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reduced cytochrome b6 + oxidized ferredoxin + hv
oxidized cytochrome b6 + reduced ferredoxin
reduced cytochrome c6 + oxidized ferredoxin + hv
oxidized cytochrome c6 + reduced ferredoxin
reduced cytochrome c6 + oxidized flavodoxin + hv
oxidized cytochrome c6 + reduced flavodoxin
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?
reduced plastocyanin + oxidized ferredoxin + hv
oxidized plastocyanin + reduced ferredoxin
reduced plastocyanin + oxidized flavodoxin + hv
oxidized plastocyanin + reduced flavodoxin
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?
additional information
?
-
reduced cytochrome b6 + oxidized ferredoxin + hv
oxidized cytochrome b6 + reduced ferredoxin
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-
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-
?
reduced cytochrome b6 + oxidized ferredoxin + hv
oxidized cytochrome b6 + reduced ferredoxin
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-
-
?
reduced cytochrome c6 + oxidized ferredoxin + hv
oxidized cytochrome c6 + reduced ferredoxin
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-
-
-
?
reduced cytochrome c6 + oxidized ferredoxin + hv
oxidized cytochrome c6 + reduced ferredoxin
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-
-
?
reduced plastocyanin + oxidized ferredoxin + hv
oxidized plastocyanin + reduced ferredoxin
-
-
-
-
?
reduced plastocyanin + oxidized ferredoxin + hv
oxidized plastocyanin + reduced ferredoxin
-
the light-harvesting complexes and internal antenna of photosystem I absorb photons and transfer the excitation energy to P700, the primary electron donor. The subsequent charge separation and electron transport leads to the reduction of ferredoxin
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-
?
reduced plastocyanin + oxidized ferredoxin + hv
oxidized plastocyanin + reduced ferredoxin
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-
-
-
?
reduced plastocyanin + oxidized ferredoxin + hv
oxidized plastocyanin + reduced ferredoxin
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-
-
-
?
reduced plastocyanin + oxidized ferredoxin + hv
oxidized plastocyanin + reduced ferredoxin
-
-
-
?
reduced plastocyanin + oxidized ferredoxin + hv
oxidized plastocyanin + reduced ferredoxin
-
the light-harvesting complexes and internal antenna of photosystem I absorb photons and transfer the excitation energy to P700, the primary electron donor. The subsequent charge separation and electron transport leads to the reduction of ferredoxin
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-
?
reduced plastocyanin + oxidized ferredoxin + hv
oxidized plastocyanin + reduced ferredoxin
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-
-
?
reduced plastocyanin + oxidized ferredoxin + hv
oxidized plastocyanin + reduced ferredoxin
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-
?
reduced plastocyanin + oxidized ferredoxin + hv
oxidized plastocyanin + reduced ferredoxin
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-
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-
?
reduced plastocyanin + oxidized ferredoxin + hv
oxidized plastocyanin + reduced ferredoxin
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-
-
-
?
reduced plastocyanin + oxidized ferredoxin + hv
oxidized plastocyanin + reduced ferredoxin
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subunit PsaE (a peripheral subunit of the PSI complex) is involved in the docking of ferredoxin/flavodoxin to the PSI complex and also participates in the cyclic electron transfer around phosphosystem I
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-
?
reduced plastocyanin + oxidized ferredoxin + hv
oxidized plastocyanin + reduced ferredoxin
-
plastocyanins from Nostoc sp. PCC 7119, Monoraphidium braunii, Arabidopsis thaliana, Spinacia oleracea, and wild-type and mutant (E85K, Q88R, E85K/Q88R, E85V, and V93K) plastocyanins from Chlamydomonas reinhardtii, docking simulations and modeling
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?
reduced plastocyanin + oxidized ferredoxin + hv
oxidized plastocyanin + reduced ferredoxin
Psychotria henryi
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?
reduced plastocyanin + oxidized ferredoxin + hv
oxidized plastocyanin + reduced ferredoxin
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-
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?
reduced plastocyanin + oxidized ferredoxin + hv
oxidized plastocyanin + reduced ferredoxin
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-
?
reduced plastocyanin + oxidized ferredoxin + hv
oxidized plastocyanin + reduced ferredoxin
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characterization of the electron donor (plastocyanin) binding site. Plastocyanin binds in a small cavity on the lumenal surface of photosystem I, close to the center and with a slight bias toward the PsaL subunit of the complex
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-
?
reduced plastocyanin + oxidized ferredoxin + hv
oxidized plastocyanin + reduced ferredoxin
-
the photosystem 1 subunit PsaF is involved in the docking of the electron-donor proteins plastocyanin and cytochrome c6, the recombinant protein binds to plastocyanin by a specific, native-like, electrostatic interaction
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-
?
reduced plastocyanin + oxidized ferredoxin + hv
oxidized plastocyanin + reduced ferredoxin
-
variations in the luminal Mg(II) concentration may modulate the binding between plastocyanin and photosystem I subunit PsaF during the light-dark transitions, being stronger in the illuminated state
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?
reduced plastocyanin + oxidized ferredoxin + hv
oxidized plastocyanin + reduced ferredoxin
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-
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-
?
reduced plastocyanin + oxidized ferredoxin + hv
oxidized plastocyanin + reduced ferredoxin
-
photosystem I (PS I) mediates electron-transfer from plastocyanin to ferredoxin via a photochemically active chlorophyll dimer (P700), a monomeric chlorophyll electron acceptor (A0), a phylloquinone (A1), and three [4Fe-4S] clusters (FX/A/B)
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-
?
reduced plastocyanin + oxidized ferredoxin + hv
oxidized plastocyanin + reduced ferredoxin
-
-
-
-
?
reduced plastocyanin + oxidized ferredoxin + hv
oxidized plastocyanin + reduced ferredoxin
-
recombinant plastocyanin is the superior electron donor to photosystem I. Detailed analysis of PSI-mediated linear electron transfer from reduced plastocyanin to NADP+, in thylakoid membranes of wild type and a psaE mutant of Synechocystis PCC 6803
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-
?
reduced plastocyanin + oxidized ferredoxin + hv
oxidized plastocyanin + reduced ferredoxin
-
the light-harvesting complexes and internal antenna of photosystem I absorb photons and transfer the excitation energy to P700, the primary electron donor. The subsequent charge separation and electron transport leads to the reduction of ferredoxin
-
-
?
reduced plastocyanin + oxidized ferredoxin + hv
oxidized plastocyanin + reduced ferredoxin
-
-
-
?
reduced plastocyanin + oxidized ferredoxin + hv
oxidized plastocyanin + reduced ferredoxin
ferredoxin from Thermosynechococcus elongatus
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-
?
reduced plastocyanin + oxidized ferredoxin + hv
oxidized plastocyanin + reduced ferredoxin
Thermosynechococcus vestitus
-
-
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-
?
reduced plastocyanin + oxidized ferredoxin + hv
oxidized plastocyanin + reduced ferredoxin
Thermosynechococcus vestitus
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ferredoxin from Thermosynechococcus elongatus
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-
?
additional information
?
-
photo-oxidation of P700 causes a broad increase in absorption in the near-infrared region due to presence of a chlorophyll cation radical (P700+)
-
-
?
additional information
?
