PubMed Health⌕ Search

SEARCH · PubMed Health

Results for “Photosystem I Protein Complex”

Explore indexed PubMed citations for clinical trials, systematic reviews and public health research. Read source abstracts and follow each citation to its original PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 73 records · Page 4Linked to original sources

AS-1 cyanophage infection inhibits the photosynthetic electron flow of photosystem II in Synechococcus sp. PCC 6301, a cyanobacterium.

In Synechococcus sp. cells AS-1 cyanophage infection gradually inhibits the photosystem II mediated photosynthetic electron flow whereas the activity of photosystem I is apparently unaffected by the cyanophage infection. Transient fluorescence induction and flash-induced delayed luminescence decay studies revealed that the inhibition may occur at the level of the secondary acceptor, QB of photosystem II. In addition, the breakdown of D1-protein is inhibited, comparable to DCMU-induced protection of D1-protein turnover, in AS-1-infected cells.

Chlorophyll↗

The effect of microgravity on proton permeability of thylakoid membranes and contribution of II and I photosystems in photosynthetic electron transport in pea chloroplasts.

According to a number investigations microgravity conditions affect membrane apparatus of photosynthesis in cells of higher plants and alga [for review, see Kordyum et al., 1994; Kordyum, 1997]. (see for review). Chloroplasts of space-grown pea plants showed disintegration of grana, shrinkage of the membrane constituting the grana stacks and other structural perturbance of the photosynthetic membranes. However there have been no studies on the effect of microgravity on proton permeability of thylakoid membranes and closely connected with this parameter their photochemical characteristics. The aim of the study is investigation of microgravity effects on protonic permeability of photosynthetic membrane and contribution of photosystem II (PSII) and photosystem I (PSI) in electron transfer from water to potassium ferrycianide (FeCy) in isolated pea chloroplasts. Pea.

Chloroplasts↗

Electrons generated by photosystem II are utilized by an oxidase in the absence of photosystem I in the cyanobacterium Synechocystis sp. PCC 6803.

The reduction and reoxidation kinetics of the first quinone-type electron acceptor in photosystem II, QA-, were measured by fluorescence in a light-tolerant, photosystem I-less strain of the cyanobacterium Synechocystis sp. PCC 6803. In this strain, which shows excellent amplitudes of variable fluorescence, the rate of QA- oxidation after photoreduction of the plastoquinone pool was about half of that in the presence of photosystem I. However, upon addition of 5 mM KCN, QA- decay was very slow, and the rate was comparable to that seen in the presence of diuron, which blocks electron transport between QA and QB. The KCN-imposed block of QA- oxidation was removed efficiently by addition of exogenous quinones that can oxidize the plastoquinone pool. These results indicate that, in the absence of photosystem I, photosystem II-generated electrons are used very effectively by an oxidase located in the thylakoid; this oxidase may be a component of the respiratory chain.

Cyanobacteria↗

Structure model of core proteins in photosystem I inferred from the comparison with those in photosystem II and bacteria; an application of principal component analysis to detect the similar regions between distantly related families of proteins.

A principal component analysis based on the physico-chemical properties of amino acid residues is developed to assign similar regions between distantly related families of proteins, taking account of the species diversities in respective families. The most important advantage of this analysis should be that it reflects different physico-chemical properties and thus can predict more detailed structural properties, including the transmembrane helices, than the hydropathy analysis. Its first application reconfirms the similarity between the core proteins of photosynthetic reaction center in purple bacteria and those of photosystem II, indicating that the low percentage of identical amino acid residues estimated previously between them is due to much allowance for amino acid substitutions in purple bacteria. The application of this analysis to the core proteins of photosystem I reveals that any of these proteins includes two domains, each showing high similarity to the amino acid sequences of core proteins in photosystem II and purple bacteria. A core structure model of A1 and A2 proteins folded into four layers of sheets of transmembrane helices is proposed to provide a molecular basis for the electron pathway suggested by spectroscopic experiments as well as for the interaction sites with plastocyanin, 9 kDa protein and LHC proteins.

Amino Acid Sequence↗

Outward photocurrent component in chloroplasts of Peperomia metallica and its assignment to the 'closed thylakoid' recording configuration.

