Influence of state-2 transition on the proton motive force across the thylakoid membrane in spinach chloroplasts.
The proton motive force (pmf) across the thylakoid membrane is composed of the proton gradient and the membrane potential, which promotes millisecond-delayed light emission (ms-DLE). In this study, the time courses of LHC II phosphorylation and ms-DLE were investigated in spinach chloroplast during State-2 transition. Red light illumination resulted in an exponential rise in LHC II phosphorylation and a biphasic time course of ms-DLE. The phospho-LHC II appeared upon approximately 1 min illumination. The phosphorylation level increased exponentially when illumination was elongated to 20 min. The t((1/2) )of saturated LHC II phosphorylation was estimated 4-5 min under present illumination. During this process, the amplitudes of ms-DLE increased transiently to a maximal amplitude within 0.5 min illumination, and the reached maximum of the fast phase of ms-DLE was approximately 140% of the dark control. Then, ms-DLE decreased from the maximum. After > or =3 min illumination, ms-DLE decreased to a lower level than the dark control. In the presence of uncouplers and inhibitors, the transient increase in the biphasic time course of ms-DLE was removed by nigericin and DCMU, and the sequential decrease was delayed by DCCD. The time course was not affected significantly by valinomycin and DBMIB. Moreover, the level of LHC II phosphorylation was enhanced by nigericin, valinomycin and DCCD, and was inhibited completely by DCMU and partially by DBMIB. Taken together, we proposed that the PS II photochemical activity remained unaffected even with a higher level of LHC II phosphorylation, which was reflected by the effect of DCCD on the time course of ms-DLE. Probably, the evidence of LHC II phosphorylation is the rearrangement of LHC II-PS II complex and the thylakoid, a feedback to light-exposure, rather than the redistribution of excitation energy from PS II to PS I.
Su
Ji-Hu
JH
Institute of Plant Physiology and Ecology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences. jfsu@sippe.ac.cn
Shen
Yun-Kang
YK
D003991:Dibromothymoquinone / Q000494:pharmacology; D004024:Dicyclohexylcarbodiimide / Q000494:pharmacology; D004237:Diuron / Q000494:pharmacology; D004579:Electron Transport / Q000187:drug effects; D007425:Intracellular Membranes / Q000187:drug effects / Q000378:metabolism*; D007476:Ionophores / Q000494:pharmacology; D008027:Light; D045342:Light-Harvesting Protein Complexes / Q000378:metabolism; D009550:Nigericin / Q000494:pharmacology; D010766:Phosphorylation; D018892:Proton-Motive Force / Q000187:drug effects / Q000502:physiology*; D018724:Spinacia oleracea / Q000166:cytology*; D020524:Thylakoids / Q000187:drug effects / Q000502:physiology*; D014634:Valinomycin / Q000494:pharmacology
D007476:Ionophores; D045342:Light-Harvesting Protein Complexes; D014634:Valinomycin; D003991:Dibromothymoquinone; D004024:Dicyclohexylcarbodiimide; D004237:Diuron; D009550:Nigericin