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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/2297/17298719d65e-830b-4ce7-bb99-e3b098bf5f64
名前 / ファイル | ライセンス | アクション |
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SC-PR-SEO-T-BBA 2001.pdf (186.6 kB)
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Item type | 学術雑誌論文 / Journal Article(1) | |||||
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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× Seo, Daisuke× Tomioka, Atushi× Kusumoto, Noriaki× Kamo, Masaharu× Enami, Isao× 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 |
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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. |