-
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in vitro plastoquinone reduction assay with the addition of ferredoxin
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-
?
additional information
?
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in the Phaeodactylum tricornutum alga, as inmost diatoms, cytochrome c6 is the only electron donor to photosystem I, and thus they lack plastocyanin as an alternative electron carrier. Analysis of electron transfer to Phaeodactylum photosystem I from several plastocyanins from cyanobacteria, green algae and plants, as compared with its own cytochrome c6, overview. Diatom photosystem I is able to effectively react with eukaryotic acidic plastocyanins, although with less efficiency than with Phaeodactylum cytochrome c6. This efficiency increases in some green alga plastocyanin mutants mimicking the electrostatics of the interaction site on the diatom cytochrome. In addition, the structure of the transient electron transfer complex between cytochrome c6 and photosystem I from Phaeodactylum is analyzed by computational docking and compared to that of green lineage and mixed systems. The Phaeodactylum system shows a lower efficiency than the green systems, both in the formation of the properly arranged [cytochrome c6-photosystem I] complex and in the electron transfer itself. Structural modeling, overview
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?
additional information
?
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oxygen uptake in the light is analyzed in suspensions of isolated pea thylakoids upon inhibition of electron transport from photosystem II (PS II) by diuron and delivery of electrons to photosystem I (PS I) by means of artificial donors in the presence of ascorbate, O2 reduction in PS I. 2,6-dichlorophenolindophenol (DCPIP) cannot be used as the donor for photosystem I. N,N,N',N'-tetramethyl-p-phenylene diamine (TMPD), applied as a donor, does not affect immediately the reaction of the O2 reduction, since an increase in its concentration does not lead to an increase in the oxygen uptake rate in the light. In the experiments with TMPD, an increase in light intensity leads to an increase in the oxygen uptake rate, and this fact was interpreted as a consequence of the increase in the apparent rate constant of the reaction of the O2 reduction by the components of the acceptor side of photosystem I. TMPD redox transformation consists of only one step, while the DCPIP transformation includes two steps. Ascorbate is capable of donating electrons to the primary pair of PS I cofactors, P700+. Addition of either DCPIP or TMPD at concentration of 0.05 mM to the suspension containing both DCMU and ascorbate results in the twofold increase in the rate of the O2 consumption. O2 reduction by PS I uses ascorbate alone or in combination with lipophilic compounds as immediate donor of electrons
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?
additional information
?
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thylakoids freshly isolated from spinach are assayed for their ability to generate a light driven proton gradient. While high rates of cyclic electron flow are observed in vivo, isolated thylakoids show only very slow rates, suggesting that the activity of a key complex is lost or downregulated upon isolation. Isolation of thylakoids in the complete absence of DTTRED leads to loss of CEF activity that is only partially restored by subsequent addition of 2 mM DTTRED, redox titration of CEF activity, overview
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?
additional information
?
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interaction analysis of photosystem I (PS I) complexes from cyanobacteria Synechocystis sp. PCC 6803 containing various quinones in the A1-site (phylloquinone PhQ in the wild-type strain and plastoquinone (PQ) or 2,3-dichloronaphthoquinone (Cl2NQ) in the menB deletion strain) and different numbers of Fe4S4 clusters (intact wild-type and ferredoxin-core complexes depleted of FA/FB centers) with external acceptors, overview. The electron transfer chain of PS I consists of the primary donor-chlorophyll (Chl) dimer P700, primary acceptor A0 (four Chl molecules), A1 (two phylloquinone molecules), and iron-sulfur clusters FX, FA, and FB.The terminal FA/FB clusters are located on the small extrinsic PsaC subunit. Electron transport in PS I occurs through both branches of the redox cofactors A and B from P700 to FX. Reaction center of PS I contains two molecules of phylloquinone (PhQ) that are characterized by extremely low midpoint redox potential
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?
additional information
?
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photo-oxidation of P700 causes a broad increase in absorption in the near-infrared region due to presence of a chlorophyll cation radical (P700+)
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?
additional information
?
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reduction of ferredoxin by photosystem I (PSI) involves the [4Fe-4S] clusters FA and FB harbored by subunit PsaC, with FB being the direct electron transfer partner of ferredoxin. Assay in presence of 5 mM MgCl2, 30 mM NaCl and 0.03% beta-dodecyl-maltoside, with 1-2.5 mM sodium ascorbate and 0.008-0.025 mM 2,6-dichlorophenolindophenol
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?
additional information
?
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upon light excitation, the excited singlet state of the primary electron donor, P700 delivers an electron to the primary Chl acceptor A0A/ A0B forming the charge-separated state P700 +A0-. The electron is then transferred in sequence to A1A/ A1B, to the iron-sulfur cluster FX, and ultimately to FA/FB. The side production of superoxide radical in the A1-site by oxygen reduction via the Mehler reaction might comprise about 0.3% of the total electron flow in photosystem I, PS I. Interaction of PS I with external acceptors, methylviologen, 2,3-dichloro-naphthoquinone and oxygen, overview. Analysis of PS I complexes containing various quinones in the A1-binding site, i.e. phylloquinone PhQ, plastoquinone-9 PQ and 2,3-dichloro-naphthoquinone, as well as FX-core complexes, depleted of terminal iron-sulfur FA/FB clusters
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?
additional information
?
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Thermosynechococcus vestitus
-
reduction of ferredoxin by photosystem I (PSI) involves the [4Fe-4S] clusters FA and FB harbored by subunit PsaC, with FB being the direct electron transfer partner of ferredoxin. Assay in presence of 5 mM MgCl2, 30 mM NaCl and 0.03% beta-dodecyl-maltoside, with 1-2.5 mM sodium ascorbate and 0.008-0.025 mM 2,6-dichlorophenolindophenol
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?
