Two lutein molecules in lhcii have different conformations and functions: insights into the molecular mechanism of thermal dissipation in plants
文献类型：期刊论文
| 作者 | Yan, Hanchi; Zhang, Pingfeng; Wang, Chao; Liu, Zhenfeng; Chang, Wenrui |
| 刊名 | Biochemical and biophysical research communications
 |
| 出版日期 | 2007-04-06 |
| 卷号 | 355期号:2页码:457-463 |
| 关键词 | Lhcii X-ray structure Lutein Conformation Pigment hetero-trimer Non-photochemical quenching |
| ISSN号 | 0006-291X |
| DOI | 10.1016/j.bbrc.2007.01.172 |
| 通讯作者 | Chang, wenrui(wrchang@sun5.ibp.ac.cn) |
| 英文摘要 | When lhcii forms aggregates, the internal conformational changes will result in chlorophyll fluorescence quenching. uncovering the molecular mechanism of this phenomenon will help us to understand how plants dissipate the excess excitation energy through non-photochemical quenching (npq) process. the crystal structure of spinach and pea lhcii have been published, and recently, we solved another crystal structure of lhcii from cucumber at 2.66 angstrom resolution. here we present the first direct structural evidence indicating that the two lutein(lut) molecules bound in each lhcii monomer have different conformations, lut621 has a more twisted conformation than that of lut620. the intimate interaction between the lut620 and chla612/chla611 dimer leads to form a hetero-trimer, which is considered to be a potential quenching site. we also discovered that the dehydration of the lhcii crystals resulted in a notable shrinkage of the crystal unit cell dimensions which was accompanied by a red-shift of the fluorescence emission spectra of the crystals. these phenomena suggest the changes in the crystal packing during dehydration might be the cause of internal conformational changes within lhcii. we proposed a conformational change related npq model based on the structure analysis. (c) 2007 elsevier inc. all rights reserved. |
| WOS关键词 | LIGHT-HARVESTING COMPLEX ; PHOTOSYSTEM-II ; PROTEIN STRUCTURES ; PHOTOPROTECTION ; PHOTOSYNTHESIS ; XANTHOPHYLLS ; RESOLUTION ; DYNAMICS ; ENERGY |
| WOS研究方向 | Biochemistry & Molecular Biology ; Biophysics |
| WOS类目 | Biochemistry & Molecular Biology ; Biophysics |
| 语种 | 英语 |
| WOS记录号 | WOS:000244774700027 |
| 出版者 | ACADEMIC PRESS INC ELSEVIER SCIENCE |
| URI标识 | http://www.irgrid.ac.cn/handle/1471x/2383056 |
| 专题 | 中国科学院大学 |
| 通讯作者 | Chang, Wenrui |
| 作者单位 | 1.Chinese Acad Sci, Inst Biophys, Natl Lab Biomacromol, Beijing 100101, Peoples R China 2.Grad Univ, Chinese Acad Sci, Beijing 100049, Peoples R China |
| 推荐引用方式 GB/T 7714 | Yan, Hanchi,Zhang, Pingfeng,Wang, Chao,et al. Two lutein molecules in lhcii have different conformations and functions: insights into the molecular mechanism of thermal dissipation in plants[J]. Biochemical and biophysical research communications,2007,355(2):457-463. |
| APA | Yan, Hanchi,Zhang, Pingfeng,Wang, Chao,Liu, Zhenfeng,&Chang, Wenrui.(2007).Two lutein molecules in lhcii have different conformations and functions: insights into the molecular mechanism of thermal dissipation in plants.Biochemical and biophysical research communications,355(2),457-463. |
| MLA | Yan, Hanchi,et al."Two lutein molecules in lhcii have different conformations and functions: insights into the molecular mechanism of thermal dissipation in plants".Biochemical and biophysical research communications 355.2(2007):457-463. |
入库方式： iSwitch采集
来源：中国科学院大学
浏览0
下载0
收藏0
其他版本
除非特别说明，本系统中所有内容都受版权保护，并保留所有权利。