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Literature summary for 1.97.1.12 extracted from
- Interaction of various types of photosystem I complexes with exogenous electron acceptors (2017), Photosynth. Res., 133, 175-184 .
No PubMed abstract available
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| 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 | Synechocystis sp. PCC 6803 |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| reduced cytochrome c6 + oxidized ferredoxin + hv | Synechocystis sp. PCC 6803 | - |
oxidized cytochrome c6 + reduced ferredoxin | - |
? |  |
| reduced cytochrome c6 + oxidized flavodoxin + hv | Synechocystis sp. PCC 6803 | - |
oxidized cytochrome c6 + reduced flavodoxin | - |
? | |
| reduced plastocyanin + oxidized ferredoxin + hv | Synechocystis sp. PCC 6803 | - |
oxidized plastocyanin + reduced ferredoxin | - |
? | |
| reduced plastocyanin + oxidized flavodoxin + hv | Synechocystis sp. PCC 6803 | - |
oxidized plastocyanin + reduced flavodoxin | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Synechocystis sp. PCC 6803 | P29254 AND P29255 AND P32422 | psaA, psaB, and psaC | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | 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 | Synechocystis sp. PCC 6803 | ? | - |
? | |
| reduced cytochrome c6 + oxidized ferredoxin + hv | - |
Synechocystis sp. PCC 6803 | oxidized cytochrome c6 + reduced ferredoxin | - |
? | |
| reduced cytochrome c6 + oxidized flavodoxin + hv | - |
Synechocystis sp. PCC 6803 | oxidized cytochrome c6 + reduced flavodoxin | - |
? | |
| reduced plastocyanin + oxidized ferredoxin + hv | - |
Synechocystis sp. PCC 6803 | oxidized plastocyanin + reduced ferredoxin | - |
? | |
| reduced plastocyanin + oxidized flavodoxin + hv | - |
Synechocystis sp. PCC 6803 | oxidized plastocyanin + reduced flavodoxin | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| 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 | Synechocystis sp. PCC 6803 |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| PS I | - |
Synechocystis sp. PCC 6803 |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 22 | - |
assay at room temperature | Synechocystis sp. PCC 6803 |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
assay at | Synechocystis sp. PCC 6803 |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| 2,3-dichloronaphthoquinone | in the mutant menB deletion strain | Synechocystis sp. PCC 6803 | |
| 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 | Synechocystis sp. PCC 6803 | |
| phylloquinone | in the wild-type strain | Synechocystis sp. PCC 6803 | |
| plastoquinone | in the mutant menB deletion strain | Synechocystis sp. PCC 6803 | |
| [4Fe-4S]-center | the enzyme contains [4Fe-4S] clusters | Synechocystis sp. PCC 6803 | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| 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 | Synechocystis sp. PCC 6803 |
| 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 | Synechocystis sp. PCC 6803 |
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Release 2023.1 (January 2023)
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