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Aromatic structure of tyrosine-92 in the extrinsic PsbU protein of red algal photosystem II is important for its functioning.

Authors
  • Okumura, Akinori
  • Sano, Masanori
  • Suzuki, Takehiro
  • Tanaka, Hiroyasu
  • Nagao, Ryo
  • Nakazato, Katsuyoshi
  • Iwai, Masako
  • Adachi, Hideyuki
  • Shen, Jian-Ren
  • Enami, Isao
Type
Published Article
Journal
FEBS Letters
Publisher
Wiley (John Wiley & Sons)
Publication Date
Nov 13, 2007
Volume
581
Issue
27
Pages
5255–5258
Identifiers
PMID: 17950730
Source
Medline
License
Unknown

Abstract

PsbU is one of the extrinsic proteins in red algal Photosystem II (PSII) and functions to optimize the availability of Ca(2+) 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/pi interaction is important for the optimal function of the Mn(4)Ca-cluster.

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