The photoinduced electrical events at energy-conserving chloroplast membranes can be studied in whole plastids using suction electrodes. In chloroplasts of Peperomia metallica the kinetic profile of photocurrent contains a minor outward component that occurs prior to and differs in polarity from the main component. The origin of this outward current was analyzed using single-turnover flashes in combination with prolonged light exposures and differential physicochemical treatments of tip-located (internal) and the exposed parts of a chloroplast. The outward current signal was higher after 10- to 20-s preillumination and gradually reduced in darkness. The relative amplitude of the outward peak current was enhanced when photosystem II (PS II) was excited by flashes given in the presence of far-red background light (lambda = 712 nm). The outward current was small or absent under conditions promoting activity of photosystem I (cyclic electron transport supported by artificial redox mediators in the presence of diuron) and was particularly high in the presence of PS II electron acceptors (e.g., p-phenylenediamine). This indicates the predominant association of the outward current with activity of PS II. The external application of diuron strongly inhibited the inward current, giving rise to a temporal increase in the outward current. On the contrary, when diuron was added into the suction pipette, the outward current was inhibited soon after sealing. The data suggest that the outward current originated in the tip-located portions of the thylakoid membrane that have orientation opposite to the exposed part of 'whole thylakoid'. These tip-located membrane portions are least accessible for inhibitors added into the outer medium and are highly sensitive to inhibitors (diuron), ionophores (gramicidin D), and detergents (Triton X-100) added into the pipette. Differential involvement of two photosystems in generation of the outward current may be caused by uneven structural distribution of photosystems I and II between appressed (granal) and nonappressed (stromal) thylakoids and by different recording configurations for these thylakoids.

Chloroplasts↗

A photosystem II-phycobilisome preparation from the red alga, Porphyridium cruentum: oxygen evolution, ultrastructure, and polypeptide resolution.

The photosystem II-phycobilisome preparation, isolated by lauryldimethyl amine oxide treatment, had a greatly reduced chlorophyll content, with an average ratio of 90 chlorophyll a/phycobilisome as compared to approximately 1200 Chl/phycobilisome in unfractionated thylakoids. P700 was not detected in the particles. By electron microscopy the preparations were relatively homogeneous and were generally devoid of chloroplast membranes. In negatively stained preparations phycobilisome particles were seen often in clusters of two and three, probably due to retention of hydrophobic thylakoid fragments. The preparation was deficient in photosystem I chlorophyll complexes, but enriched in polypeptides of 85 to 92, approximately 43, and approximately 26 kDa, as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The 43- and 26-kDa polypeptides are attributable to the PS II core and the oxygen-evolving complex, respectively.

Chlorophyll↗

Cyanobacterial ycf27 gene products regulate energy transfer from phycobilisomes to photosystems I and II.

Two open reading frames (slr0115 and slr0947) in the genome of the cyanobacterium Synechocystis sp. PCC 6803 are shown to be involved in the regulation of the coupling of phycobilisomes to photosynthetic reaction centres. Homologues of these genes, called ycf27, have been found in a range of phycobilin-containing organisms. The slr0115 and slr0947 gene products are OmpR-type DNA-binding response regulator proteins. Deletion of slr0115 results in increased efficiency of energy transfer from phycobilisomes to photosystem II relative to photosystem I. Reduction of the copy number of slr0947 has the opposite phenotypic effect. We have given the slr0115 and slr0947 genes the designations rpaA and rpaB respectively.

Amino Acid Sequence↗

Inhibition of electron transport at the cytochrome b(6)f complex protects photosystem II from photoinhibition.

Photoinhibition of photosystem II (PS II) activity was studied in thylakoid membranes illuminated in the presence of the inhibitor of the cytochrome b(6)f complex 2'iodo-6-isopropyl-3-methyl-2',4, 4'-trinitrodiphenylether (DNP-INT). DNP-INT was found to decrease photoinhibition. In the absence of DNP-INT, anaerobosis, superoxide dismutase and catalase protected against photoinhibition. No effect of these treatments was observed in the presence of DNP-INT. These data demonstrate that photoinhibition under these conditions is caused by reactive oxygen species which are formed most probably by the reduction of oxygen at photosystem I. The results are discussed in terms of the importance of photosynthetic control in protection against photoinhibition in vivo.

Anaerobiosis↗

Relationship between the structural and functional changes of the photosynthetic apparatus during chloroplast-chromoplast transition in flower bud of Lilium longiflorum.

The relationship between the structural and functional changes of the photosynthetic apparatus in the flower bud of Lilium longiflorum during chloroplast-chromoplast transition was examined. Compared with green petals, there was a five-fold increase of the carotenoid content in yellow petals, whereas the chlorophyll content decreased five-fold. Absorption and emission fluorescence spectra of chromoplasts indicated that newly synthesized carotenoids were not associated with photosystem II (PSII) photochemistry. The maximum quantum yield in the remaining PSII reaction centers remained constant during the chromoplast formation, whereas the photosynthetic electron transport beyond PSII became inhibited, as indicated by a marked decrease of the O2 evolution capacity, of the photochemical quenching of chlorophyll-alpha fluorescence and of the operational quantum yield of photosynthetic electron transport. Deconvoluted fluorescence emission spectra indicated a more rapid degradation of photosystem I (PSI) complexes than of PSII during chromoplast formation. Compared with green petals, the spillover between PSII and PSI decreased by approximately 40% in yellow petals. Our results indicate that during chloroplast-chromoplast transition in the flower bud of L. longiflorum, PSII integrity was preserved longer than the rest of the photosynthetic apparatus.

