THE ACTION OF MERCURY ON THE BINDING OF THE EXTRINSIC POLYPEPTIDES ASSOCIATED WITH THE WATER OXIDIZING COMPLEX OF PHOTOSYSTEM-II

被引：45

作者：

BERNIER, M ^{[1
]}

CARPENTIER, R ^{[1
]}

机构：

[1] UNIV QUEBEC,CTR RECH PHOTOBIOPHYS,TROIS RIVIERES,PQ G9A 5H7,CANADA

来源：

FEBS LETTERS | 1995年 / 360卷 / 03期

基金：

加拿大自然科学与工程研究理事会;

关键词：

PHOTOSYSTEM II; OXYGEN EVOLVING COMPLEX; EXTRINSIC POLYPEPTIDE (16 KDA; 23; KDA; 33; KDA); MERCURY; SULFHYDRYL GROUP;

D O I：

10.1016/0014-5793(95)00101-E

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：

Mercury (Hg2+), a sulfhydryl group reactant, was used to probe structure-function relationships in photosystem II (PSII). In the present work, we investigated the impact of mercury on the polypeptide composition of PSII submembrane preparations. Electrophoretic analysis revealed that the incubation of the membranes in the presence of mercury produces the depletion of a polypeptide of molecular weight of 33 kDa. This polypeptide corresponds to the extrinsic protein EP33 of the oxygen evolving complex removed following urea treatment. However, the two closely related extrinsic polypeptides of 16 and 23 kDa, usually removed concomitantly after urea treatment, remained unaffected after the mercury treatment. These data demonstrated the existence of an intrinsic binding site for EP23. The molecular mode of action of mercury in the oxygen evolving complex of PSII is discussed.

引用

页码：251 / 254

页数：4