Reconstitution and Organization of Photosynthetic Antenna Protein Complex Bearing Functional Hydrophilic Domains

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In purple photosynthetic bacteria, light-harvesting complex 2 (LH2) and the light harvesting-reaction center complex (LH1-RC) play the key roles of capturing and transferring light energy and subsequent charge separation. These photosynthetic apparatuses form a molecular assembly; however, how the assembly influences the efficiency of energy conversion is not yet clear. To address this issue, direct observation of the assembly at the molecular level is necessary to analyze its function. In this study, we reconstituted photosynthetic membrane proteins into artificial lipid bilayers and directly observed their assembly by AFM. The absorption spectra of the reconstituted proteins showed characteristic Q<sub>y</sub> bands of bacteriochlorophyll <i>a</i> that were identical to those of intact proteins. AFM observation of the reconstituted membranes revealed that LH2 and LH1-RC were successfully assembled into the lipid bilayer, and their observed structures were in good agreement with corresponding crystallographic structures. Specifically, binary proteins, i.e., LH2/LH1-RC and LH2/LH1, which form a densely packed molecular assembly, could be clearly identified at the molecular level by this method of observation. Energy transfer from LH2 to LH1-RC in a reconstituted lipid bilayer was observed by steady-state fluorescence spectroscopy. Enhanced energy transfer was confirmed in the membrane phase compared to that in a homogeneous micellar solution. Such reconstituted molecular assemblies are useful experimental platforms to investigate the relationship between supramolecular arrays and function. [DOI: 10.1380/ejssnt.2011.15]

収録刊行物

  • Chemistry letters

    Chemistry letters 40(11), 1280-1282, 2011-11-05

    公益社団法人 日本表面科学会

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各種コード

  • NII論文ID(NAID)
    10030220327
  • NII書誌ID(NCID)
    AA00603318
  • 本文言語コード
    ENG
  • 資料種別
    SHO
  • ISSN
    03667022
  • データ提供元
    CJP書誌  J-STAGE 
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