Secondary structure and thermal stability of the extrinsic 23 kDa protein of photosystem II studied by Fourier transform infrared spectroscopy

被引：18
|
作者：
Zhang, HM
Ishikawa, Y
Yamamoto, Y
Carpentier, R
机构：
[1] Univ Quebec, Grp Rech Energie & Informat Biomol, Trois Rivieres, PQ G9A 5H7, Canada
[2] Okayama Univ, Fac Sci, Dept Biol, Okayama 700, Japan
来源：
FEBS LETTERS | 1998年 / 426卷 / 03期
关键词：
extrinsic protein; Fourier transform infrared; oxygen evolving complex 23; photosystem II; secondary structure;
D O I：
10.1016/S0014-5793(98)00371-8
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
The secondary structure and thermal stability of the extrinsic 23 kDa protein (OEC23) of spinach photosystem II have been characterized in solution between 25 and 75 degrees C using Fourier transform infrared spectroscopy. Quantitative analysis of the amide I band (1700-1600 cm(-1)) shows that OEC23 contains 5% alpha-helix, 37% beta-sheet, 24% turn, and 34% disorder structures at 25 degrees C. No appreciable conformational changes occur below 45 degrees C. At elevated temperatures, the beta-sheet structure is unfolded into the disorder structure with a major conformational transition occurring at 55 degrees C. Implications of these results for the functions of OEC23 in photosystem II are discussed. (C) 1998 Federation of European Biochemical Societies.
引用
收藏
页码：347 / 351
页数：5
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