Optimization mechanism of electron transfer proteins
Optimization mechanism of electron transfer proteins
批准号:
08458214
负责人:
ITOH Shigeru
金额:
$1.34万
依托单位国家:
日本
项目类别:
Grant-in-Aid for Scientific Research (B)
财政年份:
1996
资助国家:
日本
项目状态:
已结题
起止时间:
1996 至 1997
中文摘要
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英文摘要
Optimization mechanisms of intra-protein electron transfer were studied in four systems below. (1) plant photosystems I and II reaction centers. (2) reaction center complexes of green sulfur bacteria. (3) A new type of photosynthetic purple bacteria that uses Zn-containing bacteriochlorophylls. (4) a new type of cyanobacteria that uses chlorophyll d which absorbs far-red light, In all the photosynthetic organisms thus far known, chlorophylls are known to be essential. We, however, showed (1) proteins function to optimize the reaction environment of chlorophylls through quinone-exchange studies in the plant photosystem I and H reaction centers, (2) Zn- bacteriochlorophyll can replace the function of Mg-bacteriochlorophyll in vivo, and (3) chlorophyll d also supports the oxygenic photosynthesis as efficient as that by chlorophyll a. These results indicate that natural photosynthetic systems have more varieties than ever estimated and that the photosynthesis with new types of chlorophylls were enabled by a minor tuning of the protein structure around chlorophylls or quinones inside the reaction center protein.
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Itoh,S.: "Dibromothymoquinone (DBMIB) replaces the function of QA at 77K in the isolated Photosystem II Reaction Center (D1-D2-cytochrome b559) complex" Plant and Cell Physiology. 37. 833-839 (1996)
Itoh,S.:“二溴百里醌 (DBMIB) 在分离的光系统 II 反应中心 (D1-D2-细胞色素 b559) 复合物中取代了 77K 的 QA 功能”《植物和细胞生理学》。
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通讯作者:
Iwaki, M.: "DELTAG_O dependence of the electron transfer rate in the photosynthetic reaction center of plant photosystem I : Natural optimization of reaction between chlorophyll a (AO) and quinone." J.Phys.Chem.100. 10802-10809 (1996)
Iwaki, M.:“植物光系统 I 光合反应中心电子转移速率的 DELTAG_O 依赖性:叶绿素 a (AO) 和醌之间反应的自然优化。”
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Saeki, K.: "Site-specific mutagenesis of Phodobacter capsulatus ferredoxin I,FdxN, that functions in nitrogen fixation-role of extra residues." J.Biol.Chem.271. 31399-31406 (1996)
Saeki, K.:“荚膜光杆菌铁氧还蛋白 I,FdxN 的位点特异性诱变,其在额外残基的固氮作用中发挥作用。”
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通讯作者:
Baba,K.et al.: "Photoinhibition of photosystem I electron transfer activity in isolated photosystem I preparations with different chlorophyll contents." Photosyntesis Research. 347. 121-130 (1996)
Baba,K.等人:“具有不同叶绿素含量的分离光系统 I 制剂中光系统 I 电子转移活性的光抑制。”
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通讯作者:
Saeki,K.: "Site-Specific Mutagenesis of Rhodobacter Capsulatus Ferredoxin I,FdxN,That Functions in Nitrogen Fixation: Role of Extra Residues" J.Biol.Chem.271. 31399-31406 (1996)
Saeki,K.:“荚膜红杆菌铁氧还蛋白 I、FdxN 的位点特异性诱变,在固氮中发挥作用:额外残留物的作用”J.Biol.Chem.271。
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海外基金