NDLI: Low pH-induced conformational changes in 33 kD protein of photosystem II

Content Provider	Springer Nature Link
Author	Weng, Jun Tan, Cuiyan Yu, Yong Ruan, Kangcheng Xu, Chunhe
Copyright Year	2004
Abstract	33 kD protein, located on the lumen side of thylakoid membranes, is one of three extrinsic proteins of photosystem II (PS II). Previous study showed that NBS modification of W241, the only tryptophan in 33 kD protein, is helpful for understanding the function of W241 in maintaining functional conformation of 33 kD protein. In this paper, studies of both circular dichroism and fluorescence spectra showed that upon decreasing pH from 6.2 to 2.5, the conformation of soluble 33 kD protein changed significantly, with an increase or a decrease in percentage of random coil or α-helix and turns. The changes in secondary structures of this protein are pH reversible. After NBS modification at pH 2.5, the conformational change of 33 kD protein was kept fixed. The CD ellipticity at 200 nm for NBS-modified 33 kD protein is much lower than that for control, indicating that the unfolding degree of 33 kD protein was enhanced after the NBS modification. Moreover, the conformational flexibility is lost in NBS-modified 33 kD protein, and the conformational change becomes pH irreversible, indicating that NBS modification blocked the reversibility of conformational change of 33 kD protein. The specific binding capability of NBS-modified 33 kD protein is much lower than that of low pH-treated control. Furthermore, the rebinding of modified protein on PS II membranes cannot restore the activity of oxygen evolution. We suggest that it is low pH but not NBS modification of W241 that leads to the conformational change of 33 kD protein from one functional to another non-functional state. The significant capability of proton transport of 33 kD protein is discussed.
Starting Page	921
Ending Page	925
Page Count	5
File Format	PDF
ISSN	10016538
Journal	Chinese Science Bulletin
Volume Number	49
Issue Number	9
e-ISSN	18619541
Language	English
Publisher	Science in China Press
Publisher Date	2004-01-01
Publisher Place	Beijing
Access Restriction	Subscribed
Subject Keyword	NBS modification 33 kD protein tryptophan functional conformation Science Life Sciences Physics Chemistry/Food Science Earth Sciences Engineering
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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