Light-Harvesting Protein Complexes↗

Quantitation of the rapid electron donors to P700, the functional plastoquinone pool, and the ratio of the photosystems in spinach chloroplasts.

Recent studies of chloroplast architecture have emphasized the segregation of photosystem I and photosystem II in different regions of the lamellar membrane. The apparent localization of photosystem II reaction centers in regions of membrane appression and of photosystem I reaction centers in regions exposed to the chloroplast stroma has focused attention on the intervening electron carriers, carriers which must be present to catalyze electron transfer between such spatially separated reaction sites. Information regarding the stoichiometries of these intermediate carriers is essential to an understanding of the processes that work together to establish the mechanism and to determine the rate of the overall process. We have reinvestigated the numbers of photosystem I and photosystem II reaction centers, the numbers of intervening cytochrome b6/f complexes, and the numbers of molecules of the relatively mobile electron carriers plastoquinone and plastocyanin that are actively involved in electron transfer. Our investigations were based on a new experimental technique made possible by the use of a modified indophenol dye, methyl purple, the reduction of which provides a particularly sensitive and accurate measure of electron transfer. Using this dye, which accepts electrons exclusively from photosystem I, it was possible to drain electrons from each of the carriers. Thus, by manipulation of the redox condition of the various carriers and through the use of specific inhibitors we could measure the electron storage capacity of each carrier in turn. We conclude that the ratio of photosystem I reaction centers to cytochrome b6/f complexes to photosystem II reaction centers is very nearly 1:1:1. The pool of rapid donors of electrons to P700 includes not only the 2 reducing equivalents stored in the cytochrome b6/f complex but also those stored in slightly more than 2 molecules of plastocyanin per P700. More slowly available are the electrons from about 6 plastoquinol molecules per P700.

Chlorophyll↗

Transcriptional and translational regulation of photosystem I and II genes in light-dark- and continuous-light-grown cultures of the unicellular cyanobacterium Cyanothece sp. strain ATCC 51142.

Cyanothece sp. strain ATCC 51142, a unicellular, diazotrophic cyanobacterium, demonstrated extensive metabolic periodicities of photosynthesis, respiration, and nitrogen fixation when grown under N2-fixing conditions. This report describes the relationship of the biosynthesis of photosynthesis genes to changes in the oligomerization state of the photosystems. Transcripts of the psbA gene family, encoding the photosystem II (PSII) reaction center protein D1, accumulated primarily during the light period, and net transcription reached a peak between 2 to 6 h in the light in light-dark (LD) growth and between 4 to 10 h in the subjective light when grown under continuous light (LL). The relative amount of the D1 protein (form 1 versus form 2) appeared to change during this diurnal cycle, along with changes in the PSII monomer/dimer ratio. D1 form 1 accumulated at approximately equal levels throughout the 24-h cycle, whereas D1 form 2 accumulated at significantly higher levels at approximately 8 to 10 h in the light or subjective light. The psbD gene, encoding the reaction center protein D2, also demonstrated differences between the two copies of this gene, with one copy transcribed more heavily around 6 to 8 h in the light. Accumulation of the PSI reaction center proteins PsaA and PsaB was maximal in the dark or subjective-dark periods, a period during which PSI was primarily in the trimeric form. We conclude that photosystem organization changes during the diurnal cycle to favor either noncyclic electron flow, which leads to O2 evolution and CO2 fixation, or cyclic electron flow, which favors ATP synthesis.

Bacterial Proteins↗

The BtpA protein stabilizes the reaction center proteins of photosystem I in the cyanobacterium Synechocystis sp. PCC 6803 at low temperature.