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2,3-dichloronaphthoquinone
in the mutant menB deletion strain
beta-carotene
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beta-carotene
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cyanobacterial PSI complexes contain 22 molecules of beta-carotene, 17 of which are in all-trans configuration
Chlorophyll
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173 chlorophyll molecules in the structure of the entire PSI super-complex. Chl1303 is located in the gap region between the core complex and the light-harvesting complex (LHCI). The Chl1303 position is sufficient for excitation energy transfer from the Lhca14 dimer to the core through chlorophylls 1302 and 1305
Chlorophyll
-
photosystem I (PS I) mediates electron-transfer from plastocyanin to ferredoxin via a photochemically active chlorophyll dimer (P700), a monomeric chlorophyll electron acceptor (A0), a phylloquinone (A1), and three [4Fe-4S] clusters (FX/A/B)
chlorophyll a
-
most abundant cofactor in PSI, role of these molecules in light absorption, charge separation, electron transfer, and biogenesis
chlorophyll a
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most abundant cofactor in PSI, role of these molecules in light absorption, charge separation, electron transfer, and biogenesis
chlorophyll a
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most abundant cofactor in PSI, role of these molecules in light absorption, charge separation, electron transfer, and biogenesis
chlorophyll a'
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one member of the P700 special pair is a chlorophyll a' molecule
chlorophyll a'
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one member of the P700 special pair is a chlorophyll a' molecule
chlorophyll a'
-
one member of the P700 special pair is a chlorophyll a' molecule
Ferredoxin
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Ferredoxin
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location of the ferredoxin-binding site in photosystem I, ferredoxin is bound on top of the stromal ridge principally interacting with the extrinsic subunits PsaC and PsaE
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iron-sulfur centre
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a PSI complex contains 12 iron atoms that constitute 3 [4Fe-4S] clusters
iron-sulfur centre
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a PSI complex contains 12 iron atoms that constitute 3 [4Fe-4S] clusters
iron-sulfur centre
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a PSI complex contains 12 iron atoms that constitute 3 [4Fe-4S] clusters
iron-sulfur centre
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electron transfer from the primary electron donor P700 to the FA/FB centers is demonstrated by flash-induced absorption change of the isolated reaction center complex, while electron paramagnetic resonance spectroscopy shows that the reaction center complex contains a full set of FeS clusters
Lipid
-
four lipid molecules can be assigned in the high-resolution structure of PSI. Three of these molecules are phosphatidylglycerol and one is monogalactosyldiacylglycerol. These molecules are embedded in the PSI complex, with the acyl chains anchored among transmembrane helices. The phosphodiester group of one of the phospholipids coordinates an antenna chlorophyll molecule
Lipid
-
four lipid molecules can be assigned in the high-resolution structure of PSI. Three of these molecules are phosphatidylglycerol and one is monogalactosyldiacylglycerol. These molecules are embedded in the PSI complex, with the acyl chains anchored among transmembrane helices. The phosphodiester group of one of the phospholipids coordinates an antenna chlorophyll molecule
Lipid
-
four lipid molecules can be assigned in the high-resolution structure of PSI. Three of these molecules are phosphatidylglycerol and one is monogalactosyldiacylglycerol. These molecules are embedded in the PSI complex, with the acyl chains anchored among transmembrane helices. The phosphodiester group of one of the phospholipids coordinates an antenna chlorophyll molecule
phylloquinone
-
phylloquinone
-
photosystem I (PS I) mediates electron-transfer from plastocyanin to ferredoxin via a photochemically active chlorophyll dimer (P700), a monomeric chlorophyll electron acceptor (A0), a phylloquinone (A1), and three [4Fe-4S] clusters (FX/A/B)
phylloquinone
-
the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
phylloquinone
-
the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
phylloquinone
-
the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
phylloquinone
in the wild-type strain
plastoquinone
-
plastoquinone
in the mutant menB deletion strain
[4Fe-4S] center
-
photosystem I (PS I) mediates electron-transfer from plastocyanin to ferredoxin via a photochemically active chlorophyll dimer (P700), a monomeric chlorophyll electron acceptor (A0), a phylloquinone (A1), and three [4Fe-4S] clusters (FX/A/B). Iron-sulfur cluster FA is in closer proximity to P700 than the FB cluster
[4Fe-4S] center
-
the enzyme contains three [4Fe-4S] clusters: FA, FB and FX
[4Fe-4S]-center
cluster Fx
[4Fe-4S]-center
Thermosynechococcus vestitus
-
reduction of ferredoxin by photosystem I (PSI) involves the [4Fe-4S] clusters FA and FB harbored by subunit PsaC, with FB being the direct electron transfer partner of ferredoxin
[4Fe-4S]-center
reduction of ferredoxin by photosystem I (PSI) involves the [4Fe-4S] clusters FA and FB harbored by subunit PsaC, with FB being the direct electron transfer partner of ferredoxin
[4Fe-4S]-center
the enzyme contains [4Fe-4S] clusters
additional information
the electron transfer chain of PS I consists of the primary donor-chlorophyll (Chl) dimer P700, primary acceptor A0 (four Chl molecules), A1 (two phylloquinone molecules), and iron-sulfur clusters FX, FA, and FB. The terminal FA/FB clusters are located on the small extrinsic PsaC subunit. Electron transport in PS I occurs through both branches of the redox cofactors A and B from P700 to FX. 2,3-Dichlorophenolindophenol reduced by ascorbate serves as an external electron donor for the photooxidized P700, while methylviologen plays a role of external acceptor capturing electrons from the photoreduced terminal FA/FB cluster
-
additional information
the electron-transfer cofactors are arranged in two nearly symmetric branches extending across the membrane from P700, which is a dimer of Chl a and a C-13 epimer of Chl a. Each branch contains an additional pair of Chl a molecules (ec2A/ec3A or ec2B/ec3B) and a phylloquinone (PhQA or PhQB), overview
-
additional information
the electron-transfer cofactors are arranged in two nearly symmetric branches extending across the membrane from P700, which is a dimer of Chl a and a C-13 epimer of Chl a. Each branch contains an additional pair of Chl a molecules (ec2A/ec3A or ec2B/ec3B) and a phylloquinone (PhQA or PhQB), overview
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Anemia, Hypochromic
Adaptation to Fe-deficiency requires remodeling of the photosynthetic apparatus.
Anemia, Hypochromic
Interaction of Chloroplasts with Inhibitors: Induction of Chlorosis by Diuron During Prolonged Illumination in Vitro.
Confusion
Early research on the role of plastocyanin in photosynthesis.
Dehydration
Differences in the stimulation of cyclic electron flow in two tropical ferns under water stress are related to leaf anatomy.
Dehydration
Differential effects of severe water stress on linear and cyclic electron fluxes through Photosystem I in spinach leaf discs in CO(2)-enriched air.
Dehydration
Effects of dehydration on the electron transport of Chlorella. An in vivo fluorescence study.
Dehydration
Molecular reorganization induced by Ca2+ of plant photosystem I reconstituted into phosphatidylglycerol liposomes.
Dehydration
Reflectance and Cyclic Electron Flow as an Indicator of Drought Stress in Cotton (Gossypium hirsutum).
Dehydration
Trehalose matrix effects on charge-recombination kinetics in Photosystem I of oxygenic photosynthesis at different dehydration levels.
Hypersensitivity
Lack of the small plastid-encoded PsbJ polypeptide results in a defective water-splitting apparatus of photosystem II, reduced photosystem I levels, and hypersensitivity to light.
Infections
A myovirus encoding both photosystem I and II proteins enhances cyclic electron flow in infected Prochlorococcus cells.
Infections
AS-1 cyanophage infection inhibits the photosynthetic electron flow of photosystem II in Synechococcus sp. PCC 6301, a cyanobacterium.
Infections
Catharanthus roseus, an Experimental Host Plant for the Citrus Strain of Xylella fastidiosa.
Infections
Catharanthus roseus, an experimental host plant for the citrus strain of Xylella fastidiosa.
Infections
Cypress canker induced inhibition of photosynthesis in field grown cypress (Cupressus sempervirens L.) needles.
Infections
Light Suppresses Bacterial Population through the Accumulation of Hydrogen Peroxide in Tobacco Leaves Infected with Pseudomonas syringae pv. tabaci.
Infections
Photoinhibition and photoinhibition-like damage to the photosynthetic apparatus in tobacco leaves induced by pseudomonas syringae pv. Tabaci under light and dark conditions.
Iron Deficiencies
A chlorophyll a/b-binding protein homolog that is induced by iron deficiency is associated with enlarged photosystem I units in the eucaryotic alga Dunaliella salina.
