Spectral properties of LH2 exhibit very similar even when heterologously express LH2 with <i>β</i>-subunit fusion protein in <i>Rhodobacter</i><i>sphaeroides</i>
Spectral properties of LH2 exhibit very similar even when heterologously express LH2 with <i>β</i>-subunit fusion protein in <i>Rhodobacter</i><i>sphaeroides</i>作者机构:Bioengineering College Chongqing University Chongqing China School of Chemistry and Pharmaceutical Engineering Sichuan University of Science & Engineering Zigong China
出 版 物:《Advances in Biological Chemistry》 (生物化学进展(英文))
年 卷 期:2013年第3卷第1期
页 面:101-107页
学科分类:1002[医学-临床医学] 100214[医学-肿瘤学] 10[医学]
主 题:LH2 Spectral Property FT-IR Photopigment
摘 要: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 β-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 β-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 β-subunit-GFP fusion protein complexes compared to that of LH2. FT-IR spectra indicated that interactions between photopigments and LH2 α/β- 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.