/pharmacology , Repressor Proteins/genetics , Synechocystis/genetics
14.
Anal Bioanal Chem ; 387(5): 1863-73, 2007 Mar.
Article in English | MEDLINE | ID: mdl-17203250

ABSTRACT

Photosynthetic reaction centres and membranes are systems of particular interest and are often taken as models to investigate the molecular mechanisms of selected bioenergetic reactions. In this work, a multivariate curve resolution by alternating least squares procedure is detailed for resolution of time-resolved difference FTIR spectra probing the evolution of quinone reduction in photosynthetic membranes from Rhodobacter sphaeroides under photoexcitation. For this purpose, different data sets were acquired in the same time range and spectroscopic domain under slightly different experimental conditions. To enable resolution and provide meaningful results the different data sets were arranged in an augmented matrix. This strategy enabled recovery of three different species despite rank-deficiency conditions. It also results in better definition (identity and evolution) of the contributions. From the resolved spectra, the species have been attributed to: 1. the formation of ubiquinol, more precisely the disappearance of Q/appearance of QH(2); 2. conformational change of the protein in the surrounding biological medium; 3. oxidation of diaminodurene, a redox mediator. Because, moreover, results obtained from augmented data sets strategies enable quantitative and qualitative interpretation of concentration profiles, other effects, for example the consequence of repeated light excitation of the same sample, choice of illumination power, or the number of spectra accumulated could be compared and discussed.


Subject(s)
Algorithms , Benzoquinones/metabolism , Pattern Recognition, Automated/methods , Photosynthetic Reaction Center Complex Proteins/physiology , Purple Membrane/physiology , Rhodobacter sphaeroides/physiology , Spectroscopy, Fourier Transform Infrared/methods , Light , Multivariate Analysis , Oxidation-Reduction/radiation effects , Photosynthetic Reaction Center Complex Proteins/drug effects , Purple Membrane/radiation effects , Rhodobacter sphaeroides/radiation effects
15.
Chemosphere ; 65(10): 1738-46, 2006 Dec.
Article in English | MEDLINE | ID: mdl-16777178

ABSTRACT

Effects of cadmium (Cd) on the growth and photosynthesis of the bloom-forming cyanobacterium Microcystis aeruginosa Kütz 854 were investigated. The growth was markedly inhibited when it was treated with 4 microM Cd. However, the biomass production was almost not influenced after a prolonged exposure at Cd concentrations < or = 2 microM. Chlorophyll content was more sensitive to Cd toxicity than phycobiliproteins at 0.5 microM Cd. However, the decrease of phycobiliproteins was larger than chlorophyll at the highest Cd concentration. A significant increase of F(v)/F(m) value was observed at Cd concentrations < or = 2 microM. On the other hand, when cells were treated with 4 microM Cd, F(v)/F(m) was significantly increased after 12 h of treatment but decreased after 48 h. The true photosynthesis was decreased with the increase of Cd concentration at 2 h. However, we noticed a recovery when the treatment was prolonged. After 48 h of exposure at the highest Cd concentration, photosynthetic oxygen evolution was markedly inhibited but dark respiration increased by 67%. Cellular Cd contents were augmented with the increase of Cd concentration. To our knowledge, we have demonstrated for the first time that the inhibitory site of Cd in M. aeruginosa is not located at the PSII or PSI level, but is probably situated on the ferredoxin/NADP(+)-oxidoreductase enzyme at the terminal of whole electron transport chain. We noticed also an increase of PSI activity, which is probably linked to the enhancement of cyclic electron transport around PSI. We can conclude that the increase of cyclic electron transport and dark respiration activities, and the decrease of phycobiliproteins might be adaptive mechanisms of M. aeruginosa 854 under high Cd conditions.


Subject(s)
Cadmium/toxicity , Microcystis/drug effects , Microcystis/physiology , Photosynthesis/drug effects , Water Pollutants, Chemical/toxicity , Biomass , Cadmium/metabolism , Chlorophyll/metabolism , Electron Transport , Ferredoxins/metabolism , Fluorescence , Microcystis/growth & development , Oxygen/metabolism , Photosynthetic Reaction Center Complex Proteins/drug effects , Pigments, Biological/metabolism , Water Pollutants, Chemical/metabolism
16.
Article in Chinese | MEDLINE | ID: mdl-16477136