Iron Deficiencies
A Nucleus-Encoded Chloroplast Phosphoprotein Governs Expression of the Photosystem I Subunit PsaC in Chlamydomonas reinhardtii.
Iron Deficiencies
Adaptation to iron deficiency: a comparison between the cyanobacterium Synechococcus elongatus PCC 7942 wild-type and a DpsA-free mutant.
Iron Deficiencies
Alteration of proteins and pigments influence the function of photosystem I under iron deficiency from Chlamydomonas reinhardtii.
Iron Deficiencies
An internal antisense RNA regulates expression of the photosynthesis gene isiA.
Iron Deficiencies
Changes in the LHCI aggregation state during iron repletion in the unicellular red alga Rhodella violacea.
Iron Deficiencies
Chlorophyll-Proteins and Electron Transport during Iron Nutrition-Mediated Chloroplast Development.
Iron Deficiencies
Differential degradation of photosystem I subunits under iron deficiency in rice.
Iron Deficiencies
Effects of iron limitation on the expression of metabolic genes in the marine cyanobacterium Trichodesmium erythraeum IMS101.
Iron Deficiencies
Fe deficiency induced changes in rice (Oryza sativa L.) thylakoids.
Iron Deficiencies
Fluorescence quenching of IsiA in early stage of iron deficiency and at cryogenic temperatures.
Iron Deficiencies
How does iron deficiency disrupt the electron flow in photosystem I of lettuce leaves?
Iron Deficiencies
Iron acquisition and allocation in stramenopile algae.
Iron Deficiencies
Iron deficiency in cyanobacteria causes monomerization of photosystem I trimers and reduces the capacity for state transitions and the effective absorption cross section of photosystem I in vivo.
Iron Deficiencies
Iron deficiency induces a chlorophyll d-binding Pcb antenna system around Photosystem I in Acaryochloris marina.
Iron Deficiencies
Iron Deficiency Induces a Partial Inhibition of the Photosynthetic Electron Transport and a High Sensitivity to Light in the Diatom Phaeodactylum tricornutum.
Iron Deficiencies
Iron deficiency induces the formation of an antenna ring around trimeric photosystem I in cyanobacteria.
Iron Deficiencies
N-terminal processing of Lhca3 Is a key step in remodeling of the photosystem I-light-harvesting complex under iron deficiency in Chlamydomonas reinhardtii.
Iron Deficiencies
Structural analysis of the photosystem I supercomplex of cyanobacteria induced by iron deficiency.
Iron Deficiencies
Structural response of Photosystem 2 to iron deficiency: characterization of a new photosystem 2-IdiA complex from the cyanobacterium Thermosynechococcus elongatus BP-1.
Iron Deficiencies
[Structural and functional organization of chloroplasts in leaves of Pisum sativum L. under conditions of root hypoxia and iron deficiency]
Magnesium Deficiency
Magnesium deficiencyinduced impairment of photosynthesis in leaves of fruiting Citrus reticulata trees accompanied by up?regulation of antioxidant metabolism to avoid photo?oxidative damage
Magnesium Deficiency
Preferential damaging effects of limited magnesium bioavailability on photosystem I in Sulla carnosa plants.
Neoplasms
Cancer Cell Specific Delivery of Photosystem I Through Integrin Targeted Liposome Shows Significant Anticancer Activity.
Neoplasms
Discovery and design of self-assembling peptides.
Photophobia
Chloroplast site-directed mutagenesis of photosystem I in Chlamydomonas: electron transfer reactions and light sensitivity.
photosystem i deficiency
Biochemical and molecular characterization of photosystem I deficiency in the NCS6 mitochondrial mutant of maize.
Retinoblastoma
Molecular photovoltaics and the photoactivation of mammalian cells.
Starvation
Aggregates of the chlorophyll-binding protein IsiA (CP43') dissipate energy in cyanobacteria.
Starvation
Ca(2+)-regulated cyclic electron flow supplies ATP for nitrogen starvation-induced lipid biosynthesis in green alga.
Starvation
Diatom proteomics reveals unique acclimation strategies to mitigate Fe limitation.
Starvation
Energy transfer and trapping in the Photosystem I complex of Synechococcus PCC 7942 and in its supercomplex with IsiA.
Starvation
Far-red light-regulated efficient energy transfer from phycobilisomes to photosystem I in the red microalga Galdieria sulphuraria and photosystems-related heterogeneity of phycobilisome population.
Starvation
Light-induced energy dissipation in iron-starved cyanobacteria: roles of OCP and IsiA proteins.
Starvation
Population-level coordination of pigment response in individual cyanobacterial cells under altered nitrogen levels.
Starvation
RESPONSE OF NANNOCHLOROPSIS GADITANA TO NITROGEN STARVATION INCLUDES A DE NOVO BIOSYNTHESIS OF TRIACYLGLYCEROLS, A DECREASE OF CHLOROPLAST GALACTOLIPIDS AND A REORGANIZATION OF THE PHOTOSYNTHETIC APPARATUS.
Starvation
Spectroscopic properties of PSI-IsiA supercomplexes from the cyanobacterium Synechococcus PCC 7942.
