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Literature summary for 3.4.21.102 extracted from
- Environment of TyrZ in photosystem II from Thermosynechococcus elongatus in which PsbA2 is the D1 protein (2012), J. Biol. Chem., 287, 13336-13347.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Thermosynechococcus vestitus | P0A446 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | the geometry of the TyrZ phenol group and its environment, likely the Tyr-O-H-Nepsilon-His bonding, are modified in isoform PsbA2-PSII when compared with isoforms PsbA(1/3)-PSII. They also point to the dynamics of the proton-coupled electron transfer processes associated with the oxidation of TyrZ being affected. The C144P and P173M substitutions in isoform PsbA2-PSII versus PsbA(1/3)-PSII, respectively located upstream of the alpha-helix bearing TyrZ and between the two alpha-helices bearing TyrZ and its hydrogen-bonded partner, His-190, are responsible for these changes | Thermosynechococcus vestitus | ? | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| photosystem II protein D1 2 | - |
Thermosynechococcus vestitus |
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Release 2023.1 (January 2023)
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