%0 Journal Article %T Spectral properties of LH2 exhibit very similar even when heterologously express LH2 with <i>¦Â</i>-subunit fusion protein in <i>Rhodobacter</i> <i>sphaeroides</i> %A Zhiping Zhao %A Xin Nie %A Zongli Hu %A Guoping Chen %A Zaixin Li %A Zhi Zhang %J Advances in Biological Chemistry %P 101-107 %@ 2162-2191 %D 2013 %I Scientific Research Publishing %R 10.4236/abc.2013.31013 %X

Interactions between the light-harvesting subunits and the non-covalently bound photopigments attribute considerably to the spectral properties of photosynthetic bacteria light-harvesting complexes. In our previous studies, we have constructed a novel Rhodobacter sphaeroides expression system. In the present study, we focus on the spectral properties of LH2 when heterologously express LH2 with ¦Â-subunit- GFP fusion protein in Rb. sphaeroides. Near infra-red spectrum of LH2 remained nearly unchanged as measured by spectroscopy. Fluorescence spectrum suggested that the LH2 with ¦Â-subunit-GFP fusion protein complexes still possessed normal activity in energy transfer. However, photopigments contents were significantly decreased to a very low level in the LH2 with ¦Â-subunit-GFP fusion protein complexes compared to that of LH2. FT-IR spectra indicated that interactions between photopigments and LH2 ¦Á/¦Â- subunits appeared not to be changed. It was concluded that the LH2 spectral properties exhibited very similar even when heterologously expressed LH2 b-subunit fusion protein in Rb. sphaeroides. Our present study may supply a new insight into better understand the interactions between light-harvesting subunits and photopigments and bacterial photosynthesis and promote the development of the novel Rb. sphaeroides expression system.

%K LH2 %K Spectral Property %K FT-IR %K Photopigment %U http://www.scirp.org/journal/PaperInformation.aspx?PaperID=28113