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Literature summary for 1.97.1.12 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

Protein Variants Comment Organism
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
N591L site-directed mutagenesis of psaB, the mutant shows structural differences and altered activity compared to the wild-type enzyme, detailed overview Chlamydomonas reinhardtii
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
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

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

Natural Substrates/ Products (Substrates)

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

Organism

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

Purification (Commentary)

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

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

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

Temperature Optimum [°C]

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

pH Optimum

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

Cofactor

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

General Information

General Information Comment Organism
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
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
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
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
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
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