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evolution
it is proposed that PSI evolved stepwise from a trimeric form to tetrameric oligomer en route to becoming monomeric in plants/algae
malfunction
-
impairment of NDH-dependent cyclic electron flow in rice specifically causes a reduction in the electron transport rate through PS I (ETR I) at low light intensity with a concomitant reduction in CO2 assimilation rate, plant biomass and importantly, grain production, while there is no effect on PS II function at low or high light intensity. Oryza sativa crr6 mutant does not accumulate the NDH complex, CRR6 is specifically required for the assembly of NdhI in subcomplex A of chloroplast NDH, knockout of the crr6 gene in rice also leads to the lack of intact chloroplast NDH, no formation of a NDH-PS I supercomplex in the Crr6 mutant. Phenotype overview
malfunction
-
photosynthetic performance is affected in WHY1 knockout mutant under different light conditions. Loss of WHIRLY1 decreases chloroplast NAD(P)H dehydrogenase-like complex (NDH) activity and the accumulation of NDH supercomplex. Loss of WHIRLY1 leads to a higher photochemical quantum yield of photosystem I Y(I) and electron transport rate and a lower non-photochemical quenching involved in the thermal dissipation of excitation energy of chlorophyll fluorescence than the wild-type. Several genes encoding the PSI-NDH complexes are also upregulated in kowhy1 and the whirly1whirly3 double mutant (ko1/3) but steady in oepWHY1 plants. Under high light conditions, both kowhy1 and ko1/3 plants show lower electron transport rate than wild-type which are contrary to that under normal light condition. Moreover, the expression of several PSI-NDH encoding genes and ERF109, which is related to jasmonate (JA) response, varies in kowhy1 under different light conditions. Loss of WHY1 seems to increase photosystem I quantum yield but not photosystem II quantum yield, phenotype, overview. Overexpression of WHY1 in both nucleus and plastid improves the transcription level of a number of genes encoding PSI core subunits which are essential to the formation of super complexes of PSI
malfunction
site-directed mutagenesis of residues involved in the respective phylloquinone-binding sites results in a specific alteration of the rates of semiquinone oxidation. Mutation in the PhQA binding pocket (PsaA-F689N) in PSI of Chlamydomonas reinhardtii reduces down PhQA- oxidation kinetics by almost two orders of magnitude. This creates an unprecedented situation in which the reduction of P700+ is faster than the oxidation of the semiquinone, thereby providing the opportunity to initiate a second photochemical event while PhQA- is still present in ETCA, kinetics, overview
malfunction
the PsaA-N604L mutation (near ec2B) results in a 50% reduction in the amount of electron transfer in the cofactor B-branch, while the PsaB-N591L mutation (near ec2A) results in a 70% reduction in the amount of electron transfer in the cofactor A-branch. The PsaB-N591L mutation had a significant effect upon trapping, while the PsaA-N604L mutation does not have a significant effect upon trapping
malfunction
the PsaA-N604L mutation (near ec2B) results in a 50% reduction in the amount of electron transfer in the cofactor B-branch, while the PsaB-N591L mutation (near ec2A) results in a 70% reduction in the amount of electron transfer in the cofactor A-branch. The PsaB-N591L mutation had a significant effect upon trapping, while the PsaA-N604L mutation does not have a significant effect upon trapping
malfunction
-
photosynthetic performance is affected in WHY1 knockout mutant under different light conditions. Loss of WHIRLY1 decreases chloroplast NAD(P)H dehydrogenase-like complex (NDH) activity and the accumulation of NDH supercomplex. Loss of WHIRLY1 leads to a higher photochemical quantum yield of photosystem I Y(I) and electron transport rate and a lower non-photochemical quenching involved in the thermal dissipation of excitation energy of chlorophyll fluorescence than the wild-type. Several genes encoding the PSI-NDH complexes are also upregulated in kowhy1 and the whirly1whirly3 double mutant (ko1/3) but steady in oepWHY1 plants. Under high light conditions, both kowhy1 and ko1/3 plants show lower electron transport rate than wild-type which are contrary to that under normal light condition. Moreover, the expression of several PSI-NDH encoding genes and ERF109, which is related to jasmonate (JA) response, varies in kowhy1 under different light conditions. Loss of WHY1 seems to increase photosystem I quantum yield but not photosystem II quantum yield, phenotype, overview. Overexpression of WHY1 in both nucleus and plastid improves the transcription level of a number of genes encoding PSI core subunits which are essential to the formation of super complexes of PSI
-
malfunction
-
site-directed mutagenesis of residues involved in the respective phylloquinone-binding sites results in a specific alteration of the rates of semiquinone oxidation. Mutation in the PhQA binding pocket (PsaA-F689N) in PSI of Chlamydomonas reinhardtii reduces down PhQA- oxidation kinetics by almost two orders of magnitude. This creates an unprecedented situation in which the reduction of P700+ is faster than the oxidation of the semiquinone, thereby providing the opportunity to initiate a second photochemical event while PhQA- is still present in ETCA, kinetics, overview
-
metabolism
cyclic electron flow (CEF) can be stimulated to provide significant additional protection in plants when they are confronted with acidic pH conditions. But at low pH, the photosynthetic efficiency greatly decreases resulting in excessive excitation pressure in PS II and consequently an increased risk of damage on the donor side of PS II
metabolism
-
the physiological contribution of NDH-mediated CEF is greater in C4 photosynthesis than in C3 photosynthesis, suggesting that the mechanism of PET in C4 photosynthesis has changed from that in C3 photosynthesis accompanying the changes in the mechanism of CO2 assimilation
physiological function
-
Cyclic electron flow (CEF) can produce ATP without producing NADPH by transporting electrons from the accepter side of PSI to plastoquinone in a cyclic manner and promoting proton translocation across the thylakoid membrane. CEF around PSI mediated by chloroplast NADH dehydrogenase-like complex (NDH), is an alternative pathway of photosynthetic electron transport (PET) and plays a crucial role in C4 photosynthesis, although the contribution of NDH-mediated CEF is small in C3 photosynthesis. NDH-suppressed plants grow poorly, especially under low light conditions. Electron donation to PSI from NDH occurs via the Cyt b6/f complex, the Cyt b6/f complex functions as a proton pump across the thylakoid membrane
physiological function
cyclic electron flow (CEF) PS I is a highly dynamic, regulated and large capacity pathway involving ferredoxin (Fd) and Cytb6f complex. In CEF, the plastoquinone (PQ) pool is reduced by Fd which is photoreduced by PS I. The reduced PQ pool is oxidized by the Cytb6f complex, where DpH is generated across thylakoid membranes through the Q cycle. This DpH drives ATP synthase and produces the ATP required for the net CO2 assimilation and also stimulates NPQ. It has been proposed that there are two physiological functions of CEF in thylakoid membrane. During photosynthesis, cyclic electron flow around PSI can generate a pH gradient across the thylakoid membrane that not only is used to synthesize ATP, but can also induce thermal dissipation and provide protection for the photosynthetic apparatus
physiological function
photosystem I (PS I) is a key pigment-protein complex of the electron transfer (ET) chain of oxygenic photosynthetic organisms. It includes both a large antenna system for harvesting solar energy and a photochemical reaction center catalyzing charge separation across the membrane. PS I is the key element of the energy-transducing pathways because the electron flow in thylakoids is controlled by the redox states of cofactors in the acceptor part of PS I
physiological function
photosystem I (PSI) is a large pigment-protein complex that functions as a light-driven oxidoreductase, catalyzing an otherwise uphill electron transfer from cytochrome c or plastocyanin to ferredoxin or flavodoxin
physiological function
photosystem I (PSI) is a large pigment-protein complex that functions as a light-driven oxidoreductase, catalyzing an otherwise uphill electron transfer from cytochrome c or plastocyanin to ferredoxin or flavodoxin
physiological function
photosystem I (PSI) is one of two large reaction centres responsible for converting light photons into the chemical energy needed to sustain life. In the thylakoid membranes of plants, PSI is found together with its integral light-harvesting antenna, light-harvesting complex I (LHCI), in a membrane supercomplex containing hundreds of light-harvesting pigments
physiological function
pigment-protein complex of photosystem I (PS I) is one of the crucial enzymes in the electron transfer (ET) chain in thylakoid membranes of oxygenic photosynthetic organisms. PS I complex catalyzes the light-driven ET from peripheral donor proteins plastocyanin or cytochrome c6 to ferredoxin or flavodoxin. Electron transport in PS I occurs through both branches of the redox cofactors A and B from P700 to FX
