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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

Hyperfine Sublevel Correlation Spectroscopy Studies of Iron–Sulfur Cluster in Rieske Protein from Green Sulfur Bacterium Chlorobaculum tepidum

http://hdl.handle.net/2237/26261
c3c7a43d-3a55-4fe7-92a2-b516a068e053
名前 / ファイル ライセンス アクション
resub_Rieske_manuscript_forlibrarydocx.pdf resub_Rieske_manuscript_forlibrarydocx.pdf ファイル公開:2018/03/02 (1.4 MB)
Item type 学術雑誌論文 / Journal Article(1)
公開日 2017-05-10
タイトル
タイトル Hyperfine Sublevel Correlation Spectroscopy Studies of Iron–Sulfur Cluster in Rieske Protein from Green Sulfur Bacterium Chlorobaculum tepidum
著者 Nagashima, Hiroki

× Nagashima, Hiroki

WEKO 71398

Nagashima, Hiroki

Search repository
Kishimoto, Hiraku

× Kishimoto, Hiraku

WEKO 71399

Kishimoto, Hiraku

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Mutoh, Risa

× Mutoh, Risa

WEKO 71400

Mutoh, Risa

Search repository
Terashima, Naotaka

× Terashima, Naotaka

WEKO 71401

Terashima, Naotaka

Search repository
Oh-oka, Hirozo

× Oh-oka, Hirozo

WEKO 71402

Oh-oka, Hirozo

Search repository
Kurisu, Genji

× Kurisu, Genji

WEKO 71403

Kurisu, Genji

Search repository
Mino, Hiroyuki

× Mino, Hiroyuki

WEKO 71404

Mino, Hiroyuki

Search repository
権利
権利情報 “This document is the Accepted Manuscript version of a Published Work that appeared in final form in [The Journal of Physical Chemistry B], copyright © American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see [http://pubs.acs.org/articlesonrequest/AOR-aI6FDDWFX3BNHMpYkfAK].”
抄録
内容記述 The magnetic properties of the Rieske protein purified from Chlorobaculum tepidum were investigated using electron paramagnetic resonance and hyperfine sublevel correlation spectroscopy (HYSCORE). The g-values of the Fe2S2 center were gx = 1.81, gy = 1.90, and gz = 2.03. Four classes of nitrogen signals were obtained by HYSCORE. Nitrogens 1 and 2 had relatively strong magnetic hyperfine couplings and were assigned as the nitrogen directly ligated to Fe. Nitrogens 3 and 4 had relatively weak magnetic hyperfine couplings and were assigned as the other nitrogen of the His ligands and peptide nitrogen connected to the sulfur atom via hydrogen bonding, respectively. The anisotropy of nitrogen 3 reflects the different spin density distributions on the His ligands, which influences the electron transfer to quinone.
内容記述タイプ Abstract
出版者
出版者 ACS Publications
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
ISSN
収録物識別子タイプ ISSN
収録物識別子 1520-6106
書誌情報 The Journal of Physical Chemistry B

巻 121, 号 12, p. 2543-2553, 発行日 2017-03-02
著者版フラグ
値 author
URI
識別子 http://doi.org/10.1021/acs.jpcb.6b12968
識別子タイプ DOI
URI
識別子 http://hdl.handle.net/2237/26261
識別子タイプ HDL
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