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Ammonia Accelerates PSII Photodamage of Cyanobacterium Synechocystis PCC 6803 via oxygen-evolving complex and the Silent psbA1 Gene Contributes it the Resistance to Ammonia Toxicity

Ammonia Accelerates PSII Photodamage of Cyanobacterium Synec...

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中国藻类学会第八次会员大会暨第十六次学术讨论会

作者： Karl Forchhammer Hubei Key Laboratory of Genetic Regulation and Integrative Biology Central China Normal University

＜正＞The effects of ammonia on the photodamage of photosystemⅡ（PSII） and repair of damaged PSII in cyanobacterium Synechocystis *** PCC 6803 were investigated in this *** was shown to accelerate the decrease of PSII activity through a mechanism that directly caused photodamage of PSII,rather than inhibition of the repair of photodamaged *** Dl protein of photosynthetic organisms is known to be rapidly turned over in the light,with the rate being proportional to light intensity. Previous studies indicated that the psbAl gene encoded one form of Dl protein that was not expressed in wild-type Synechocystis *** present investigation shows that its expression is induced by high *** wild-type cells are more resistant to high light and ammonia than a psbAT deficient mutant,indicating that the psbAl gene is not redundant,but could play a role in protection of PSII against high light and ammonia *** thylakoid membranes lost PSII activity upon ammonia treatment,with the oxygen-evolving complex being the primary target for ammonia toxicity.

关键词： Ammonia Photodamage Cyanobacterium oxygen-evolving complex psbA1 Gene

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Model Compounds of the Mn Cluster in oxygen-evolving complex of PSⅡ

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Acta Botanica Sinica 2000年第12期42卷 1249-1252页

作者：陈昌能朱红平黄德光刘秋田中国科学院福建物质结构研究所结构化学国家重点实验室福州350002

Six model compounds have been synthesized and used for probing the structural features of the Mn cluster in oxygen_evolving complex (OEC) of photosystem Ⅱ (PSⅡ). The model compounds contain Mn 2(μ_O) 2 and μ_O_μ_carboxylato di_manganese structural units, which offer Mn—Mn, Mn……Mn, and Mn—O(N) structural parameters consistent with the corresponding data of the OEC in PSⅡ, implying that the Mn cluster in OEC may possess similar structural features. Two model compounds containing halide anion have been used for discussing the binding of Cl - to Mn in PSⅡ. It is suggested that in the five S states, ligand exchange would lead to the ligation of chloride to Mn in the S states with Mn of higher valence.

关键词： photosystem oxygen-evolving complex model compound manganese cluster

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Necessity of structural rearrangements for O-O bond formation between O5 and W2 in photosystemⅡ

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Journal of Energy Chemistry 2021年第6期30卷 436-442,I0011页

作者： Yu Guo Biaobiao Zhang Lars Kloo Licheng Sun Department of Chemistry School of Engineering Sciences in ChemistryBiotechnology and HealthKTH Royal Institute of Technology.S E-10044 StockholmSweden State Key Laboratory of Fine Chemicals Institute of Artificial PhotosynthesisDUT-KTH Joint Education and Research Center on Molecular DevicesDalian University of Technology(DUT)Dalian 116024LiaoningChina Center of Artificial Photosynthesis for Solar Fuels School of ScienceWestlake University.Hangzhou 310024ZhejiangChina

Numerous aspects of the water oxidation mechanism in photosystemⅡhave not been fully elucidated,especially the O-O bond formation ***,a body of experimental evidences have identified the O5 and W2 ligands of the oxygen-evolving complex as the highly probable substrate *** this work,we studied O-O bond formation between O5 and W2 based on the native Mn4 Ca cluster by density functional *** rearrangements before the formation of the S_(4) state were found as a prerequisite for O-O bond formation between O5 and W2,regardless if the suggested pathways involving the typical Mnl(Ⅳ)-O·species or the recently proposed Mn4(Ⅶ)(O)2 *** alternatives for the S2→S_(3) and S_(3)→S_(4) transitions accounting for such required rearrangements are *** findings reflect that the structural flexibility of the Mn4 Ca cluster is essential to allow structural rearrangements during the catalytic cycle.

关键词： Density functional theory oxygen-evolving complex Substrate water OAO bond formation Structural rearrangement

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Inner Envelope CHLOROPLAST MANGANESE TRANSPORTER 1 Supports Manganese Homeostasis and Phototrophic Growth in Arabidopsis

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Molecular Plant 2018年第7期11卷 943-954页

作者： Bin Zhang Chi Zhang Congge Liu Yanping Jing Yuan Wang Ling Jin Lei Yang Aigen Fu Jisen Shi Fugeng Zhao Wenzhi Lan Sheng Luan Nanjing University-Nanjing Forestry University Joint Institute for Plant Molecular Biology College of Life Sciences Nanjing University Nanjing 210093 China The Key Laboratory of Western Resources Biology and Biological Technology College of Life Sciences Northwest University Xi'an China Nanjing University-Nanjing Forestry University Joint Institute for Plant Molecular Biology Key Laboratory of Forest Genetics and BiotechnologyNanjing Forestry University Nanjing 210037 China Department of Plant and Microbial Biology University of California Berkeley CA 94720 USA These authors contributed equally to this article.

Manganese （Mn） is an essential catalytic metal in the Mn-cluster that oxidizes water to produce oxygen dur- ing photosynthesis. However, the transport protein（s） responsible for Mn2＋ import into the chloroplast re- mains unknown. Here, we report the characterization ofArabidopsis CMT1 （Chloroplast Manganese Trans- porter 1）, an evolutionarily conserved protein in the Uncharacterized Protein Family 0016 （UPFO016）, that is required for manganese accumulation into the chloroplast. CMT1 is expressed primarily in green tissues, and its encoded product is localized in the inner envelope membrane of the chloroplast. Disruption of CMT1 in the T-DNA insertional mutant cmtl-1 resulted in stunted plant growth, defective thylakoid stacking, and severe reduction of photosystem II complexes and photosynthetic activity. Consistent with reduced oxy- gen evolution capacity, the mutant chloroplasts contained less manganese than the wild-type ones. In sup- port of its function as a Mn transporter, CMT1 protein supported the growth and enabled Mn2＋ accumula- tion in the yeast cells of Mn2＋-uptake deficient mutant （3smfl）. Taken together, our results indicate that CMT1 functions as an inner envelope Mn transporter responsible for chloroplast Mn2＋ uptake.

关键词： chloroplast inner envelope manganese transporter metal transport oxygen-evolving complex

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