Proton-coupled electron-transfer processes in photosystem II probed by highly resolved g -anisotropy of redox-active tyrosine YZ

Hideto Matsuoka, Jian Ren Shen, Asako Kawamori, Kei Nishiyama, Yasunori Ohba, Seigo Yamauchi

研究成果: Article査読

22 被引用数 (Scopus)

抄録

The oxidation of a redox-active tyrosine residue YZ in photosystem II (PSII) is coupled with proton transfer to a hydrogen-bonded D1-His190 residue. Because of the apparent proximity of YZ to the water-oxidizing complex and its redox activity, it is believed that Y Z plays a significant role in water oxidation in PSII. We investigated the g-anisotropy of the tyrosine radical YZ• to provide insight into the mechanism of YZ• proton-coupled electron transfer in Mn-depleted PSII. The anisotropy was highly resolved by electron paramagnetic resonance spectroscopy at the W-band (94.9 GHz) using PSII single crystals. The gX-component along the phenolic C-O bond of YZ• was calculated by density functional theory (DFT). It was concluded from the highly resolved g-anisotropy that YZ loses a phenol proton to D1-His190 upon tyrosine oxidation, and D1-His190 redonates the same proton back to YZ• upon reduction.

本文言語English
ページ(範囲)4655-4660
ページ数6
ジャーナルJournal of the American Chemical Society
133
12
DOI
出版ステータスPublished - 2011 3月 30

ASJC Scopus subject areas

  • 触媒
  • 化学 (全般)
  • 生化学
  • コロイド化学および表面化学

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