Abstract
PsbU is one of the extrinsic proteins in red algal Photosystem II (PSII) and functions to optimize the availability of Ca2+ and Cl- cofactors for water oxidation. To determine the functional residue of PsbU, we constructed various PsbU mutants from a red alga Cyanidium caldarium and reconstituted these mutants with the red algal PSII. The results revealed that Tyr-92 of PsbU, especially its aromatic ring, was essential for maintaining its function. From the crystal structure of PSII, Tyr-92 is located close to Pro-340 of D1, suggesting that the aromatic ring of Tyr-92 interacts with the CH group of Pro-340 of D1, and this CH/π interaction is important for the optimal function of the Mn4Ca-cluster.
Original language | English |
---|---|
Pages (from-to) | 5255-5258 |
Number of pages | 4 |
Journal | FEBS Letters |
Volume | 581 |
Issue number | 27 |
DOIs | |
Publication status | Published - Nov 13 2007 |
Keywords
- Extrinsic protein
- Oxygen evolution
- Photosystem II
- PsbU
- Red algae
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology