Structural characteristics of extra-membrane domains and guanidine hydrochloride-induced denaturation of photosystem 2 core antenna complexes CP43 and CP47

被引:7
作者
Qu, Y. -G.
Gong, Y. -D.
Guo, S. -K.
Li, L. -B.
Kuang, T. -Y.
机构
[1] Chinese Acad Sci, Inst Bot, Photosynth Res Ctr, Key Lab Photosynth & Environm Mol Physiol, Beijing 100093, Peoples R China
[2] Tsing Hua Univ, Dept Biol Sci & Biotechnol, State Key Lab Biomembrane & Membrane Biotechnol, Beijing 100084, Peoples R China
[3] Chinese Acad Sci, Grad Sch, Beijing 100049, Peoples R China
基金
中国国家自然科学基金;
关键词
aromatic amino acid; chlorophyll; circular dichroism; CP43; CP47; denaturation; energy transfer; extra-membrane domain; fluorescence; guanidine hydrochloride; beta-carotene;
D O I
10.1007/s11099-006-0049-y
中图分类号
Q94 [植物学];
学科分类号
071001 ;
摘要
The structural characteristics of the extra-membrane domains and guanidine hydrochloride-induced denaturation of photosystem 2 (PS2) core antenna complexes CP43 and CP47 were investigated using fluorescence emission and circular dichroism (CD) spectra. The extra-membrane domains of CP43 and CP47 possessed a certain degree of secondary and tertiary structure and not a complete random coil conformation. The tertiary structure and the chlorophyll (Chl) a microenvironment of CP47 were more sensitive to guanidine hydrochloride (GuHCl) than that of CP43: Changes in energy transfer from P-carotene to Chl a corresponded well to changes in the tertiary structure while their correlation with changes in the secondary structure was rather poor. Unlike most of water-soluble proteins, both CP43 and CP47 are partly resistant to denaturation induced by guanidine hydrochloride (GuHCl); the denaturation of CP43 or CP47 is not a two-state process. Those features most probably reflect their character as intrinsic membrane proteins.
引用
收藏
页码:447 / 453
页数:7
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