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Purification and characterization of ferredoxin–NAD(P)+ reductase from the green sulfur bacterium Chlorobium tepidum
http://hdl.handle.net/2297/1728
http://hdl.handle.net/2297/1728dde49873-aa64-4ae7-8749-c67119899524
| 名前 / ファイル | ライセンス | アクション |
|---|---|---|
SC-PR-SEO-T-BBA 2002 .pdf (720.6 kB)
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| 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 and characterization of ferredoxin–NAD(P)+ reductase 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× Sakurai, Hidehiro |
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| 書誌情報 |
Biochimica et biophysica acta. Protein structure and molecular enzymology 巻 1597, 号 1, p. 123-132, 発行日 2002-01-01 |
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| ISSN | ||||||
| 収録物識別子タイプ | ISSN | |||||
| 収録物識別子 | 0167-4838 | |||||
| DOI | ||||||
| 関連タイプ | isVersionOf | |||||
| 識別子タイプ | DOI | |||||
| 関連識別子 | https://doi.org/10.1016/s0167-4838(02)00269-8 | |||||
| 出版者 | ||||||
| 出版者 | Elsevier Biomedical Press | |||||
| 抄録 | ||||||
| 内容記述タイプ | Abstract | |||||
| 内容記述 | Ferredoxin–NAD(P)+ reductase [EC 1.18.1.3, 1.18.1.2] was isolated from the green sulfur bacterium Chlorobium tepidum and purified to homogeneity. The molecular mass of the subunit is 42 kDa, as deduced by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The molecular mass of the native enzyme is approximately 90 kDa, estimated by gel-permeation chromatography, and is thus a homodimer. The enzyme contains one FAD per subunit and has absorption maxima at about 272, 385, and 466 nm. In the presence of ferredoxin (Fd) and reaction center (RC) complex from C. tepidum, it efficiently catalyzes photoreduction of both NADP+ and NAD+. When concentrations of NADP+ exceeded 10 μM, NADP+ photoreduction rates decreased with increased concentration. The inhibition by high concentrations of substrate was not observed with NAD+. It also reduces 2,6-dichlorophenol-indophenol (DPIP) and molecular oxygen with either NADPH or NADH as efficient electron donors. It showed NADPH diaphorase activity about two times higher than NADH diaphorase activity in DPIP reduction assays at NAD(P)H concentrations less than 0.1 mM. At 0.5 mM NAD(P)H, the two activities were about the same, and at 1 mM, the former activity was slightly lower than the latter. | |||||
| 著者版フラグ | ||||||
| 出版タイプ | AM | |||||
| 出版タイプResource | http://purl.org/coar/version/c_ab4af688f83e57aa | |||||
