中国科学院机构知识库网格
Chinese Academy of Sciences Institutional Repositories Grid
Specific Ca2+-binding motif in the LH1 complex from photosynthetic bacterium Thermochromatium tepidum as revealed by optical spectroscopy and structural modeling

文献类型:期刊论文

作者Ma, Fei2,3; Kimura, Yukihiro1; Yu, Long-Jiang1; Wang, Peng2; Ai, Xi-Cheng2; Wang, Zheng-Yu1; Zhang, Jian-Ping2
刊名FEBS JOURNAL
出版日期2009-03-01
卷号276期号:6页码:1739-1749
关键词3d Structural Modeling Light-harvesting-reaction Center Core Complex (Lh1-rc) Photosynthetic Purple Bacterium Raman Spectroscopy Thermochromatium (Tch.) Tepidum
ISSN号1742-464X
DOI10.1111/j.1742-4658.2009.06905.x
英文摘要Native and Ca2+-depleted light-harvesting-reaction center core complexes (LH1-RC) from the photosynthetic bacterium Thermochromatium (Tch.) tepidum exhibit maximal LH1-Q(y) absorption at 915 and 889 nm, respectively. To understand the structural origins of the spectral variation, we performed spectroscopic and structure modeling investigations. For the 889 nm form of LH1-RC, bacteriochlorophyll a (BChl a) in the native form was found by means of near-infrared Fourier-transform Raman spectroscopy, a higher degree of macrocycle distortion and a stronger hydrogen bond with the beta-Trp(-8) residue. SWISS-MODEL structure modeling suggests the presence of a specific coordination motif of Ca2+ at the C-terminus of the alpha-subunit of LH1, while MODELLER reveals the tilt of alpha- and beta-polypeptides with reference to the structural template, as well as a change in the concentric orientation of BChl a molecules, both of which may be connected to the long-wavelength LH1-Q(y) absorption of the 915 nm form. The carotenoid spirilloxanthin shows a twisted all-trans configuration in both forms of LH1 as evidenced by the resonance Raman spectroscopic results. With regard to the thermal stability, the 915 nm form was shown by the use of temperature-dependent fluorescence spectroscopy to be approximately 20 K more stable than the 889 nm form, which may be ascribed to the specific Ca2+-binding motif of LH1.
语种英语
WOS记录号WOS:000264991400023
出版者WILEY-BLACKWELL
源URL[http://ir.iccas.ac.cn/handle/121111/66031]  
专题中国科学院化学研究所
通讯作者Wang, Zheng-Yu
作者单位1.Ibaraki Univ, Fac Sci, Mito, Ibaraki 3108512, Japan
2.Renmin Univ China, Dept Chem, Beijing, Peoples R China
3.Chinese Acad Sci, Beijing Natl Lab Mol Sci, State Key Lab Struct Chem Unstable & Stable Speci, Inst Chem, Beijing 100864, Peoples R China
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GB/T 7714
Ma, Fei,Kimura, Yukihiro,Yu, Long-Jiang,et al. Specific Ca2+-binding motif in the LH1 complex from photosynthetic bacterium Thermochromatium tepidum as revealed by optical spectroscopy and structural modeling[J]. FEBS JOURNAL,2009,276(6):1739-1749.
APA Ma, Fei.,Kimura, Yukihiro.,Yu, Long-Jiang.,Wang, Peng.,Ai, Xi-Cheng.,...&Zhang, Jian-Ping.(2009).Specific Ca2+-binding motif in the LH1 complex from photosynthetic bacterium Thermochromatium tepidum as revealed by optical spectroscopy and structural modeling.FEBS JOURNAL,276(6),1739-1749.
MLA Ma, Fei,et al."Specific Ca2+-binding motif in the LH1 complex from photosynthetic bacterium Thermochromatium tepidum as revealed by optical spectroscopy and structural modeling".FEBS JOURNAL 276.6(2009):1739-1749.

入库方式: OAI收割

来源:化学研究所

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