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Probing the pigment binding sites in LHCII with resonance Raman spectroscopy: The effect of mutations at S123

文献类型：期刊论文

作者Kish, Elizabeth; Wang, Ke1; Llansola-Portoles, Manuel J.; Ilioaia, Cristian; Pascal, Andrew A.; Robert, Bruno; Yang, Chunhong1
刊名BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS
出版日期2016
卷号1857期号:9页码:1490-1496
关键词Carotenoid Electronic absorption LHCII Lutein Neoxanthin Resonance Raman
ISSN号0005-2728
DOI10.1016/j.bbabio.2016.06.001
文献子类Article
英文摘要Resonance Raman spectroscopy was used to evaluate the structure of light-harvesting chlorophyll (Chl) a/b complexes of photosystem II (LHCII), reconstituted from wild-type (WT) and mutant apoproteins over-expressed in Escherichia coli. The point mutations involved residue 5123, exchanged for either P (S123P) or G (S123G). In all reconstituted proteins, lutein 2 displayed a distorted conformation, as it does in purified LHCII trimers. Reconstituted WT and S123G also exhibited a conformation of bound neoxanthin (Nx) molecules identical to the native protein, while the S123P mutation was found to induce a change in Nx conformation. This structural change of neoxanthin is accompanied by a blue shift of the absorption of this carotenoid molecule. The interactions assumed by (and thus the structure of the binding sites of) the bound Chls b were found identical in all the reconstituted proteins, and only marginally perturbed as compared to purified LHCII. The interactions assumed by bound Chls a were also identical in purified LHCII and the reconstituted WT. However, the keto carbonyl group of one Chl a, originally free-from-interactions in WT LHCII, becomes involved in a strong H-bond with its environment in LHCII reconstituted from the S123P apoprotein. As the absorption in the Q(y) region of this protein is identical to that of the LHCII reconstituted from the WT apoprotein, we conclude that the interaction state of the keto carbonyl of Chl a does not play a significant role in tuning the binding site energy of these molecules. (C) 2016 Elsevier B.V. All rights reserved.
学科主题Biochemistry & Molecular Biology ; Biophysics
出版地AMSTERDAM
电子版国际标准刊号1879-2650
WOS关键词LIGHT-HARVESTING COMPLEX ; PHOTOSYSTEM-II LHCII ; CIS-TRANS ISOMERS ; PHOTOSYNTHETIC BACTERIA ; REACTION CENTERS ; CHLOROPHYLL ; IDENTIFICATION ; SPECTRA ; BACTERIOCHLOROPHYLL ; CONFORMATION
WOS研究方向Science Citation Index Expanded (SCI-EXPANDED)
语种英语
WOS记录号WOS:000382590400015
出版者ELSEVIER
资助机构European Research CouncilEuropean Research Council (ERC)European Commission [267333] ; French Infrastructure for Integrated Structural Biology [ANR-10-INSB-05-01] ; CEA interdisciplinary program Technology for Health (MEDIASPEC project) ; National Basic Research Program of ChinaNational Basic Research Program of China [2011CBA00904] ; Key Research Program of the Chinese Academy of Sciences Grant [KSZD-EW-Z-018]
源URL[http://ir.ibcas.ac.cn/handle/2S10CLM1/25298]  
专题中科院光生物学重点实验室
作者单位1.Univ Paris Saclay, Univ Paris 11, CNRS, Inst Integrat Biol Cell,CEA, F-91198 Gif Sur Yvette, France
2.Chinese Acad Sci, Inst Bot, Key Lab Photobiol, Beijing 100093, Peoples R China
推荐引用方式
GB/T 7714		 Kish, Elizabeth,Wang, Ke,Llansola-Portoles, Manuel J.,et al. Probing the pigment binding sites in LHCII with resonance Raman spectroscopy: The effect of mutations at S123[J]. BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS,2016,1857(9):1490-1496.
APA Kish, Elizabeth.,Wang, Ke.,Llansola-Portoles, Manuel J..,Ilioaia, Cristian.,Pascal, Andrew A..,...&Yang, Chunhong.(2016).Probing the pigment binding sites in LHCII with resonance Raman spectroscopy: The effect of mutations at S123.BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS,1857(9),1490-1496.
MLA Kish, Elizabeth,et al."Probing the pigment binding sites in LHCII with resonance Raman spectroscopy: The effect of mutations at S123".BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS 1857.9(2016):1490-1496.

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来源：植物研究所

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