Aromatic structure of Tyrosine-92 in the extrinsic PsbU protein of red algal Photosystem II is important for its functioning

Akinori Okumura, Masanori Sano, Takehiro Suzuki, Hiroyasu Tanaka, Ryo Nagao, Katsuyoshi Nakazato, Masako Iwai, Hideyuki Adachi, Jian Ren Shen, Isao Enami

    Research output: Contribution to journalArticlepeer-review

    6 Citations (Scopus)

    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 languageEnglish
    Pages (from-to)5255-5258
    Number of pages4
    JournalFEBS Letters
    Volume581
    Issue number27
    DOIs
    Publication statusPublished - 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

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