BRENDA - Enzyme Database show

Photosystem I: function and physiology

Chitnis, P.R.; Annu. Rev. Plant Physiol. Plant Mol. Biol. 52, 593-626 (2001)

Data extracted from this reference:

Crystallization (Commentary)
EC Number
Crystallization
Organism
1.97.1.12
-
Arabidopsis thaliana
1.97.1.12
-
Chlamydomonas reinhardtii
Localization
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
Natural Substrates/ Products (Substrates)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
1.97.1.12
reduced plastocyanin + oxidized ferredoxin + hv
Chlamydomonas reinhardtii
-
oxidized plastocyanin + reduced ferredoxin
-
-
?
1.97.1.12
reduced plastocyanin + oxidized ferredoxin + hv
Arabidopsis thaliana
-
oxidized plastocyanin + reduced ferredoxin
-
-
?
1.97.1.12
reduced plastocyanin + oxidized ferredoxin + hv
Synechocystis sp.
-
oxidized plastocyanin + reduced ferredoxin
-
-
?
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
1.97.1.12
Arabidopsis thaliana
-
-
-
1.97.1.12
Chlamydomonas reinhardtii
-
-
-
1.97.1.12
Synechocystis sp.
-
-
-
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.97.1.12
reduced plastocyanin + oxidized ferredoxin + hv
-
710876
Chlamydomonas reinhardtii
oxidized plastocyanin + reduced ferredoxin
-
-
-
?
1.97.1.12
reduced plastocyanin + oxidized ferredoxin + hv
-
710876
Arabidopsis thaliana
oxidized plastocyanin + reduced ferredoxin
-
-
-
?
1.97.1.12
reduced plastocyanin + oxidized ferredoxin + hv
-
710876
Synechocystis sp.
oxidized plastocyanin + reduced ferredoxin
-
-
-
?
1.97.1.12
reduced plastocyanin + oxidized ferredoxin + hv
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
710876
Chlamydomonas reinhardtii
oxidized plastocyanin + reduced ferredoxin
-
-
-
?
1.97.1.12
reduced plastocyanin + oxidized ferredoxin + hv
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
710876
Arabidopsis thaliana
oxidized plastocyanin + reduced ferredoxin
-
-
-
?
1.97.1.12
reduced plastocyanin + oxidized ferredoxin + hv
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
710876
Synechocystis sp.
oxidized plastocyanin + reduced ferredoxin
-
-
-
?
Subunits
EC Number
Subunits
Commentary
Organism
1.97.1.12
More
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
Arabidopsis thaliana
1.97.1.12
More
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
Chlamydomonas reinhardtii
1.97.1.12
More
a cyanobacterial PSI monomer consists of 1112 protein subunits
Synechocystis sp.
Cofactor
EC Number
Cofactor
Commentary
Organism
Structure
1.97.1.12
beta-carotene
-
Arabidopsis thaliana
1.97.1.12
beta-carotene
-
Chlamydomonas reinhardtii
1.97.1.12
beta-carotene
cyanobacterial PSI complexes contain 22 molecules of beta-carotene, 17 of which are in all-trans configuration
Synechocystis sp.
1.97.1.12
chlorophyll a
most abundant cofactor in PSI, role of these molecules in light absorption, charge separation, electron transfer, and biogenesis
Arabidopsis thaliana
1.97.1.12
chlorophyll a
most abundant cofactor in PSI, role of these molecules in light absorption, charge separation, electron transfer, and biogenesis
Chlamydomonas reinhardtii
1.97.1.12
chlorophyll a
most abundant cofactor in PSI, role of these molecules in light absorption, charge separation, electron transfer, and biogenesis
Synechocystis sp.
1.97.1.12
chlorophyll a'
one member of the P700 special pair is a chlorophyll a' molecule
Arabidopsis thaliana
1.97.1.12
chlorophyll a'
one member of the P700 special pair is a chlorophyll a' molecule
Chlamydomonas reinhardtii
1.97.1.12
chlorophyll a'
one member of the P700 special pair is a chlorophyll a' molecule
Synechocystis sp.
1.97.1.12
iron-sulfur centre
a PSI complex contains 12 iron atoms that constitute 3 [4Fe-4S] clusters
Arabidopsis thaliana
1.97.1.12
iron-sulfur centre
a PSI complex contains 12 iron atoms that constitute 3 [4Fe-4S] clusters
Chlamydomonas reinhardtii
1.97.1.12
iron-sulfur centre
a PSI complex contains 12 iron atoms that constitute 3 [4Fe-4S] clusters
Synechocystis sp.
1.97.1.12
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
Arabidopsis thaliana
1.97.1.12
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
Chlamydomonas reinhardtii
1.97.1.12
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
Synechocystis sp.
1.97.1.12
phylloquinone
the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
Arabidopsis thaliana
1.97.1.12
phylloquinone
the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