Specific inhibition of photosystem I (PSI) was observed under low-temperature conditions in the cyanobacterium Synechocystis sp. strain PCC 6803. Growth at 20 degrees C caused inhibition of PSI activity and increased degradation of the PSI reaction center proteins PsaA and PsaB, while no significant changes were found in the level and activity of photosystem II (PSII). BtpA, a recently identified extrinsic thylakoid membrane protein, was found to be a necessary regulatory factor for stabilization of the PsaA and PsaB proteins under such low-temperature conditions. At normal growth temperature (30 degrees C), the BtpA protein was present in the cell, and its genetic deletion caused an increase in the degradation of the PSI reaction center proteins. However, growth of Synechocystis cells at 20 degrees C or shifting of cultures grown at 30 degrees C to 20 degrees C led to a rapid accumulation of the BtpA protein, presumably to stabilize the PSI complex, by lowering the rates of degradation of the PsaA and PsaB proteins. A btpA deletion mutant strain could not grow photoautotrophically at low temperature, and exhibited rapid degradation of the PSI complex after transfer of the cells from normal to low temperature.

Bacterial Proteins↗

Chlamydomonas, a model system for studying the assembly and dynamics of photosynthetic complexes.

The green unicellular alga Chlamydomonas reinhardtii has emerged as a powerful model system for studying the biosynthesis of the photosynthetic apparatus and the acclimation of this system to changes in light conditions. The assembly of the photosynthetic complexes involves the coordinate interaction between the nuclear and chloroplast genetic systems. Many factors involved in specific chloroplast post-transcriptional steps have been identified and characterized. Chlamydomonas is able to adapt to changes in light quality and in cellular ATP content by performing state transition, a process that leads to a redistribution of light excitation energy between photosystem II and photosystem I and that involves the redox state of the plastoquinone pool, the cytochrome b(6)f complex and one or several kinases specific for the light-harvesting system. Genetic approaches have provided new insights into this process.

Adaptation, Physiological↗

State transitions or delta pH-dependent quenching of photosystem II fluorescence in red algae.

Fluorescence changes attributed to state transitions have been shown to exist in phycobilisome-containing organisms. Contradictory conclusions have been derived from studies about the mechanism of state transitions carried out either in cyanobacteria or in red algae. In this paper, fluorescence changes induced by light 1 and light 2 are reinvestigated in a unicellular red alga, Rhodella violacea, by performing 77 K fluorescence spectra and fluorescence yield measurements at room temperature in the presence of uncouplers and inhibitors of the electron transfer. We show that transfer of light 1-adapted cells to light 2 (green light) induces a large quenching of photosystem II which is suppressed by subsequent incubation in light 1 (far-red or blue light). The level of the photosystem I-related fluorescence does not change during these transfers. We demonstrate that the large quenching of photosystem II induced by low intensities of green light is completely suppressed by addition of NH4Cl, an uncoupler that inhibits ATP synthesis by canceling the delta pH across the membrane. DCCD, which is an inhibitor of the ATPase that swells the delta pH, maintains the quenched state even under light 1 illumination. The opposite effects of DCMU and DBMIB on state transitions are demonstrated to be due to a suppression (by DCMU) or maintenance (by DBMIB) of the delta pH and not to change in the redox state of the plastoquinone. We conclude that, in R. violacea, the fluorescence change commonly associated with state 2 transition is in fact a delta pH-dependent quenching. This type of quenching has always been associated with near-saturating light intensities. Here, we show that very low intensities of a light that activates only the photosystem II induce a delta pH across the membrane that is not dissipated since the ATPase is not activated. The delta pH is dissipated only under conditions in which the photosystem I turns, confirming that the thioredoxin must be reduced to activate the ATPase. We suggest that the fluorescence changes, induced by various light conditions, in cyanobacteria and red algae could be associated with different phenomena.

Ammonium Chloride↗

Herbicidal action of 2-hydroxy-3-alkyl-1,4-naphthoquinones.

The main mode of herbicidal activity of 2-hydroxy-3-alkyl-1,4-naphthoquinones is shown to be inhibition of photosystem II (PSII). The herbicidal and in vitro activities have been measured and correlated with their (Log)octanol/water partition coefficients (Log Ko/w). The length of the 3-n-alkyl substituent for optimal activity differed between herbicidal and in vitro activity. The maximum in vitro activity was given by the nonyl to dodecyl homologues (Log Ko/w between 6.54 and 8.12), whereas herbicidal activity peaked with the n-hexyl compound (Log Ko/w = 4.95). The effect of chain branching was also investigated using isomeric pentyl analogues substituted at position 3. All exhibited similar levels of in vitro activities but herbicidal activities differed, albeit moderately, with the exception of one analogue that was much less phytotoxic. Other modes of action were also investigated using two representative compounds. They did not show any activity on photosystem I or mitochondrial complex I, or generate toxic oxygen radicals by redox cycling reactions. Only moderate activity was found against mitochondrial complex III from plants, in contrast to much higher corresponding activity using an insect enzyme.

Algorithms↗

Photosynthetic activity of far-red light in green plants.