ABSTRACT

Choline chloride 1.07 mmol/L treatment diminished the saturated lipid contents of the fatty acid components mainly the phosphatidylglycerol (PG) resulting in the decrease of the saturation of lipid (Table 1), declined the permeability of cell membrane and the production of MDA from lipid peroxidation (Fig.2) in the cucumber seedling leaves under low temperature and weak light (6 degrees C, PFD 100 micromol m(-2) s(-1)). Furthermore, the choline chloride treatment alleviated the degradation of chlorophyll pigments especially chlorophyll b, the decrease in maximum photochemical efficiency (Fv/Fm), the capture efficiency of excited energy (Fv'/Fm'), the photochemical quenching coefficient (q(p)) and the actual photochemical efficiency (Phi PSII) of PSII (Table 2, Fig.3A, B & C), and decreases in activity of antioxidant enzymes such as POD, APX and CAT (Fig.4) in chilled leaves under weak light. In addition, choline chloride treatment increased the non-photochemical quenching (NPQ) (Fig.3D) and the proline content (Fig.5) in chilled leaves under weak light. The above results indicate that choline chloride protected the cell membrane and the photosynthetic apparatus in cucumber seedling leaves from chilling stress in weak light.


Subject(s)
Cell Membrane/drug effects , Chlorides/toxicity , Cucumis sativus/drug effects , Photosynthetic Reaction Center Complex Proteins/drug effects , Seedlings/drug effects , Calcium/metabolism , Chlorophyll/physiology , Cold Temperature , Cucumis sativus/growth & development , Light , Photosynthetic Reaction Center Complex Proteins/metabolism , Plant Leaves/drug effects , Plant Leaves/metabolism , Potassium/metabolism , Seedlings/chemistry , Seedlings/metabolism , Sodium/metabolism
17.
Planta ; 223(5): 1047-57, 2006 Apr.
Article in English | MEDLINE | ID: mdl-16292567

ABSTRACT

The cause of the strong non-photochemical fluorescence quenching was examined in maize (Zea mays L.) plants that were treated with lincomycin during the 72 h period of greening. They were deficient in core complexes but seemed to contain the full complement of antennae. The following results were obtained: (1) High F(o) could not be attributed to the dark reduction of Q(A) but to the presence of a high amount of not properly organized antenna complexes due to the inhibited synthesis of reaction centres. (2) On illumination fluorescence intensity dropped considerably below F(o) within 20 s, and reached a steady state still below F(o). (3) Slowly relaxing part of non-photochemical quenching was significantly higher than in control plants. (4) De-epoxidation state was constant, and corresponded to the maximal value of the control. (5) Free Lhca1/4 dimers could be detected in all submembrane fractions, including the grana, obtained by digitonin fractionation. (6) Increase in the 679 and 700 nm fluorescence emissions could be attributed to the monomerisation of part of LHCII and to the presence of free Lhca2 or LHCII aggregates, respectively. (7) LHCII or PSII+LHCII and Lhca1/4 interaction may contribute to the increase of long-wavelength fluorescence in the granal fraction. We assume that the elevated fluorescence quenching of monomeric LHCII as well as the interaction between LHCII or PSII+LHCII and Lhca1/4 can be considered as an explanation for the extensive non-photochemical fluorescence quenching in lincomycin treated plants. The permanent presence of zeaxanthin may have contributed to the fast formation of quenching.


Subject(s)
Anti-Bacterial Agents/pharmacology , Fluorescence , Lincomycin/pharmacology , Photosynthetic Reaction Center Complex Proteins/drug effects , Zea mays/drug effects , Carotenoids/metabolism , Chlorophyll/metabolism , Chloroplasts/drug effects , Light
18.
Plant Cell Physiol ; 46(5): 729-35, 2005 May.
Article in English | MEDLINE | ID: mdl-15753102

ABSTRACT

Chlorella, when heterotrophically cultivated in the dark, is able to grow with Zn2+ at 10-40 mM, which is 10 times the concentration lethal to autotrophically grown cells. However, the lag phase is prolonged with increasing concentrations of Zn2+; for example, in this study, 1 d of the control lag phase was prolonged to about 16 d with Zn2+ at 16.7 mM (x2,000 of the control). Once the cells started to grow, the log phase was finished within 4-6 d regardless of Zn concentration, which was almost the same as that of the control. The photosysystem I reaction center chlorophyll, P700, and the far-red fluorescence were detected only after the late log phase of the growth curve, suggesting that chlorophyll-protein complexes can be organized after cell division has ceased. Interestingly, at more than 16.7 mM of Zn2+, Zn-chlorophyll a was accumulated and finally accounted for about 25% of the total chlorophyll a in the late stationary phase. We found that the Zn-chlorophyll a was present in the thylakoid membranes and not in the soluble fractions of the cells. The rather low fluorescence yield at around 680 nm in the stationary phase suggests that Zn-chlorophyll a can transfer its excitation energy to other chlorophylls. Before accumulation of Zn-chlorophyll a, a marked amount of pheophytin a was temporally accumulated, suggesting that Zn-chlorophyll a could be chemically synthesized via pheophytin a.


