1.97.1.12: photosystem I
This is an abbreviated version!
For detailed information about photosystem I, go to the full flat file.
Word Map on EC 1.97.1.12
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1.97.1.12
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photosystems
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chlorophyl
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thylakoids
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chloroplast
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light-harvesting
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cyanobacterium
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antenna
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spinach
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synechocystis
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synechococcus
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chlamydomonas
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photochemical
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photoinhibition
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plastoquinone
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light-induced
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ferredoxins
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reinhardtii
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photoautotrophic
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non-photochemical
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methylviologen
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pump-probe
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phycobilisomes
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thermoluminescence
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supercomplexes
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pigment-protein
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chlorophyll-proteins
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photooxidation
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oxygen-evolving
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lhcii
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photocurrent
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3-3,4-dichlorophenyl-1,1-dimethylurea
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grana
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water-splitting
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intersystem
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photoprotection
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phylloquinone
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excitonic
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light-driven
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photoreduced
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photoinhibitory
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photoreduction
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thermosynechococcus
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far-red
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picosecond
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flash-induced
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violaxanthin
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electrochromic
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photophosphorylation
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elongatus
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photochemistry
- 1.97.1.12
- photosystems
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chlorophyl
- thylakoids
- chloroplast
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light-harvesting
- cyanobacterium
- antenna
- spinach
- synechocystis
- synechococcus
- chlamydomonas
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photochemical
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photoinhibition
- plastoquinone
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light-induced
- ferredoxins
- reinhardtii
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photoautotrophic
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non-photochemical
- methylviologen
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pump-probe
- phycobilisomes
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thermoluminescence
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supercomplexes
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pigment-protein
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chlorophyll-proteins
- photooxidation
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oxygen-evolving
- lhcii
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photocurrent
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3-3,4-dichlorophenyl-1,1-dimethylurea
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grana
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water-splitting
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intersystem
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photoprotection
- phylloquinone
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excitonic
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light-driven
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photoreduced
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photoinhibitory
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photoreduction
- thermosynechococcus
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far-red
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picosecond
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flash-induced
- violaxanthin
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electrochromic
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photophosphorylation
- elongatus
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photochemistry
Reaction
Synonyms
OsCRR6, photosystem I P700 chlorophyll a apoprotein A2, PS I, PS-I, PS-I complex, PsaB, PsaF, PSI, PSI core complex
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Cofactor
Cofactor on EC 1.97.1.12 - photosystem I
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2,3-dichloronaphthoquinone
in the mutant menB deletion strain
beta-carotene
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cyanobacterial PSI complexes contain 22 molecules of beta-carotene, 17 of which are in all-trans configuration
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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
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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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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
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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'
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one member of the P700 special pair is a chlorophyll a' molecule
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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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
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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
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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
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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
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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
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the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
phylloquinone
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the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
phylloquinone
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the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
plastoquinone
in the mutant menB deletion strain
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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
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the enzyme contains three [4Fe-4S] clusters: FA, FB and FX
[4Fe-4S]-center
Thermosynechococcus vestitus
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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
[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
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
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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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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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