Purification and characterization of a new heme-binding protein (hbp59) from the mutant strain dj35 of azotobacter vinelandii
文献类型：期刊论文
| 作者 | Bian, Shao-Min; Wang, Huang-Ping; Zhou, Hui-Na; Zhao, Ying; Zhao, Jian-Feng; Huang, Ju-Fu |
| 刊名 | Journal of integrative plant biology
 |
| 出版日期 | 2007-03-01 |
| 卷号 | 49期号:3页码:336-342 |
| 关键词 | Absorption spectra Azotobacter vinelandii Characterization by matrix-assisted laser desorption ionization time-of-flight (maldi-tof) Circular dichroism spectra and titration Heme-binding protein (hbp59) Mutant strain dj35 Purification |
| ISSN号 | 1672-9072 |
| DOI | 10.1111/j.1672-9072.2006.00372.x |
| 通讯作者 | Huang, ju-fu(jfhuang@ibcas.ac.cn) |
| 英文摘要 | A new protein, an approximately 59-kda monomer containing iron atoms, was first isolated from the mutant strain dj35 of azotobacter vinelandii lipmann. after analysis by matrix-assisted laser desorption ionization time-of-flight mass spectrometry, the protein was identified as the product of a predicted gene. thus, the protein was tentatively called hbp59. its absorption spectra (abs) in the reduced state exhibited three peaks at 421, 517, and 556 nm and the maximal peak was shifted from 421 to 413 nm after exposure of hbp59 to air. the soret circular dichroism (cd) spectrum of hbp59 in the reduced state displayed four positive peaks at 364, 382, 406, and 418 nm and two negative peaks at 398 and 433 nm; the delta epsilon (cd extinction coefficient) values of these peaks were found to be 0.92, 0.58, 0.87, 0.72, -0.65 and -1.12 l/mol per cm, respectively. titration with heme showed that the protein has 0.1 heme molecules/protein molecule. after hbp59 had fully interacted with heme, its maximal abs value and soret cd intensity were increased by approximately 10-fold compared with values before interaction. therefore, it seems that one molecule of hbp59 can be interacted with only one heme. these results indicate that hbp59 contains heme with low spin and may be involved in heme utilization or adhesion. |
| WOS关键词 | CYTOCHROME-C BIOGENESIS ; NITROGEN-FIXATION ; MOFE PROTEIN ; RHIZOBIUM-LEGUMINOSARUM ; ESCHERICHIA-COLI ; CYCHJKL GENES ; IRON ; BACTERIOFERRITIN ; PRODUCTS ; NIFE |
| WOS研究方向 | Biochemistry & Molecular Biology ; Plant Sciences |
| WOS类目 | Biochemistry & Molecular Biology ; Plant Sciences |
| 语种 | 英语 |
| WOS记录号 | WOS:000244645200009 |
| 出版者 | BLACKWELL PUBLISHING |
| URI标识 | http://www.irgrid.ac.cn/handle/1471x/2380336 |
| 专题 | 中国科学院大学 |
| 通讯作者 | Huang, Ju-Fu |
| 作者单位 | 1.Chinese Acad Sci, Key Lab Photosynthesis & Environm Mol Physiol, Inst Bot, Beijing 100093, Peoples R China 2.Fujian Normal Univ, Bioengn Coll, Beijing 350007, Peoples R China 3.Chinese Acad Sci, Grad Sch, Beijing 100039, Peoples R China |
| 推荐引用方式 GB/T 7714 | Bian, Shao-Min,Wang, Huang-Ping,Zhou, Hui-Na,et al. Purification and characterization of a new heme-binding protein (hbp59) from the mutant strain dj35 of azotobacter vinelandii[J]. Journal of integrative plant biology,2007,49(3):336-342. |
| APA | Bian, Shao-Min,Wang, Huang-Ping,Zhou, Hui-Na,Zhao, Ying,Zhao, Jian-Feng,&Huang, Ju-Fu.(2007).Purification and characterization of a new heme-binding protein (hbp59) from the mutant strain dj35 of azotobacter vinelandii.Journal of integrative plant biology,49(3),336-342. |
| MLA | Bian, Shao-Min,et al."Purification and characterization of a new heme-binding protein (hbp59) from the mutant strain dj35 of azotobacter vinelandii".Journal of integrative plant biology 49.3(2007):336-342. |
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来源：中国科学院大学
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