The azido[14C]atrazine photoaffinity technique labels a 34‐kDa protein in Scenedesmus which functions on the oxidizing side of photosystem II

FEBS Letters

Bricker, Terry M.¹  Metz, James G.¹  Seibert, Michael¹ 

[1] Photoconversion Research Branch,Solar Energy Research Institute, Golden, CO 80401, USA

关键词: Oxygen evolution;    Herbicide binding;    Photosystem II;    Azidoatrazine;    Scenedesmus;    LF-1 mutant;    azidoatrazine;    2-azido-4-ethylamino-6-isopropylamino-s-triazine;    Ch1;    chlorophyll;    DCMU;    3-(3;    4-dichlorophenyl)-1;    1-dimethylurea;    LDS;    lithium dodecyl sulfate;    LF-;    low fluorescent;    PAGE;    polyacrylamide gel electrophoresis;    PQ;    plastoquinone;    PS;    photosystem;    QA;    primary PS II quinone acceptor;    QB;    the secondary quinone acceptor of PS II;    WT;    wild type;   

DOI  :  10.1016/0014-5793(85)80768-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

We have used azido[¹⁴C]atrazine to photoaffinity label thylakoids from wild-type (WT) Scenedesmus and a mutant, LF-1, which is blocked on the oxidizing side of photosystem II (PS II). One protein is labeled in each case, at 34 kDa in the WT and 36 kDa in LF-1. Previous comparison of the WT with LF-1 had been used to assign a PS II donor side function to the 34-kDa protein. These results suggest that this photoaffinity technique does not label the herbicide-binding protein involved in electron transfer on the reducing side of PS II.

【 授权许可】

Unknown