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Literature summary extracted from

  • Badshah, S.; Sun, J.; Mula, S.; Gorka, M.; Baker, P.; Luthra, R.; Lin, S.; van der Est, A.; Golbeck, J.; Redding, K.
    Mutations in algal and cyanobacterial photosystem I that independently affect the yield of initial charge separation in the two electron transfer cofactor branches (2018), Biochim. Biophys. Acta, 1859, 42-55 .
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.97.1.12 N591L site-directed mutagenesis of psaB, the mutant shows structural differences and altered activity compared to the wild-type enzyme, detailed overview Synechocystis sp. PCC 6803
1.97.1.12 N591L site-directed mutagenesis of psaB, the mutant shows structural differences and altered activity compared to the wild-type enzyme, detailed overview Chlamydomonas reinhardtii
1.97.1.12 N604L site-directed mutagenesis of psaA, the mutant shows structural differences and altered activity compared to the wild-type enzyme, detailed overview Synechocystis sp. PCC 6803
1.97.1.12 N604L site-directed mutagenesis of psaA, the mutant shows structural differences and altered activity compared to the wild-type enzyme, detailed overview Chlamydomonas reinhardtii

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.97.1.12 thylakoid
-
Synechocystis sp. PCC 6803 9579
-
1.97.1.12 thylakoid
-
Chlamydomonas reinhardtii 9579
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.97.1.12 reduced plastocyanin + oxidized ferredoxin + hv Synechocystis sp. PCC 6803
-
oxidized plastocyanin + reduced ferredoxin
-
?
1.97.1.12 reduced plastocyanin + oxidized ferredoxin + hv Chlamydomonas reinhardtii
-
oxidized plastocyanin + reduced ferredoxin
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.97.1.12 Chlamydomonas reinhardtii P12154 AND P09144 AND Q00914 psaA, psaB, and psaC
-
1.97.1.12 Synechocystis sp. PCC 6803 P29254 AND P29255 AND P32422 psaA, psaB, and psaC
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.97.1.12 recombinant His6-tagged enzyme from thylakoid membranes by nickel affinity chromatography and ultrafiltration Chlamydomonas reinhardtii

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.97.1.12 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+) Synechocystis sp. PCC 6803 ?
-
?
1.97.1.12 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+) Chlamydomonas reinhardtii ?
-
?
1.97.1.12 reduced plastocyanin + oxidized ferredoxin + hv
-
Synechocystis sp. PCC 6803 oxidized plastocyanin + reduced ferredoxin
-
?
1.97.1.12 reduced plastocyanin + oxidized ferredoxin + hv
-
Chlamydomonas reinhardtii oxidized plastocyanin + reduced ferredoxin
-
?

Subunits

EC Number Subunits Comment Organism
1.97.1.12 trimer cyanobacterial PSI is usually trimeric Synechocystis sp. PCC 6803
1.97.1.12 trimer cyanobacterial PSI is usually trimeric Chlamydomonas reinhardtii

Synonyms

EC Number Synonyms Comment Organism
1.97.1.12 PSI
-
Synechocystis sp. PCC 6803
1.97.1.12 PSI
-
Chlamydomonas reinhardtii

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.97.1.12 22
-
assay at room temperature Synechocystis sp. PCC 6803
1.97.1.12 22
-
assay at room temperature Chlamydomonas reinhardtii

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.97.1.12 7.5
-
assay at Synechocystis sp. PCC 6803
1.97.1.12 7.5
-
assay at Chlamydomonas reinhardtii

Cofactor

EC Number Cofactor Comment Organism Structure
1.97.1.12 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 Synechocystis sp. PCC 6803
1.97.1.12 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 Chlamydomonas reinhardtii
1.97.1.12 phylloquinone
-
Synechocystis sp. PCC 6803
1.97.1.12 phylloquinone
-
Chlamydomonas reinhardtii

General Information

EC Number General Information Comment Organism
1.97.1.12 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 Synechocystis sp. PCC 6803
1.97.1.12 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 Chlamydomonas reinhardtii
1.97.1.12 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 Synechocystis sp. PCC 6803
1.97.1.12 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 Chlamydomonas reinhardtii
1.97.1.12 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 Synechocystis sp. PCC 6803
1.97.1.12 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 Chlamydomonas reinhardtii