physiological function
-
plastid-nucleus-located WHIRLY1 protein, which plays a role in regulating leaf senescence and is believed to associate with the increase of reactive oxygen species delivered from redox state of the photosynthetic electron transport chain, interacts with light-harvesting protein complex I (LHCA1) and affects the expression of genes encoding photosystem I (PSI) and light harvest complexes (LHCI). WHY1 might not regulate the NDH-PSI super complex genes directly in transcriptional level, but have a role in the formation of NDH-PSI super complex. WHY1 in chloroplast may have a protective effect on photosystem I, and WHIRLY1 may act as a communicator between the plastids and the nucleus
physiological function
the chloroplast must regulate supply of reducing equivalents and ATP to meet rapid changes in downstream metabolic demands. Cyclic electron flow around photosystem I (CEF) is proposed to balance the ATP/NADPH budget by using reducing equivalents to drive plastoquinone reduction, leading to the generation of proton motive force and subsequent ATP synthesis. Photosynthetic energy is stored by linear electron flow (LEF), which involves electron transfer through both photosystem II (PS II) and photosystem I (PS I). Multiple alternative electron pathways are identified or proposed including the water-water cycle, themalate shunt, the plastid terminal oxidase, and cyclic electron flow around photosystem I (CEF). Cyclic electron flow can alleviate an ATP deficit by passing electrons fromthe acceptor side of PS I back to PQ, driving the translocation of protons into the lumen without net reduction of NADP+. High rates of CEF are readily measured in vivo
physiological function
two functional electron transfer (ET) chains, related by a pseudo-C2 symmetry, are present in the reaction center of photosystem I (PSI). Due to slight differences in the environment around the cofactors of the two branches, there are differences in both the kinetics of ET and the proportion of ET that occurs on the two branches. The oxidation rates of the reduced phylloquinone (PhQ) cofactor differ by an order of magnitudes. The presence of PhQ-A does not impact the overall quantum yield and leads to an almost complete redistribution of the fractional utilization of the two functional ET chains, in favor of the one that does not bear the charged species, molecular mechanism that gives rise to the high quantum efficiency in PSI, overview
physiological function
-
while linear electron transport generates both ATP and NADPH, cyclic electron transport around photosystem I (PS I) is exclusively involved in ATP synthesis without the accumulation of NADPH. The role of cyclic electron transport around PS I is proposed to be essential for balancing the ATP/NADPH production ratio and/or for protecting both photosystems from the damage via stromal overreduction. Two pathways of PS I cyclic electron transport have been proposed: the main pathway depends on PGR5 (proton gradient regulation 5) and PGRL1 (PGR5-like photosynthetic phenotype) proteins, whereas the minor pathway is mediated by a chloroplast NADH dehydrogenase-like (NDH) complex. The chloroplast NDH-dependent PS I cyclic electron transport plays a role in alleviation of oxidative damage in strong light. Significant physiological function for the chloroplast NDH at low light intensities commonly experienced during the reproductive and ripening stages of rice cultivation that have adverse effects crop yield. Regulation of photosynthetic electron transport in the thylakoid membrane of chloroplasts is fundamental for the maximum photosynthetic yield and plant growth. Formation of a NDH-PS I supercomplex
physiological function
-
plastid-nucleus-located WHIRLY1 protein, which plays a role in regulating leaf senescence and is believed to associate with the increase of reactive oxygen species delivered from redox state of the photosynthetic electron transport chain, interacts with light-harvesting protein complex I (LHCA1) and affects the expression of genes encoding photosystem I (PSI) and light harvest complexes (LHCI). WHY1 might not regulate the NDH-PSI super complex genes directly in transcriptional level, but have a role in the formation of NDH-PSI super complex. WHY1 in chloroplast may have a protective effect on photosystem I, and WHIRLY1 may act as a communicator between the plastids and the nucleus
-
physiological function
-
two functional electron transfer (ET) chains, related by a pseudo-C2 symmetry, are present in the reaction center of photosystem I (PSI). Due to slight differences in the environment around the cofactors of the two branches, there are differences in both the kinetics of ET and the proportion of ET that occurs on the two branches. The oxidation rates of the reduced phylloquinone (PhQ) cofactor differ by an order of magnitudes. The presence of PhQ-A does not impact the overall quantum yield and leads to an almost complete redistribution of the fractional utilization of the two functional ET chains, in favor of the one that does not bear the charged species, molecular mechanism that gives rise to the high quantum efficiency in PSI, overview
-
additional information
charge transfer and recombination reactions in intact and PsaC-depleted (FX-core) wild-type PS I complexes and in the menB PS I complexes containing plastoquinone (menB-PQ) and 2,3-dichloro-1,4-naphthoquinone (menB-Cl2NQ), overview. 2,3-Dichlorophenolindophenol reduced by ascorbate serves as an external electron donor for the photooxidized P700, while methylviologen plays a role of external acceptor capturing electrons from the photoreduced terminal FA/FB cluster
additional information
cyclic electron flow around photosystem I is enhanced at low pH of 5.5. The light response curve of PS I is significantly affected by acidification of the thylakoid membranes
additional information
-
cyclic electron flow around photosystem I is enhanced at low pH of 5.5. The light response curve of PS I is significantly affected by acidification of the thylakoid membranes
additional information
-
cytochrome c6 in the Phaeodactylum tricornutum alga, as inmost diatoms, is the only electron donor to photosystem I, and thus they lack plastocyanin as an alternative electron carrier
additional information
in photosystem I, light-induced electron transfer can occur in either of two symmetry-related branches of cofactors, each of which is composed of a pair of chlorophylls (ec2A/ec3A or ec2B/ec3B) and a phylloquinone (PhQA or PhQB). The axial ligand to the central Mg2+ of the ec2A and ec2B chlorophylls is a water molecule that is also H-bonded to a nearby Asn residue, an important interaction for charge separation by converting each of the Asn residues to a Leu in the cyanobacterium Synechocystis sp. PCC6803. Each branch of the reaction center appears to operate independently of the other in carrying out light-induced charge separation
additional information
in photosystem I, light-induced electron transfer can occur in either of two symmetry-related branches of cofactors, each of which is composed of a pair of chlorophylls (ec2A/ec3A or ec2B/ec3B) and a phylloquinone (PhQA or PhQB). The axial ligand to the central Mg2+ of the ec2A and ec2B chlorophylls is a water molecule that is also H-bonded to a nearby Asn residue, an important interaction for charge separation by converting each of the Asn residues to a Leu in the green alga, Chlamydomonas reinhardtii. Each branch of the reaction center appears to operate independently of the other in carrying out light-induced charge separation
additional information
lipid structure and enzyme complex structure analysis of photosystem I supercomplex including light-harvesting complex I, PSI-LHCI, overview. Foerster rate calculations reveal the importance of the luminal-side pigment junctions. Chlorophyll b molecules are coordinated by a mixture of polar and hydrophobic interactions
additional information
PS I binding analysis using redox-inactive gallium ferredoxin, overview. Gallium ferredoxin binds to PSI competitively with ferredoxin suggesting a single ferredoxin-binding site in PSI, kinetics
additional information
Thermosynechococcus vestitus
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PS I binding analysis using redox-inactive gallium ferredoxin, overview. Gallium ferredoxin binds to PSI competitively with ferredoxin suggesting a single ferredoxin?binding site in PSI, kinetics
additional information
the membrane-embedded core of each PS I monomer is formed by the two largest subunits, PsaA and PsaB, which bind electron transport cofactors arranged in two symmetrical branches, A and B, extending from P700, a pair of chlorophyll a molecules located on the lumenal side, to the [4Fe-4S] cluster FX, placed on the opposite stromal side of the complex. Each of the two branches, related by a pseudo-C2 rotation axis which passes through P700 and FX, carries two electronically coupled Chl a molecules (termed A0A or A0B) and one phylloquinone A1A or A1B
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?
