The structural basis for the difference in absorbance spectra for the FMO antenna protein from various green sulfur bacteria

被引:254
作者
Tronrud, Dale E. [3 ]
Wen, Jianzhong [1 ,2 ]
Gay, Leslie [3 ]
Blankenship, Robert E. [1 ,2 ]
机构
[1] Washington Univ, Dept Biol, St Louis, MO 63130 USA
[2] Washington Univ, Dept Chem, St Louis, MO 63130 USA
[3] Univ Oregon, Howard Hughes Med Inst, Inst Mol Biol, Eugene, OR 97403 USA
关键词
FMO; Bacteriochlorophyll; Crystal structure; Absorbance spectra; Bidentate ligation; STEADY-STATE SPECTRA; PROSTHECOCHLORIS-AESTUARII; BACTERIOCHLOROPHYLL-A; CHLOROBIUM-TEPIDUM; INTEGRAL INTERPRETATION; OPTICAL-SPECTRA; COMPLEX; SPECTROSCOPY; ORIENTATION; EVOLUTION;
D O I
10.1007/s11120-009-9430-6
中图分类号
Q94 [植物学];
学科分类号
071001 ;
摘要
The absorbance spectrum of the Fenna-Matthews-Olson protein-a component of the antenna system of Green Sulfur Bacteria-is always one of two types, depending on the species of the source organism. The FMO from Prosthecochloris aestuarii 2K has a spectrum of type 1 while that from Chlorobaculum tepidum is of type 2. The previously reported crystal structures for these two proteins did not disclose any rationale that would explain their spectral differences. We have collected a 1.3 A... X-ray diffraction dataset of the FMO from Prosthecochloris aestuarii 2K, which has allowed us to identify an additional Bacteriochlorophyll-a molecule with chemical attachments to both sides of the central magnesium atom. A new analysis of the previously published X-ray data for the Chlorobaculum tepidum FMO shows the presence of a Bacteriochlorophyll-a molecule in an equivalent location but with a chemical attachment from only one side. This difference in binding is shown to be predictive of the spectral type of the FMO.
引用
收藏
页码:79 / 87
页数:9
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