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  1. B100 理学部/理学研究科
  2. B100a 雑誌掲載論文
  3. 学術雑誌

D1-Asn-298 in photosystem II is involved in a hydrogen-bond network near the redox-active tyrosine YZ for proton exit during water oxidation

http://hdl.handle.net/2237/00027915
5a17b8e8-eb02-4a14-a119-4edc9572b8fe
名前 / ファイル ライセンス アクション
J_BiolChem-2017-Nagao-20046-57.pdf J_BiolChem-2017-Nagao-20046-57 (1.7 MB)
Item type 学術雑誌論文 / Journal Article(1)
公開日 2018-04-17
タイトル
タイトル D1-Asn-298 in photosystem II is involved in a hydrogen-bond network near the redox-active tyrosine YZ for proton exit during water oxidation
著者 Nagao, Ryo

× Nagao, Ryo

WEKO 76141

Nagao, Ryo

Search repository
Ueoka-Nakanishi, Hanayo

× Ueoka-Nakanishi, Hanayo

WEKO 76142

Ueoka-Nakanishi, Hanayo

Search repository
Noguchi, Takumi

× Noguchi, Takumi

WEKO 76143

Noguchi, Takumi

Search repository
権利
権利情報 This research was originally published in the Journal of Biological Chemistry. Ryo Nagao, Hanayo Ueoka-Nakanishi, and Takumi Noguchi. D1-Asn-298 in photosystem II is involved in a hydrogen-bond network near the redox-active tyrosine YZ for proton exit during water oxidation. J. Biol. Chem. 2017; 292:200046-20057. © the American Society for Biochemistry and Molecular Biology or © the Author(s).
キーワード
主題Scheme Other
主題 cyanobacteria
キーワード
主題Scheme Other
主題 Fourier transform IR (FTIR)
キーワード
主題Scheme Other
主題 photosynthesis
キーワード
主題Scheme Other
主題 photosystem II
キーワード
主題Scheme Other
主題 site-directed mutagenesis
キーワード
主題Scheme Other
主題 D1-Asn298
キーワード
主題Scheme Other
主題 YZ
キーワード
主題Scheme Other
主題 proton trasfer
キーワード
主題Scheme Other
主題 thermoluminescence
キーワード
主題Scheme Other
主題 water oxidation
抄録
内容記述 In photosynthetic water oxidation, two water molecules are converted into one oxygen molecule and four protons at the Mn4CaO5 cluster in photosystem II (PSII) via the S-state cycle. Efficient proton exit from the catalytic site to the lumen is essential for this process. However, the exit pathways of individual protons through the PSII proteins remain to be identified. In this study, we examined the involvement of a hydrogen-bond network near the redox-active tyrosine YZ in proton transfer during the S-state cycle. We focused on spectroscopic analyses of a site-directed variant of D1-Asn-298, a residue involved in a hydrogen-bond network near YZ. We found that the D1-N298A mutant of Synechocystis sp. PCC 6803 exhibits an O2 evolution activity of ∼10% of the wild-type. D1-N298A and the wild-type D1 had very similar features of thermoluminescence glow curves and of an FTIR difference spectrum upon YZ oxidation, suggesting that the hydrogen-bonded structure of YZ and electron transfer from the Mn4CaO5 cluster to YZ were little affected by substitution. In the D1-N298A mutant, however, the flash-number dependence of delayed luminescence showed a monotonic increase without oscillation, and FTIR difference spectra of the S-state cycle indicated partial and significant inhibition of the S2 → S3 and S3 → S0 transitions, respectively. These results suggest that the D1-N298A substitution inhibits the proton transfer processes in the S2 → S3 and S3 → S0 transitions. This in turn indicates that the hydrogen-bond network near YZ can be functional as a proton transfer pathway during photosynthetic water oxidation.
内容記述タイプ Abstract
内容記述
内容記述 ファイル公開日: 2018/12/08
内容記述タイプ Other
出版者
出版者 American Society for Biochemistry and Molecular Biology
言語
言語 eng
資源タイプ
資源タイプresource http://purl.org/coar/resource_type/c_6501
タイプ journal article
DOI
関連識別子
識別子タイプ DOI
関連識別子 http://doi.org/10.1074/jbc.M117.815183
ISSN
収録物識別子タイプ ISSN
収録物識別子 0021-9258
書誌情報 Journal of Biological Chemistry

巻 292, 号 49, p. 20046-20057, 発行日 2017-12-08
著者版フラグ
値 publisher
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