TY - JOUR
T1 - Spectroscopic properties of LH2 from Thermochromatium tepidum in liposome and detergent micelles
AU - Huo, Yilin
AU - Shi, Ying
AU - Wang, Qinyue
AU - Li, Luoyuan
AU - Yu, Longjiang
AU - Wang, Peng
AU - Zhang, Jianping
AU - Wang, Zhengyu
N1 - Funding Information:
Supported by the National Natural Science Foundation of China(Nos.21273282, 21173265) and the International Cooperation Project Between China and Russia(No.21411130185).
Publisher Copyright:
© 2016, Higher Education Press. All right reserved.
PY - 2016/9/10
Y1 - 2016/9/10
N2 - By the use of dynamic light scattering(DLS), transmission electron microscopy(TEM), UV-Vis and resonance Raman spectroscopy, the properties of LH2 from Thermochromatium(Tch.) tepidum in two detergent micelles and in liposome were studied, respectively. The results show that in LH2-liposome the conformation of spirilloxanthin, an incorporated longer chain carotenoid, is obviously different from that in detergent micelles. The charge state of the terminal groups of detergents or lipids is the key factor affecting the B850 absorption. Generally, the calcium ions cause red-shift of the B850 absorption and hyperchromicity, while the proton has the opposite effect. Based on the amino acid sequence analysis, several amino acid residues on the C-terminus of α apo-protein were proposed to constitute the potential binding site for the calcium ion and proton. Such Ca2+- and H+-regulated changes of B850 absorption might be an adaptive mechanism to the living environment for this species.
AB - By the use of dynamic light scattering(DLS), transmission electron microscopy(TEM), UV-Vis and resonance Raman spectroscopy, the properties of LH2 from Thermochromatium(Tch.) tepidum in two detergent micelles and in liposome were studied, respectively. The results show that in LH2-liposome the conformation of spirilloxanthin, an incorporated longer chain carotenoid, is obviously different from that in detergent micelles. The charge state of the terminal groups of detergents or lipids is the key factor affecting the B850 absorption. Generally, the calcium ions cause red-shift of the B850 absorption and hyperchromicity, while the proton has the opposite effect. Based on the amino acid sequence analysis, several amino acid residues on the C-terminus of α apo-protein were proposed to constitute the potential binding site for the calcium ion and proton. Such Ca2+- and H+-regulated changes of B850 absorption might be an adaptive mechanism to the living environment for this species.
KW - Detergent
KW - Liposome
KW - Peripheral antenna complex LH2
KW - Thermochromatium tepidum
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U2 - 10.7503/cjcu20160277
DO - 10.7503/cjcu20160277
M3 - Article
AN - SCOPUS:84987819645
VL - 37
SP - 1678
EP - 1685
JO - Kao Teng Hsueh Hsiao Hua Heush Hsueh Pao/ Chemical Journal of Chinese Universities
JF - Kao Teng Hsueh Hsiao Hua Heush Hsueh Pao/ Chemical Journal of Chinese Universities
SN - 0251-0790
IS - 9
ER -