Subject(s)
Chlorella/drug effects , Chlorella/metabolism , Chlorophyll/biosynthesis , Photosynthetic Reaction Center Complex Proteins/drug effects , Zinc/pharmacology , Cell Division/drug effects , Cell Division/physiology , Chlorella/growth & development , Chlorophyll/chemistry , Chlorophyll A , Darkness , Dose-Response Relationship, Drug , Pheophytins/metabolism , Photosynthetic Reaction Center Complex Proteins/metabolism , Photosystem I Protein Complex/drug effects , Photosystem I Protein Complex/metabolism , Thylakoids/drug effects , Thylakoids/metabolism , Zinc/metabolism
19.
Protoplasma ; 224(3-4): 167-77, 2004 Dec.
Article in English | MEDLINE | ID: mdl-15614477

ABSTRACT

Asynchronous cultures of wild-type Euglena gracilis were tested for their morphophysiological response to 10 mM MnSO4. Growth was only moderately slowed (15%), while oxygen evolution was never compromised. Inductively coupled plasma analyses indicated that the Mn cell content doubled with respect to controls, but no signs of localised accumulation were detected with X-ray microanalysis. Evident morphological alterations were found at the plastid level with transmission electron microscopy and confocal laser scanning microscopy. An increase in the plastid mass, accompanied by frequent aberrations of chloroplast shape and of the organisation of the thylakoid system, was observed. These aspects paralleled a decrease in the molar ratio of chlorophyll a to b and an increase in the fluorescence emission ratio of light-harvesting complex II to photosystem II, the latter evaluated by in vivo single-cell microspectrofluorimetry. These changes were observed between 24 and 72 h of treatment. However, the alterations in the pigment pattern and photosystem II fluorescence were no longer observed after 96 h of Mn exposure, notwithstanding the maintenance of the large plastid mass. The response of the photosynthetic apparatus probably allows the alga to limit the photooxidative damage linked to the inappropriately large peripheral antennae of photosystem II. On the whole, the resistance of Euglena gracilis to Mn may be due to an exclusion-tolerance mechanism since most Mn is excluded from the cell, and the small amount entering the organism is tolerated by means of morphophysiological adaptation strategies, mainly acting at the plastid level.


Subject(s)
Adaptation, Physiological/physiology , Chloroplasts/metabolism , Euglena gracilis/metabolism , Manganese/metabolism , Photosynthetic Reaction Center Complex Proteins/metabolism , Plastids/metabolism , Adaptation, Physiological/drug effects , Animals , Chlorophyll/metabolism , Chlorophyll A , Chloroplasts/drug effects , Chloroplasts/ultrastructure , Drug Resistance/physiology , Euglena gracilis/drug effects , Euglena gracilis/ultrastructure , Light-Harvesting Protein Complexes/drug effects , Light-Harvesting Protein Complexes/metabolism , Manganese/pharmacology , Manganese Compounds/pharmacology , Microscopy, Confocal , Microscopy, Electron, Transmission , Oxidative Stress/drug effects , Oxidative Stress/physiology , Photosynthesis/drug effects , Photosynthesis/physiology , Photosynthetic Reaction Center Complex Proteins/drug effects , Photosynthetic Reaction Center Complex Proteins/ultrastructure , Photosystem II Protein Complex/drug effects , Photosystem II Protein Complex/metabolism , Plastids/drug effects , Plastids/ultrastructure , Sulfates/pharmacology , Thylakoids/drug effects , Thylakoids/metabolism , Thylakoids/ultrastructure
20.
Prikl Biokhim Mikrobiol ; 40(6): 659-67, 2004.
Article in Russian | MEDLINE | ID: mdl-15609857

ABSTRACT

Carboxylase activities of the key enzyme of carbon metabolism, ribulose-bisphosphate carboxylase/oxygenase (RuBisCO; EC 4.1.1.39), and phosphoenolpyruvate carboxylase (PEPC; EC 4.1.1.31), as well as intensities of carbon dioxide photosynthetic assimilation in young seedlings and adult leaves of the wheat Triticum aestivum L. cultivars Mironovskaya 808 (a more tolerant) and Lyutestsens 758 (a less tolerant), were compared under conditions of progressive water deficiency. The water stress had more pronounced negative effects on all the studied characteristics of photosynthetic apparatus of cultivar Lyutestsens 758 photosynthetic machinery of the cultivar Lyutestsens 758. Its seedlings were more sensitive to water stress. Compounds with a cytokinin activity (6-benzylaminopurine, thidiazuron, cartolin 2, and cartolin 4) played a protective role, increasing the stability of the photosynthetic machinery under conditions of water deficiency. Preparations of cartolins displayed the maximum protective effect.


Subject(s)
Cytokinins/pharmacology , Photosynthetic Reaction Center Complex Proteins/drug effects , Triticum/drug effects , Water , Species Specificity , Triticum/physiology
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