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21000-22000 Da, photosystem 1 subunit PsaF that is involved in the docking of the electron-donor proteins plastocyanin and cytochrome c6, SDS-PAGE
dimer
in strain TS-821 PSI forms tetrameric, dimeric, and monomeric species, a tetrameric PSI has two PSI dimers associated together with interdimer gaps, while the PSI dimer is composed of two tightly tethered PSI monomers, subunit organization, structure comparisons, overview
heterotetramer
two-dimensional maps obtained by single particle electron microscopy clearly show that the tetramer lacks four-fold symmetry and is actually composed of a dimer of dimers with C2 symmetry, cryo-electron microscopy is used for 3D reconstruction of the PSI tetramer complex and a 3D model at 11.5 A resolution is obtained. A 2D map within the membrane plane of about 6.1 A is used for modeling, structure model comparison with the PSI structure of Thermosynechococcus elongatus at 2.5 A, PDB ID 1JB0, overview. The PsaL subunit of strain TS-821 is modeled using PsaL subunit of Pisum sativum as a template, PDB ID 4Y28L. The modeled PsaL subunit of TS-821 is used to substitute the existing PsaL subunit in crystal structure of Thermosynechococcus elongatus and most of the subunits from the crystal structure of Thermosynechococcus elongatus are fitted separately into the 3D volumemap of TS-821. Comparison of trimeric interface of Thermosynechococcus elongatus with interface type 1 of TS-821
tetramer
in strain TS-821 PSI forms tetrameric, dimeric, and monomeric species, a tetrameric PSI has two PSI dimers associated together with interdimer gaps, while the PSI dimer is composed of two tightly tethered PSI monomers, subunit organization, structure comparisons, overview
monomer
in strain TS-821 PSI forms tetrameric, dimeric, and monomeric species, a tetrameric PSI has two PSI dimers associated together with interdimer gaps, while the PSI dimer is composed of two tightly tethered PSI monomers, subunit organization, structure comparisons, overview
monomer
Thermosynechococcus vestitus
inside the trimer, subunits PsaL, PsaI and PsaM (5 alpha-helices in total) are located in the center of the trimerization domain of PSI, thereby forming most of the contacts between the monomers
trimer
cyanobacterial PSI is usually trimeric
trimer
cyanobacterial PSI is usually trimeric
trimer
three-dimensional structure analysis using PDB ID 1JB0, overview. Two transmembrane large protein subunits PsaA and PsaB compose C2-symmetrical heterodimeric core complex containing most of the electron transfer cofactors. The electron transfer chain of PS I consists of the primary donor-chlorophyll (Chl) dimer P700, primary acceptor A0 (four Chl molecules), A1 (two phylloquinone molecules), and iron-sulfur clusters FX, FA, and FB.The terminal FA/FB clusters are located on the small extrinsic PsaC subunit
trimer
Thermosynechococcus vestitus
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-
trimer
Thermosynechococcus vestitus
inside the trimer, subunits PsaL, PsaI and PsaM (5 alpha-helices in total) are located in the center of the trimerization domain of PSI, thereby forming most of the contacts between the monomers
additional information
-
plant and algal PSI complexes contain 14-15 protein subunits. Of these, only PsaA, PsaB, and PsaC bind the cofactors of the electron transfer system. PsaA and PsaB form the core complex around which other subunits are organized. The PsaC, PsaD, PsaH, and PsaE proteins form the stromal peripheral domain that contains the terminal electron donors and the ferredoxin-docking site. PsaN of plant and algal PSI is a lumenal peripheral protein. PsaN and the large lumenal domain of PsaF form the plastocyanin docking site of plant and algal PSI. The remaining proteins of PSI are integral membrane proteins with 13 transmembrane helices. The function of the PSI proteins
additional information
-
plant and algal PSI complexes contain 14-15 protein subunits. Of these, only PsaA, PsaB, and PsaC bind the cofactors of the electron transfer system. PsaA and PsaB form the core complex around which other subunits are organized. The PsaC, PsaD, PsaH, and PsaE proteins form the stromal peripheral domain that contains the terminal electron donors and the ferredoxin-docking site. PsaN of plant and algal PSI is a lumenal peripheral protein. PsaN and the large lumenal domain of PsaF form the plastocyanin docking site of plant and algal PSI. The remaining proteins of PSI are integral membrane proteins with 13 transmembrane helices. The function of the PSI proteins
additional information
amino acid sequence comparisons
additional information
the PSI core complex prepared from cucumber cotyledons contains 80 chlorophylls per reaction center (P700) and eight polypeptides with apparent molecular masses of 65/63, 20,19.5,18.5,17.5,7.6, and 5.8 kDa. The amount of 18.5 kDa polypeptide in the PSI complex affects the activity. When this polypeptide is largely depleted, the complex is almost inactive. The inactivation is due to inhibition of electron transfer from plastocyanin to photooxidized P700. Chemical cross-linking and N-terminal amino acid sequencing experiments indicate that the 18.5-kDa polypeptide is the plastocyanin-docking protein and the psaF gene product
additional information
-
the PSI core complex prepared from cucumber cotyledons contains 80 chlorophylls per reaction center (P700) and eight polypeptides with apparent molecular masses of 65/63, 20,19.5,18.5,17.5,7.6, and 5.8 kDa. The amount of 18.5 kDa polypeptide in the PSI complex affects the activity. When this polypeptide is largely depleted, the complex is almost inactive. The inactivation is due to inhibition of electron transfer from plastocyanin to photooxidized P700. Chemical cross-linking and N-terminal amino acid sequencing experiments indicate that the 18.5-kDa polypeptide is the plastocyanin-docking protein and the psaF gene product
additional information
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PsaE (a peripheral subunit of the PSI complex) is involved in the docking of ferredoxin/flavodoxin to the PSI complex and also participates in the cyclic electron transfer around phosphosystem I. The interactions formed between different subunits of the complex may be hydrophobic or electrostatic in nature
additional information
-
the photosystem I reaction center is obtained in two forms, monomeric and trimeric
additional information
the crystal structure reveals the configuration of PsaK, a core subunit important for state transitions in plants, a conserved network of water molecules surrounding the electron transfer centres and an elaborate structure of lipids bridging PSI and its LHCI antenna. The structure of Psak suggests alternative conformations, overview
additional information
-
the photosystem I reaction center complex is composed of the 83 kDa subunits A and B, and at least six other subunits with molecular mass below 20 kDa
additional information
-
a cyanobacterial PSI monomer consists of 1112 protein subunits
additional information
the membrane-embedded core of each PS I monomer is formed by the two largest subunits, PsaA and PsaB, which bind electron transport cofactors arranged in two symmetrical branches, A and B, extending from P700, a pair of chlorophyll a molecules located on the lumenal side, to the [4Fe-4S] cluster FX, placed on the opposite stromal side of the complex
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D612H/E613H
mutation in subunit PsaB of photosystem I. Photosystem I harboring the has a high affinity toward binding of the electron donors and possesses an altered pH dependence of electron transfer with plastocyanin and cytochrome c6. The mutant strain exhibits a strong light sensitive growth phenotype, indicating that decelerated turnover between plastocyanin/cytochrome c6 and photosystem I with respect to electron transfer is deleterious to the cells
