中国科学院机构知识库网格
Chinese Academy of Sciences Institutional Repositories Grid
The negatively charged amino acids in the lumenal loop influence the pigment binding and conformation of the major light-harvesting chlorophyll a/b complex of photosystem II

文献类型:期刊论文

作者Yang, Chunhong2,3; Lambrev, Petar4; Chen, Zhi1,5; Javorfi, Tamas; Kiss, Anett Z.4; Paulsen, Harald3; Garab, Gyoezoe4
刊名BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS
出版日期2008-11
卷号1777期号:11页码:1463-1470
ISSN号0005-2728
关键词Major light-harvesting a/b complex of photosystem II Spectroscopy Mutagenesis Low pH
DOI10.1016/j.bbabio.2008.08.009
文献子类Article
英文摘要The major chlorophyll (Chl) a/b complexes of photosystem II (LHCIIb), in addition to their primary light-harvesting function, play key roles in the organization of the granal ultrastructure of the thylakoid membranes and in various regulatory processes. These functions depend on the structural stability and flexibility of the complexes. The lumenal side of LHCIIb is exposed to broadly variable pH environments, due to the build-up and decay of the pH gradient during photosynthesis. Therefore, the negatively charged amino acids in the lumenal loop might be of paramount importance for adjusting the structure and functions of LHCIIb. In order to clarify the structural roles of these residues, we investigated the pigment stoichiometries, absorption, linear and circular dichroism spectra of the reconstituted LHCIIb complexes, in which the negatively charged amino acids in the lumenal loop were exchanged to neutral ones (E94G, E107V and DIM). The mutations influenced the pigment binding and the molecular architecture of the complexes. Exchanging E94 to G destabilized the 3(10) helix in the lumenal loop structure and led to an acquired pH sensitivity of the LHCIIb structure. We conclude that these amino acids are important not only for pigment binding in the complexes, but also in stabilizing the conformation of LHCIIb at different pHs. (C) 2008 Elsevier B.V. All rights reserved.
WOS关键词MOLECULAR-DYNAMICS ; HIGHER-PLANTS ; THYLAKOID STRUCTURE ; NEOXANTHIN BINDING ; THERMAL-STABILITY ; PROTEIN COMPLEX ; LHCII ; ANTENNA ; STOICHIOMETRY ; MACRODOMAINS
资助项目Marie Curie[MCRTN-CF-2003-505069] ; Hungarian Fund for Basic Research[OTKA K63252] ; Deutsche Forschungsgemeinschaft[00000000] ; National Natural Science Foundation of China[30470149] ; Knowledge Innovation Program of the Chinese Academy of Sciences[KSCX2-YW-R-137] ; EMBO Shortterm Fellowships[ASTF 190-04]
WOS研究方向Biochemistry & Molecular Biology ; Biophysics
语种英语
出版者ELSEVIER SCIENCE BV
WOS记录号WOS:000261080200009
源URL[http://119.78.100.183/handle/2S10ELR8/279441]  
专题中国科学院上海药物研究所
通讯作者Yang, Chunhong
作者单位1.Chinese Acad Sci, Shanghai Inst Biol Sci, Shanghai Inst Mat Med, Ctr Drug Discovery & Design,State Key Lab Drug Re, Beijing 100864, Peoples R China;
2.Chinese Acad Sci, Inst Bot, Key Lab Photosynth & Environm Mol Physiol, Beijing 100093, Peoples R China;
3.Johannes Gutenberg Univ Mainz, Inst Allgemeine Bot, D-55099 Mainz, Germany;
4.Hungarian Acad Sci, Inst Plant Biol, H-6701 Szeged, Hungary;
5.Chinese Acad Sci, Grad Sch, Beijing 100864, Peoples R China
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Yang, Chunhong,Lambrev, Petar,Chen, Zhi,et al. The negatively charged amino acids in the lumenal loop influence the pigment binding and conformation of the major light-harvesting chlorophyll a/b complex of photosystem II[J]. BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS,2008,1777(11):1463-1470.
APA Yang, Chunhong.,Lambrev, Petar.,Chen, Zhi.,Javorfi, Tamas.,Kiss, Anett Z..,...&Garab, Gyoezoe.(2008).The negatively charged amino acids in the lumenal loop influence the pigment binding and conformation of the major light-harvesting chlorophyll a/b complex of photosystem II.BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS,1777(11),1463-1470.
MLA Yang, Chunhong,et al."The negatively charged amino acids in the lumenal loop influence the pigment binding and conformation of the major light-harvesting chlorophyll a/b complex of photosystem II".BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS 1777.11(2008):1463-1470.

入库方式: OAI收割

来源:上海药物研究所

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