A rare protein fluorescence behavior where the emission is dominated by tyrosine: case of the 33-kDa protein from spinach photosystem II
文献类型：期刊论文
| 作者 | Ruan, KC; Li, J; Liang, RQ; Xu, CH; Yu, Y; Lange, R; Balny, C |
| 刊名 | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
 |
| 出版日期 | 2002 |
| 卷号 | 293期号:1页码:593-597 |
| 关键词 | fluorescence tyrosine and tryptophan fluorescence hydrophobicity high pressure denaturation |
| 通讯作者 | Balny, C (reprint author), INSERM, U128, IFR 24, CNRS, F-34293 Montpellier 05, France., |
| 英文摘要 | An abnormal fluorescence emission of protein was observed in the 33-kDa protein which is one component of the three extrinsic proteins in spinach photosystem 11 particle (PS II). This protein contains one tryptophan and eight tyrosine residues, belonging to a "B type protein". It was found that the 33-kDa protein fluorescence is very different from most B type proteins containing both tryptophan and tyrosine residues. For most B type proteins studied so far, the fluorescence emission is dominated by the tryptophan emission, with the tyrosine emission hardly being detected when excited at 280 nm. However, for the present 33-kDa protein, both tyrosine and tryptophan fluorescence emissions were observed, the fluorescence emission being dominated by the tyrosine residue emission upon a 280 nm excitation. The maximum emission wavelength of the 33-kDa protein tryptophan fluorescence was at 317 nm, indicating that the single tryptophan residue is buried in a very strong hydrophobic region. Such a strong hydrophobic environment is rarely observed in proteins when using tryptophan fluorescence experiments. All parameters of the protein tryptophan fluorescence such as quantum yield, fluorescence decay, and absorption spectrum including the fourth derivative spectrum were explored both in the native and pressure-denatured forms. (C) 2002 Elsevier Science (USA). All rights reserved. |
| 学科主题 | Biochemistry & Molecular Biology; Biophysics |
| 类目[WOS] | Biochemistry & Molecular Biology ; Biophysics |
| 关键词[WOS] | DERIVATIVE UV-SPECTROSCOPY ; HIGH HYDROSTATIC-PRESSURE ; OXYGEN-EVOLUTION SYSTEM ; DEHYDROGENASE ; DENATURATION |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000175514700090 |
| 版本 | 出版稿 |
| 源URL | [http://202.127.25.143/handle/331003/2415]  |
| 专题 | 上海生化细胞研究所_上海生科院生化细胞研究所 |
| 推荐引用方式 GB/T 7714 | Ruan, KC,Li, J,Liang, RQ,et al. A rare protein fluorescence behavior where the emission is dominated by tyrosine: case of the 33-kDa protein from spinach photosystem II[J]. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS,2002,293(1):593-597. |
| APA | Ruan, KC.,Li, J.,Liang, RQ.,Xu, CH.,Yu, Y.,...&Balny, C.(2002).A rare protein fluorescence behavior where the emission is dominated by tyrosine: case of the 33-kDa protein from spinach photosystem II.BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS,293(1),593-597. |
| MLA | Ruan, KC,et al."A rare protein fluorescence behavior where the emission is dominated by tyrosine: case of the 33-kDa protein from spinach photosystem II".BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS 293.1(2002):593-597. |
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