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  1. B. 理工学域; 数物科学類・物質化学類・機械工学類・フロンティア工学類・電子情報通信学類・地球社会基盤学類・生命理工学類
  2. b 10. 学術雑誌掲載論文
  3. 1.査読済論文(理)

Purification of ferredoxins and their reaction with purified reaction center complex from the green sulfur bacterium Chlorobium tepidum

http://hdl.handle.net/2297/1729
http://hdl.handle.net/2297/1729
8719d65e-830b-4ce7-bb99-e3b098bf5f64
名前 / ファイル ライセンス アクション
SC-PR-SEO-T-BBA SC-PR-SEO-T-BBA 2001.pdf (186.6 kB)
Item type 学術雑誌論文 / Journal Article(1)
公開日 2017-10-03
タイトル
タイトル Purification of ferredoxins and their reaction with purified reaction center complex from the green sulfur bacterium Chlorobium tepidum
言語
言語 eng
資源タイプ
資源タイプ識別子 http://purl.org/coar/resource_type/c_6501
資源タイプ journal article
著者 瀨尾, 悌介

× 瀨尾, 悌介

WEKO 15237

瀨尾, 悌介

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Seo, Daisuke

× Seo, Daisuke

WEKO 15055
e-Rad 10339616
金沢大学研究者情報 10339616
研究者番号 10339616

Seo, Daisuke

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Tomioka, Atushi

× Tomioka, Atushi

WEKO 15238

Tomioka, Atushi

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Kusumoto, Noriaki

× Kusumoto, Noriaki

WEKO 15239

Kusumoto, Noriaki

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Kamo, Masaharu

× Kamo, Masaharu

WEKO 15240

Kamo, Masaharu

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Enami, Isao

× Enami, Isao

WEKO 15241

Enami, Isao

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Sakurai, Hidehiro

× Sakurai, Hidehiro

WEKO 15242

Sakurai, Hidehiro

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書誌情報 Biochimica et biophysica acta. Bioenergetics

巻 1503, 号 3, p. 377-384, 発行日 2001-01-19
ISSN
収録物識別子タイプ ISSN
収録物識別子 0005-2728
DOI
識別子タイプ DOI
関連識別子 https://doi.org/10.1016/s0005-2728(00)00245-0
出版者
出版者 Elsevier Biomedical Press
抄録
内容記述タイプ Abstract
内容記述 Four ferredoxin (Fd) fractions, namely, FdA–D were purified from the green sulfur bacterium Chlorobium tepidum. Their absorption spectra are typical of 2[4Fe–4S] cluster type Fds with peaks at about 385 and 280 nm and a shoulder at about 305 nm. The A385/A280 ratios of the purified Fds were 0.76–0.80. Analysis of the N-terminal amino acid sequences of these Fds (15–25 residues) revealed that those of FdA and FdB completely agree with those deduced from the genes, fdx3 and fdx2, respectively, found in this bacterium (Chung and Bryant, personal communication). The N-terminal amino acid sequences of FdC and FdD (15 residues) were identical, and agree with that deduced from the gene fdx1 (Chung and Bryant, personal communication). The A385 values of these Fds were unchanged when they were stored for a month at −80°C under aerobic conditions and decreased by 10–15% when they were stored for 6 days at 4°C under aerobic conditions, indicating that they are not extremely unstable. In the presence of Fd-NADP+ reductase from spinach, and a purified reaction center (RC) preparation from C. tepidum composed of five kinds of polypeptides, these Fds supported the photoreduction of NADP+ at room temperature with the following Km and Vmax (in μmol NADP+ μmol BChl a−1 h−1): FdA, 2.0 μM and 258; FdB, 0.49 μM and 304; FdC, 1.13 μM and 226; FdD, 0.5 μM and 242; spinach Fd, 0.54 μM and 183. The Vmax value of FdB was more than twice that previously reported for purified RC preparations from green sulfur bacteria.
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