A model of the protein–pigment baseplate complex in chlorosomes of photosynthetic green bacteria

被引:0
作者
Marie Ø. Pedersen
Juha Linnanto
Niels-Ulrik Frigaard
Niels Chr. Nielsen
Mette Miller
机构
[1] Aarhus University,Center for Insoluble Protein Structures (inSPIN), Interdisciplinary Nanoscience Center (iNANO)
[2] Aarhus University,Department of Chemistry
[3] University of Jyväskylä,Department of Chemistry
[4] University of Copenhagen,Department of Biology
[5] University of Southern Denmark,Department of Biochemistry and Molecular Biology
来源
Photosynthesis Research | 2010年 / 104卷
关键词
Chlorosome; Baseplate; CsmA; Molecular modeling; Photosynthetic antenna;
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摘要
In contrast to photosynthetic reaction centers, which share the same structural architecture, more variety is found in the light-harvesting antenna systems of phototrophic organisms. The largest antenna system described, so far, is the chlorosome found in anoxygenic green bacteria, as well as in a recently discovered aerobic phototroph. Chlorosomes are the only antenna system, in which the major light-harvesting pigments are organized in self-assembled supramolecular aggregates rather than on protein scaffolds. This unique feature is believed to explain why some green bacteria are able to carry out photosynthesis at very low light intensities. Encasing the chlorosome pigments is a protein-lipid monolayer including an additional antenna complex: the baseplate, a two-dimensional paracrystalline structure containing the chlorosome protein CsmA and bacteriochlorophyll a (BChl a). In this article, we review current knowledge of the baseplate antenna complex, which physically and functionally connects the chlorosome pigments to the reaction centers via the Fenna–Matthews–Olson protein, with special emphasis on the well-studied green sulfur bacterium Chlorobaculum tepidum (previously Chlorobium tepidum). A possible role for the baseplate in the biogenesis of chlorosomes is discussed. In the final part, we present a structural model of the baseplate through combination of a recent NMR structure of CsmA and simulation of circular dichroism and optical spectra for the CsmA–BChl a complex.
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页码:233 / 243
页数:10
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共 140 条
[1]  
Adolphs J(2006)How proteins trigger excitation energy transfer in the FMO complex of green sulfur bacteria Biophys J 91 2778-2797
[2]  
Renger T(2000)Effect of carotenoid biosynthesis inhibition on the chlorosome organization in Photochem Photobiol 71 715-723
[3]  
Arellano JB(2005) strain CL1401 PNAS 102 9306-9310
[4]  
Psencik J(2004)An obligately photosynthetic bacterial anaerobe from a deep-sea hydrothermal vent FEBS Lett 564 274-280
[5]  
Borrego CM(1982)Evolution of photosystem I—from symmetry through pseudo-symmetry to asymmetry Biochim Biophys Acta 680 194-201
[6]  
Beatty JT(2002)Antenna organization and evidence for the function of a new antenna pigment species in the green photosynthetic bacterium Biochemistry 41 14403-14411
[7]  
Overmann J(2007)Selective protein extraction from Science 317 523-526
[8]  
Lince MT(2003) chlorosomes using detergents. Evidence that CsmA forms multimers and binds bacteriochlorophyll Photosynth Res 75 49-55
[9]  
Ben-Shem A(1996)“ Photosynth Res 50 41-59
[10]  
Frolow F(1994) Chloracidobacterium thermophilum”: an aerobic phototrophic acidobacterium Photosynth Res 41 261-275