F689N
site-directed mutagenesis of subunit PsaA, the mutation causes in an about 100fold decrease in the observed rate of cofactor phylloquinone PhQA- oxidation, resulting in a lifetime that exceeds that of the terminal electron donor, P700+. This situation allows a second photochemical charge separation event to be initiated before PhQA- has decayed, thereby mimicking in PSI a situation that occurs in type II reaction centers. Simulation of the pump-pump kinetics in PsaA-F689N, overview
N591L
site-directed mutagenesis of psaB, the mutant shows structural differences and altered activity compared to the wild-type enzyme, detailed overview
N604L
site-directed mutagenesis of psaA, the mutant shows structural differences and altered activity compared to the wild-type enzyme, detailed overview
F689N
-
site-directed mutagenesis of subunit PsaA, the mutation causes in an about 100fold decrease in the observed rate of cofactor phylloquinone PhQA- oxidation, resulting in a lifetime that exceeds that of the terminal electron donor, P700+. This situation allows a second photochemical charge separation event to be initiated before PhQA- has decayed, thereby mimicking in PSI a situation that occurs in type II reaction centers. Simulation of the pump-pump kinetics in PsaA-F689N, overview
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F647C
-
mutant strain cannot grow under photoautotrophic conditions because of low photosystem I activity, possibly due to low levels of proteins
F649C/G650I
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mutant strain cannot grow under photoautotrophic conditions because of low photosystem I activity, possibly due to low levels of proteins
H651C/L652M
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mutant strain cannot grow under photoautotrophic conditions because of low photosystem I activity, possibly due to low levels of proteins
S641C/V642I
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mutation in subunit PsaB. Mutant strain grows photoautotrophically and shows no obvious reduction in the photosystem I activity. Kinetics of P700 re-reduction by plastocyanin remains unaltered
W643C/A644I
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mutation in subunit PsaB. Mutant strain grows photoautotrophically and shows no obvious reduction in the photosystem I activity. Kinetics of P700 re-reduction by plastocyanin remains unaltered
W645C
-
mutation in subunit PsaB. Mutant strain grows photoautotrophically and shows no obvious reduction in the photosystem I activity. Kinetics of P700 re-reduction by plastocyanin remains unaltered
N591L
site-directed mutagenesis of psaB, the mutant shows structural differences and altered activity compared to the wild-type enzyme, detailed overview
N604L
site-directed mutagenesis of psaA, the mutant shows structural differences and altered activity compared to the wild-type enzyme, detailed overview
additional information
-
generation of Arabidopsis thaliana whirly1 knockout (kowhy1) and plastid-localized WHIRLY1 overexpression (oepWHY1) plants. The WHY1 knockout line (kowhy1) has a T-DNA insertion in exon1. Loss of WHIRLY1 leads to a higher photochemical quantum yield of photosystem I Y(I) and electron transport rate and a lower non-photochemical quenching involved in the thermal dissipation of excitation energy of chlorophyll fluorescence than the wild-type. Higher Y(I) in kowhy1 mutant demonstrates an elevated redox rate of P700 caused by the lack of WHY1 at an early stage of leaf senescence. Under high light conditions, both kowhy1 and ko1/3 plants show lower electron transport rate than wild-type which are contrary to that under normal light condition. Moreover, the expression of several PSI-NDH encoding genes and ERF109, which is related to jasmonate response, varies in kowhy1 under different light conditions. Mutation of WHY1 leads to the increased expression level of ERF109 and ERF13 compared to wild-type plants in response to high light treatment. ERF13 is a CE1 (coupling element 1) binding protein and confers ABA hypersensitivity in Arabidopsis thaliana
additional information
-
generation of Arabidopsis thaliana whirly1 knockout (kowhy1) and plastid-localized WHIRLY1 overexpression (oepWHY1) plants. The WHY1 knockout line (kowhy1) has a T-DNA insertion in exon1. Loss of WHIRLY1 leads to a higher photochemical quantum yield of photosystem I Y(I) and electron transport rate and a lower non-photochemical quenching involved in the thermal dissipation of excitation energy of chlorophyll fluorescence than the wild-type. Higher Y(I) in kowhy1 mutant demonstrates an elevated redox rate of P700 caused by the lack of WHY1 at an early stage of leaf senescence. Under high light conditions, both kowhy1 and ko1/3 plants show lower electron transport rate than wild-type which are contrary to that under normal light condition. Moreover, the expression of several PSI-NDH encoding genes and ERF109, which is related to jasmonate response, varies in kowhy1 under different light conditions. Mutation of WHY1 leads to the increased expression level of ERF109 and ERF13 compared to wild-type plants in response to high light treatment. ERF13 is a CE1 (coupling element 1) binding protein and confers ABA hypersensitivity in Arabidopsis thaliana
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additional information
-
generation of the rice mutant defective in the OsCRR6 gene by the Tos17 retrotransposon insertion
additional information
-
molecular analysis of spontaneous revertants from the mutants H651C/L652M, F649C/G650I and F647C suggests that an aromatic residue at F647 and a small residue at G650 may be necessary for maintaining the structural integrity of photosystem I
additional information
the menB deletion strain carries a mutation in the PhQ biosynthetic pathway, charge recombination kinetics in the PS I complexes from menB mutant, which binds either PQ or Cl2NQ instead of the native PhQ in the A1 binding site of the wild-type PS I, overview
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Ben-Shem, A.; Nelson, N.; Frolow, F.
Crystallization and initial X-ray diffraction studies of higher plant photosystem I
Acta Crystallogr. Sect. D
59
1824-1827
2003
Pisum sativum
brenda
Chitnis, P.R.
Photosystem I: function and physiology
Annu. Rev. Plant Physiol. Plant Mol. Biol.
52
593-626
2001
Synechocystis sp., Arabidopsis thaliana, Chlamydomonas reinhardtii
brenda
van Thor, J.J.; Geerlings, T.H.; Matthijs, H.C.; Hellingwerf, K.J.
Kinetic evidence for the PsaE-dependent transient ternary complex photosystem I/ferredoxin/ferredoxin:NADP+ reductase in a cyanobacterium
Biochemistry
38
12735-12746
1999
Synechocystis sp.
brenda
Lakshmi, K.V.; Jung, Y.S.; Golbeck, J.H.; Brudvig, G.W.
Location of the iron-sulfur clusters FA and FB in photosystem I: an electron paramagnetic resonance study of spin relaxation enhancement of P700+
Biochemistry
38
13210-13215
1999
Synechococcus sp.
brenda
Lushy, A.; Verchovsky, L.; Nechushtai, R.
The stable assembly of newly synthesized PsaE into the photosystem I complex occurring via the exchange mechanism is facilitated by electrostatic interactions
Biochemistry
41
11192-11199
2002
Mastigocladus laminosus
brenda
Bttcher, B.; Grber, P.; Boekema, E.J.
The structure of photosystem I from the thermophilic cyanobacterium Synechococcus sp. determined by electron microscopy of two-dimensional crystals
Biochim. Biophys. Acta
1100
125-136
1992
Synechococcus sp.
brenda
Jansson, H.; Hansson, O.
Competitive inhibition of electron donation to photosystem 1 by metal-substituted plastocyanin
Biochim. Biophys. Acta
1777
1116-1121
2008
Spinacia oleracea
brenda
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