ApcD is required for state transition but not involved in blue-light induced quenching in the cyanobacterium Anabaena sp.PCC7120

Pbycobilisomes(PBS) are able to transfer absorbed energy to photosystem I and Ⅱ,and the distribution of light energy between two photosystems is regulated by state transitions.In this study we show that energy transfer from PBS to photosystem I(PSI) requires ApcD.Cells were unable to perform state transitions in the absence of ApcD.The apcD mutant grows more slowly in light mainly absorbed by PBS,indicating that ApcD-dependent energy transfer to PSI is required for optimal growth under this condition.The apcD mutant showed normal blue-light induced quenching,suggesting that ApcD is not required for this process and state transitions are independent of blue-light induced quenching.Under nitrogen fixing condition,the growth rates of the wild type and the mutant were the same,indicating that energy transfer from PBS to PSI in heterocysts was not required for nitrogen fixation.     

pH Dependence of Chlorophyll States, Protein Structures and Function of the PSII Membranes

IntroductionPhotosystem II ( PSII) is a pigment- proteincomplex in the thylakoid membrane. Its reactioncenter( PSII- RC) ,which is composed of D1 andD2 proteins,generates the highly positive oxidantrequired for the oxidation of water by light- drivencharge separation. Water oxidation occurs at theMn4cluster positioned atthe center of the oxygen-evolving complex on the lumenal surface of PSII.In green plants,the highly reactive Mn4cluster isshielded by a number of extrinsic proteins( 33…     

Recombinant PsbF from Synechococcus sp. PCC 7002 forms β:β homodimeric cytochrome b559

All organisms with oxygenic photosynthesis contain two photosystems:photosystem Ⅰ(PSⅠ)and photo-systemⅡ(PSⅡ),The minimal photosystem Ⅱ particles which are photochemically active contain three subunits:D1,D2 and cytochrome b559 (Cyt b559),The function of Cyt b559 remains unclear,We have successfully overxpressed the psbF gene,encoding the β subunit of Cyt b559,from a marine cyanobacterium Synechoccous sp.PCC 7002 as a fusion gene and obtained a redox-active from of Cyt b559,When the N-terminal GST protein of the fusion gene product was removed with thrombin ,the PsbF protein was still redox-active,suggesting that the recombinant PsbF can form dimer in Escherichia coli.The absorption spectra of either the oxidized from or the reduced form of both GST fusion protein and the purified PsbF dimer and the difference Spectra between the two forms are the same as that of the Cyt b559 isolated from the higher plants .Redox titration analysis of recombinant PsbF showed that the mid-point redox potential of the recombinant Cyt b559 was approximately 50 mV, which is close to the low potential of Cyt b559 ,The results are helpful to the understanding of locatlization and function of Cyt b559 on thylakoid membranes.Ⅰ     

弱光和Tris处理条件下PSⅡ放氧核心复合物的损伤

弱光条件下(120μmol·m-2·s-1)用Tris(0.8mol/L,pH6.5～10.0)处理具有放氧活性的PSⅡ核心复合物,可引起33kD锰稳定蛋白的释放和锰复合物的破坏,并导致核心复合物的结构发生明显的改变.温和电泳、SDS-PAGE和双向电泳分析表明,主要是PSⅡ核心复合物的二聚体和单体减少,并且复合物部分解体;除反应中心D1和D2蛋白外,核心天线CP43和CP7的量也减少,33kD锰稳定蛋白要发生降解.避光时,PSⅡ核心复合物不受影响.     

New structure model of oxygen-evolving center and mechanism for oxygen evolution in photosynthesis

So far, many important questions and problems concerning the structure and mechanism of photosynthetic oxygen evolution are still unsolved. On the basis of recent achievements in this field, a new structure model is proposed whereby two H2O molecules bind asymmetrically to two manganese ions (Mn1Ⅱ and Mn4Ⅲ) at the open end of "C" shaped cluster and keep rather large distance. Two histidine residues coordinate to the other two manganese ions in higher oxidation state (Mn2Ⅳ and Mn3Ⅳ ) through their nitrogen atoms of the imidazole. Cl bound as terminal ligand to Mn4Ⅲl is connected to Ca, and the latter is needed to maintain the special configuration of two Mn2O2 units by bridged-oxo and bridged-carboxylate ligands. The whole structure of oxygen evolution center is asymmetry. A new mechanism for oxygen evolution invokes predictions of asymmetric oxidation of two H2O molecules, dynamic structural changes of oxygen e-volving center and indirect proton transport, etc. Only in S2 state, could Mn1Ⅳ = O. intermediate with high oxidation potential be formed. The S2→S3 process occurs with significant structural changes, as well as intramolecular and intermolecular hydrogen transfer. The S3 state corresponds to intermediate of Mn1Ⅳ-O… H… O-Mn4Ⅳ . During S3→ [S4] →S0, the O-O bond is formed only in S4 state. The change of nucleophilic interaction between Cl and manganese ions different oxidation states has consequence for the significant structural changes in H2O oxidation process.     

Effect of calcium ions on the secondary structures of photosystemⅡ and its relations with photoinhibition

Calcium ions play an important role in the oxygen_evolving process of photosystem Ⅱ as demonstrated in many experiments. The changes of the secondary structures of PS Ⅱ induced by the depletion of Ca 2+ were reported. The results indicated that the removal of Ca 2+ led to the transition of α helix to turns and sheet structures. While Ca 2+ was re_added to the media, only the structures changed to turns could be recovered. The protein conformational changes of PS Ⅱ during the donor side photoinhibition induced by the depletion of Ca 2+ were also studied. This showed that the protein conformational changes differed between the control and Ca 2+ _depleted samples in a short period of illumination (within 10 min). However, the changes became similar when the illumination time was increased.     

Bio-rational design of photosystem Ⅱ inhibitors (Ⅰ)──Molecular modeling of cyanoacrylates and ureas in photosystem Ⅱ D1 protein of Pisum sativum

Molecular modeling of cyanoacrylates and ureas with D1 protein of Pisum sativum have been presented. Studies show that these two kinds of inhibitors occupy the similar region in the D1 protein. Cyanoacrylates have more binding sites than ureas, thus they have higher activities.     

Effect of Mn cluster on the formation of superoxide radicals in photoinhibition of photosystem Ⅱ

To further realize the action of superoxide radicals (O₂^{− .}) in photoinhibition of photosystem Ⅱ (PSⅡ), we employed 5,5-dimethyl-1-pyrroline-N-oxide (DMPO) as a spin trap, associated with EPR spectroscopy, to study the effect of illumination time on O₂^{− .} formation during high light photoinhibition in PSⅡ membranes and Mn-depleted PSⅡ membranes. Results indicated that the removal of Mn cluster from PS
membranes has a strong influence on the dynamics of superoxide formation. The relative mechanism was also discussed. These novel findings may further promote the studies of the structure and function of PSⅡ and the mechanism of photoinhibition.