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Specific Ca2+-binding motif in the LH1 complex from photosynthetic bacterium Thermochromatium tepidum as revealed by optical spectroscopy and structural modeling
Ma, Fei2,3; Kimura, Yukihiro1; Yu, Long-Jiang1; Wang, Peng2; Ai, Xi-Cheng2; Wang, Zheng-Yu1; Zhang, Jian-Ping2
2009-03-01
Source PublicationFEBS JOURNAL
ISSN1742-464X
Volume276Issue:6Pages:1739-1749
AbstractNative 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.
Keyword3d Structural Modeling Light-harvesting-reaction Center Core Complex (Lh1-rc) Photosynthetic Purple Bacterium Raman Spectroscopy Thermochromatium (Tch.) Tepidum
DOI10.1111/j.1742-4658.2009.06905.x
Indexed BySCI
Language英语
WOS IDWOS:000264991400023
PublisherWILEY-BLACKWELL
Citation statistics
Cited Times:21[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Identifierhttp://ir.iccas.ac.cn/handle/121111/66032
Collection中国科学院化学研究所
Corresponding AuthorWang, Zheng-Yu
Affiliation1.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
Recommended Citation
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.
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