PHOTOSYNTHESIS AT DAWN

黎明时的光合作用

• 批准号: 14390051
• 负责人: INOUE Kazuhito
• 金额: $ 8万
• 依托单位: Kanagawa University
• 依托单位国家: 日本
• 项目类别: Grant-in-Aid for Scientific Research (B)
• 财政年份: 2002
• 资助国家: 日本
• 起止时间: 2002 至 2005
• 项目状态: 已结题
• 来源: https://kaken.nii.ac.jp/grant/KAKENHI-PROJECT-14390051/
• 关键词: PHOTOSYNTHESIS; PHOTOSYNTHETIC BACTERIA; PIGMENT; EVOLUTION; CHLOROPHYLL; CYANOBACTERIA; ENERGY METABOLISM; ENVIROMENTAL ADAPTATION; 光合成細; カロテノイド

The origin and evolution of photosynthesis have long remained enigmatic. To probe early evolutionary history of photosynthesis, we have investigated (B)Chl synthesis, biogenesis of photosynthetic apparatus, and electron transport of purple bacteria, green sulfur bacteria, heliobacteria and cyanobacteria. The summary of this study are as follows (Only the main results are shown).(1)Chlorophyll synthesis : A number of genes involved in (B)Chl synthesis were isolated from various phototrophic prokaryote. Homologues of bchF and bchG from green-sulfur bacterium Chlorobium tepidum were introduced and expressed in non-sulfur bacterium Rhodobacter capsulatus and cyanobacteria Synechocystis sp.PCC6803. Novel pigments accumulated in the cells of R.capsulatus and Synechocystis.(2)Biogenesis of photosynthetic apparatus : Assembly factors of Iron-sulfur cluster, IscR and IscS, from C.tepidum were overexpressed and characterized. Ferredoxin and iron-sulfur type RC were isolated from heliobacteria and they supported NADP^+ photoreduction in vitro. Nitrogenase-like enzyme, Dark POR, was isolated from R.capsulatus and characterized its biochemical properties.(3)Electron transport : Bound cytochrome of Rubrivivax gelatinosus belongs tri-heme type, while that of Blastochloris viridis is tetra-heme type. Chimeric RC of R.gelatinosus which contained B.viridis cytochrome subunit was constructed and investigated their electron transport.

光合作用的起源和演变长期以来一直是神秘的。为了探测光合作用的早期进化史，我们已经研究了（b）CHL合成，光合作用仪的生物发生以及紫色细菌的电子转运，绿色硫细菌，螺旋细菌和蓝细菌。这项研究的摘要如下（仅显示主要的结果）。（1）叶绿素合成：（b）Chl合成中涉及的许多基因是从各种光养原原核生物中分离出来的。在非硫细菌杜鹃花杆菌和蓝细菌Sychocystis sp.pcc6803中引入并表达了来自绿色硫细菌绿叶绿色细菌的BCHF和BCHG的同源物。 （2）光合作用设备的生物发生：来自C.tepidum的铁硫簇，ISCR和ISC的组装因子，从c.tepidum过度表达和表征。从地球细菌中分离出铁蛋白和铁硫型RC，并在体外支持NADP^+光摄取。从r.capsulatus中分离出氮酶状的酶，深色POR，并表征其生化特性。（3）电子传输：rubrivivax胶质质量的细胞色素属性属性属性属于三 - 赫米类型，而blastochloris viridis viridis viridis as tetra is tetra is tetra-heme类型。构建并研究了其电子传输的木质体的嵌合rc，其中包含B.viridis cytothrome子单位。

项目成果

Hirabayashi H., Ishi T., Takaichi S., Inoue K., Uehara: "The role of carotenoids in the photoadaptation of the brown-colored sulfur bacterium Chlorobium phaeobacteroides"Photochemistry and photobiology. 79(3)(掲載決定). (2004)

Hirabayashi H.、Ishi T.、Takaichi S.、Inoue K.、Uehara：“类胡萝卜素在棕色硫细菌 Chlorobium phaeobacteroides 的光适应中的作用”光化学和光生物学 79(3)（出版决定）。 ）

Overexpression of the ferredoxin gene located on the downstream of nif operon in the green sulfur bacterium Chlorobium tepidum

绿色硫细菌温绿球菌中nif操纵子下游铁氧还蛋白基因的过表达

• 发表时间: 2005
• 期刊: Photosynthesis : Fundamental Aspects to Global Perspectives (ed by A.van der Est, D.Bruce)
• 作者: Furusawa;T.;Seo;D.;Sakurai;H.;Inoue;K.
• 通讯作者: K.

High-potential iron-sulfur protein (HiPIP) is the major electron donor to the reaction center complex in photosynthetically growing cells of the purple bacteria Rubrivivax gelatinosus.

高电位铁硫蛋白 (HiPIP) 是紫色细菌 Rubrivivax gelatinosus 光合生长细胞中反应中心复合物的主要电子供体。

• 发表时间: 2002
• 期刊: Biochemistry 41
• 作者: Nagashima K.V.P;Matsuura K.;Shimada K;Vermeglio A.
• 通讯作者: Vermeglio A.

Kada S., Koike H., Satoh K., Hase T., Fujita Y.: "Arrest of chlorophyll synthesis and differential decrease of Photosystems I and II in a cyanobacterial mutant lacking light-independent protochlorophyllide reductase"Plant Molecular Biology. 51(2). 225-235

Kada S.、Koike H.、Satoh K.、Hase T.、Fujita Y.：“缺乏光独立的原叶绿素还原酶的蓝藻突变体中叶绿素合成的阻止和光系统 I 和 II 的差异减少”植物分子生物学。

Role of trehalose synthesis pathway in salt tolelance mechanism of Rhodobacter sphaeroides f.sp.denitrificans IL106.

海藻糖合成途径在球形红杆菌反硝化菌IL106耐盐机制中的作用。

• 发表时间: 2005
• 期刊: Arc.Microbiol. 184
• 作者: Makihara F.;Tsuzuki M.;Sato K.;Masuda S.;Nagashima K.V.P.;Abo M.;Okubo A.
• 通讯作者: Okubo A.