Low concentrations of NaHSO_3 enhance NAD(P)H dehydrogenasedependent cyclic photophosphorylation and alleviate the oxidative damage to improve photosynthesis in tobacco

Bisulfite at low concentrations(L-NaHSO3) increases cyclic electron transport around photosystem I(PSI) and photosynthesis.However,little is known regarding the detailed contribution of cyclic electron transport to the promoted photosynthesis by L-NaHSO3.In the present work,we used tobacco mutant defective in ndhC-ndhK-ndhJ(ndhCKJ) to investigate the role of NAD(P)H dehydrogenase(NDH)-dependent cyclic electron transport around PSI in an increase in photosynthesis by L-NaHSO3.After the treatment of tobacco leaves with L-NaHSO3(10 μmol L-1),the NDH-dependent cyclic electron transport,monitored by a transient post-illumination increase in Chl fluorescence and the amount of NDH,was notably up-regulated in wild type(WT).The NDH-dependent cyclic electron transport was severely impaired in ndhCKJ and was not significantly affected by treatment with L-NaHSO3.Accordingly,the NDH-dependent transthylakoid membrane proton gradient(pH),as reflected by the slow phase of millisecond-delayed light emission(ms-DLE),was increased by L-NaHSO3 in WT,but not in ndhCKJ;the enhancement of cyclic photophosphorylation(PSP) activity by L-NaHSO3 was more obvious in WT than ndhCKJ.The accumulation of both superoxide and hydrogen peroxide was reduced in WT when subjected to L-NaHSO3 treatment,but not in ndhCKJ.Furthermore,the increase of photosynthetic O 2 evolution rate by L-NaHSO3 was more significant in WT than in ndhCKJ.We therefore conclude that L-NaHSO3 alleviates the photo-oxidative damage by the enhancement of NDH-dependent cyclic PSP,thereby improving photosynthesis.

ATPG is required for the accumulation and function of chloroplast ATP synthase in Arabidopsis

The subunit Ⅱ of chloroplast ATP synthase is one of the two peripheral stalks, which associates the catalytic CF1 with mem-brane-spanning CFo . Although the structural and functional roles of chloroplast ATP synthase have been extensively examined, the physiological significance of subunit Ⅱ in vivo is still unclear. In this work, we identified one Arabidopsis T-DNA insertion mutant of atpG gene encoding the subunit Ⅱ of chloroplast ATP synthase. The atpg null mutant displayed an albino lethal pheno-type, as it could not grow photoautotrophically. Transmission electron microscopy analysis showed that chloroplasts of atpg lacked the organized thylakoid membranes. Loss of subunit Ⅱ affected the accumulation of CF1-CFo complex, however, it did not seem to have an effect on the CF1 assembly. The light induced ATP formation of atpg was significantly reduced compared with the wild type. Based on these results, we suggested that ATPG was essential for the accumulation and function of chloroplast ATP synthase.

Changes in the transthylakoid proton gradient are caused by the movement of phycobilisomes in the cyanobacterium Synechocystis sp. strain PCC 6803

Phycobilisomes (PBSs) are the main accessory light-harvesting complexes in cyanobacteria and their movement between photosystems (PSs) affects cyclic and respiratory electron transport.However,it remains unclear whether the movement of PBSs between PSs also affects the transthylakoid proton gradient (ΔpH).We investigated the effect of PBS movement on ΔpH levels in a unicellular cyanobacterium Synechocystis sp.strain PCC 6803,using glycinebetaine to immobilize and couple PBSs to photosystem II (PSII) or photosystem I (PSI) by applying under far-red or green light,respectively.The immobilization of PBSs at PSII inhibited decreases in ΔpH,as reflected by the slow phase of millisecond-delayed light emission (ms-DLE) that occurs during the movement of PBSs from PSII to PSI.By contrast,the immobilization of PBSs at PSI inhibited the increase in ΔpH that occurs when PBSs move from PSI to PSII.Comparison of the changes in ΔpH and electron transport caused by the movement of PBSs between PSs indicated that the changes in ΔpH were most likely caused by respiratory electron transport.This will further improve our understanding of the physiological role of PBS movement in cyanobacteria.