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Literature summary for 1.97.1.12 extracted from
- Photosystem I: function and physiology (2001), Annu. Rev. Plant Physiol. Plant Mol. Biol., 52, 593-626.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
- |
Chlamydomonas reinhardtii |
- |
Arabidopsis thaliana |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| reduced plastocyanin + oxidized ferredoxin + hv | Chlamydomonas reinhardtii | - |
oxidized plastocyanin + reduced ferredoxin | - |
? |  |
| reduced plastocyanin + oxidized ferredoxin + hv | Arabidopsis thaliana | - |
oxidized plastocyanin + reduced ferredoxin | - |
? | |
| reduced plastocyanin + oxidized ferredoxin + hv | Synechocystis sp. | - |
oxidized plastocyanin + reduced ferredoxin | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Arabidopsis thaliana | - |
- |
- |
| Chlamydomonas reinhardtii | - |
- |
- |
| Synechocystis sp. | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| reduced plastocyanin + oxidized ferredoxin + hv | - |
Chlamydomonas reinhardtii | oxidized plastocyanin + reduced ferredoxin | - |
? | |
| reduced plastocyanin + oxidized ferredoxin + hv | - |
Arabidopsis thaliana | oxidized plastocyanin + reduced ferredoxin | - |
? | |
| reduced plastocyanin + oxidized ferredoxin + hv | - |
Synechocystis sp. | oxidized plastocyanin + reduced ferredoxin | - |
? | |
| 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 | Chlamydomonas reinhardtii | oxidized plastocyanin + reduced ferredoxin | - |
? | |
| 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 | Arabidopsis thaliana | oxidized plastocyanin + reduced ferredoxin | - |
? | |
| 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 | Synechocystis sp. | oxidized plastocyanin + reduced ferredoxin | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | a cyanobacterial PSI monomer consists of 1112 protein subunits | Synechocystis sp. |
| 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 |
| 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 |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| PSI | - |
Chlamydomonas reinhardtii |
| PSI | - |
Arabidopsis thaliana |
| PSI | - |
Synechocystis sp. |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| beta-carotene | - |
Chlamydomonas reinhardtii | |
| beta-carotene | - |
Arabidopsis thaliana | |
| beta-carotene | cyanobacterial PSI complexes contain 22 molecules of beta-carotene, 17 of which are in all-trans configuration | Synechocystis sp. | |
| chlorophyll a | most abundant cofactor in PSI, role of these molecules in light absorption, charge separation, electron transfer, and biogenesis | Chlamydomonas reinhardtii | |
| chlorophyll a | most abundant cofactor in PSI, role of these molecules in light absorption, charge separation, electron transfer, and biogenesis | Arabidopsis thaliana | |
| chlorophyll a | most abundant cofactor in PSI, role of these molecules in light absorption, charge separation, electron transfer, and biogenesis | Synechocystis sp. | |
| chlorophyll a' | one member of the P700 special pair is a chlorophyll a' molecule | Chlamydomonas reinhardtii | |
| chlorophyll a' | one member of the P700 special pair is a chlorophyll a' molecule | Arabidopsis thaliana | |
| chlorophyll a' | one member of the P700 special pair is a chlorophyll a' molecule | Synechocystis sp. | |
| iron-sulfur centre | a PSI complex contains 12 iron atoms that constitute 3 [4Fe-4S] clusters | Chlamydomonas reinhardtii | |
| iron-sulfur centre | a PSI complex contains 12 iron atoms that constitute 3 [4Fe-4S] clusters | Arabidopsis thaliana | |
| iron-sulfur centre | a PSI complex contains 12 iron atoms that constitute 3 [4Fe-4S] clusters | Synechocystis sp. | |
| 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 | |
| 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 | |
| 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. | |
| 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 | |
| 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 | |
| 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. | |
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