Modification of photosystem II activity by protein phosphorylation

FEBS Letters

Hodges, M.¹  Packham, N.K.¹  Barber, J.¹ 

[1] AFRC Photosynthesis Research Group, Imperial College, London SW7 2BB, England

关键词: Protein phosphorylation;    Photosystem II;    Chlorophyll fluorescence;    Herbicide inhibition;    PQ redox state;    Electron transport;    PS;    photosystem;    LHC;    light harvesting chl a/b protein complex;    DCMU;    3-(3;    4-dichlorophenyl)-1;    1-dimethylurea;    DCPIP;    2;    6-dichlorophenol-indophenol;    DPC;    diphenylcarbazide;    Tricine;    N-tris(hydroxymethyl)methylglycine;    F o;    initial chlorophyll fluorescence;    F m;    maximum chlorophyll fluorescence;    F i;    chlorophyll fluorescence at i;    Qa;    primary stable electron acceptor of PS II;    Qb;    secondary stable electron acceptor of PS II;   

DOI  :  10.1016/0014-5793(85)81118-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Phosphorylation of proteins within pea thylakoid membranes decreases photosystem II (PSII) mediated electron transfer at saturating light intensities which, according to changes in room temperature chlorophyll fluorescence transients, is due to a modification in the electron transfer from Q_A to Q_B. However, a previously reported increase in the ability of DCMU to inhibit PS2 electron flow to DCPIP, as a consequence of protein phosphorylation, was not observed, although changes in DCMU efficacy were found to depend upon the redox state of the plastoquinone (PQ) pool.

【 授权许可】

Unknown