Chlamydomonas reinhardtii
1.97.1.12
phylloquinone
the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
Synechocystis sp.
Cofactor (protein specific)
EC Number
Cofactor
Commentary
Organism
Structure
1.97.1.12
beta-carotene
-
Arabidopsis thaliana
1.97.1.12
beta-carotene
-
Chlamydomonas reinhardtii
1.97.1.12
beta-carotene
cyanobacterial PSI complexes contain 22 molecules of beta-carotene, 17 of which are in all-trans configuration
Synechocystis sp.
1.97.1.12
chlorophyll a
most abundant cofactor in PSI, role of these molecules in light absorption, charge separation, electron transfer, and biogenesis
Arabidopsis thaliana
1.97.1.12
chlorophyll a
most abundant cofactor in PSI, role of these molecules in light absorption, charge separation, electron transfer, and biogenesis
Chlamydomonas reinhardtii
1.97.1.12
chlorophyll a
most abundant cofactor in PSI, role of these molecules in light absorption, charge separation, electron transfer, and biogenesis
Synechocystis sp.
1.97.1.12
chlorophyll a'
one member of the P700 special pair is a chlorophyll a' molecule
Arabidopsis thaliana
1.97.1.12
chlorophyll a'
one member of the P700 special pair is a chlorophyll a' molecule
Chlamydomonas reinhardtii
1.97.1.12
chlorophyll a'
one member of the P700 special pair is a chlorophyll a' molecule
Synechocystis sp.
1.97.1.12
iron-sulfur centre
a PSI complex contains 12 iron atoms that constitute 3 [4Fe-4S] clusters
Arabidopsis thaliana
1.97.1.12
iron-sulfur centre
a PSI complex contains 12 iron atoms that constitute 3 [4Fe-4S] clusters
Chlamydomonas reinhardtii
1.97.1.12
iron-sulfur centre
a PSI complex contains 12 iron atoms that constitute 3 [4Fe-4S] clusters
Synechocystis sp.
1.97.1.12
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
Arabidopsis thaliana
1.97.1.12
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
Chlamydomonas reinhardtii
1.97.1.12
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
Synechocystis sp.
1.97.1.12
phylloquinone
the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
Arabidopsis thaliana
1.97.1.12
phylloquinone
the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
Chlamydomonas reinhardtii
1.97.1.12
phylloquinone
the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
Synechocystis sp.
Crystallization (Commentary) (protein specific)
EC Number
Crystallization
Organism
1.97.1.12
-
Arabidopsis thaliana
1.97.1.12
-
Chlamydomonas reinhardtii
Localization (protein specific)
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
Natural Substrates/ Products (Substrates) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
1.97.1.12
reduced plastocyanin + oxidized ferredoxin + hv
Chlamydomonas reinhardtii
-
oxidized plastocyanin + reduced ferredoxin
-
-
?
1.97.1.12
reduced plastocyanin + oxidized ferredoxin + hv
Arabidopsis thaliana
-
oxidized plastocyanin + reduced ferredoxin
-
-
?
1.97.1.12
reduced plastocyanin + oxidized ferredoxin + hv
Synechocystis sp.
-
oxidized plastocyanin + reduced ferredoxin
-
-
?
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.97.1.12
reduced plastocyanin + oxidized ferredoxin + hv
-
710876
Chlamydomonas reinhardtii
oxidized plastocyanin + reduced ferredoxin
-
-
-
?
1.97.1.12
reduced plastocyanin + oxidized ferredoxin + hv
-
710876
Arabidopsis thaliana
oxidized plastocyanin + reduced ferredoxin
-
-
-
?
1.97.1.12
reduced plastocyanin + oxidized ferredoxin + hv
-
710876
Synechocystis sp.
oxidized plastocyanin + reduced ferredoxin
-
-
-
?
1.97.1.12
reduced plastocyanin + oxidized ferredoxin + hv
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
710876
Chlamydomonas reinhardtii
oxidized plastocyanin + reduced ferredoxin
-
-
-
?
1.97.1.12
reduced plastocyanin + oxidized ferredoxin + hv
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
710876
Arabidopsis thaliana
oxidized plastocyanin + reduced ferredoxin
-
-
-
?
1.97.1.12
reduced plastocyanin + oxidized ferredoxin + hv
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
710876
Synechocystis sp.
oxidized plastocyanin + reduced ferredoxin
-
-
-
?
Subunits (protein specific)
EC Number
Subunits
Commentary
Organism
1.97.1.12
More
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
Arabidopsis thaliana
1.97.1.12
More
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
Chlamydomonas reinhardtii
1.97.1.12
More
a cyanobacterial PSI monomer consists of 1112 protein subunits
Synechocystis sp.