We have found that long-wavelength quanta up to 780 nm support oxygen evolution from the leaves of sunflower and bean. The far-red light excitations are supporting the photochemical activity of photosystem II, as is indicated by the increased chlorophyll fluorescence in response to the reduction of the photosystem II primary electron acceptor, Q(A). The results also demonstrate that the far-red photosystem II excitations are susceptible to non-photochemical quenching, although less than the red excitations. Uphill activation energies of 9.8+/-0.5 kJ mol(-1) and 12.5+/-0.7 kJ mol(-1) have been revealed in sunflower leaves for the 716 and 740 nm illumination, respectively, from the temperature dependencies of quantum yields, comparable to the corresponding energy gaps of 8.8 and 14.3 kJ mol(-1) between the 716 and 680 nm, and the 740 and 680 nm light quanta. Similarly, the non-photochemical quenching of far-red excitations is facilitated by temperature confirming thermal activation of the far-red quanta to the photosystem II core. The observations are discussed in terms of as yet undisclosed far-red forms of chlorophyll in the photosystem II antenna, reversed (uphill) spill-over of excitation from photosystem I antenna to the photosystem II antenna, as well as absorption from thermally populated vibrational sub-levels of photosystem II chlorophylls in the ground electronic state. From these three interpretations, our analysis favours the first one, i.e., the presence in intact plant leaves of a small number of far-red chlorophylls of photosystem II. Based on analogy with the well-known far-red spectral forms in photosystem I, it is likely that some kind of strongly coupled chlorophyll dimers/aggregates are involved. The similarity of the result for sunflower and bean proves that both the extreme long-wavelength oxygen evolution and the local quantum yield maximum are general properties of the plants.

Electron Transport↗

Effects of selective inactivation of individual genes for low-molecular-mass subunits on the assembly of photosystem II, as revealed by chloroplast transformation: the psbEFLJoperon in Nicotiana tabacum.

Photosystem (PSII) is a supramolecular polypeptide complex found in oxygenic photosynthetic membranes, which is capable of extracting electrons from water for the reduction of plastoquinone. An intriguing feature of this assembly is the fact that it includes more than a dozen low-mass polypeptides of generally unknown function. Using a transplastomic approach, we have individually disrupted the genes of the psbEFLJoperon in Nicotiana tabacum, which encode four such polypeptides, without impairing expression of downstream loci of the operon. All four mutants exhibited distinct phenotypes; none of them was capable of photoautotrophic growth. All mutants bleached rapidly in the light. Disruption of psbEand psbF, which code for the alpha and beta apoproteins of cytochrome b(559), abolished PSII activity, as expected; Delta psbL and Delta psbJ plants displayed residual PSII activity in young leaves. Controlled partial solubilisation of thylakoid membranes uncovered surprisingly severe impairment of PSII structure, with subunit and assembly patterns varying depending on the mutant considered. In the Delta psbL mutant PSII was assembled primarily in a monomeric form, the homodimeric form was preponderant in Delta psbJ, and, unlike the case in Delta psbZ, the thylakoids of both mutants released some PSII supercomplexes. On the other hand, Photosystem I (PSI), the cytochrome b(6)f complex, ATP synthase, LHCII, and CP24/CP26/CP29 antennae were present in near wild-type levels. The data are discussed in terms of their implications for structural, biogenetic and functional aspects of PSII.

Base Sequence↗

Involvement of active oxygen species in degradation of light-harvesting proteins under light stresses.

This paper presents evidence for light-mediated degradation of isolated light-harvesting proteins (Lhc2) and involvement of oxygen free radicals in the process. The time course of light harvesting photodestruction is much slower than that of D1 protein (requiring hours for complete breakdown). By use of mass spectrometry and amino acid sequencing, it has been revealed that the primary cleavages take place in the hydrophilic portion of the NH(2) region where oxygen-containing radicals attack randomly and not at specific sites. Moreover, these chlorophyll binding proteins are completely fragmented. From the effectiveness of scavengers and the preliminary electron paramagnetic resonance measurements reported, it appears that singlet oxygen is involved as a short-lived species, and hydroxyl and alkoxyl radicals act at higher light intensity or over a longer time, whereas hydrogen peroxide and superoxide anions are not observed. Antenna proteins appear more resistance to photodestruction in their monomeric form than in trimeric form, while minor antenna are highly sensitive. However, the organization of both minor and major proteins in the photosystem II supracomplex affords some photoprotection. Interestingly, leaves exposed to strong light contained degraded major antenna, unlike those kept in the dark, which is consistent with studies on the illumination of isolated proteins, supporting the hypothesis that active oxygen species play a role in vivo in the short-term acclimative adaptation of plants.

Amino Acid Sequence↗