Elucidation of Ubiquinone-binding Site of Membrane-bound Quinoproteins in Oxidative Bacteria
氧化细菌中膜结合奎宁蛋白的泛醌结合位点的阐明
基本信息
- 批准号:06660113
- 负责人:
- 金额:$ 1.34万
- 依托单位:
- 依托单位国家:日本
- 项目类别:Grant-in-Aid for General Scientific Research (C)
- 财政年份:1994
- 资助国家:日本
- 起止时间:1994 至 1995
- 项目状态:已结题
- 来源:
- 关键词:
项目摘要
This research project was performed by elucidating the ubiquinone-binding sites of membrane-bound quinoproteins of oxidative bacteria, glucose dehydrogenase (GDH) and alcohol dehydrogenase (ADH), which are functioning in the glucose oxidase respiratory chain of Escherichia coli and in the alcohol oxidase respiratory chain of acetic acid bacteria, respectively. GDH is a single peptide quinoprotein which consists of membrane-spanning N-terminal region and large soluble region containing prroloquinoline quinone (PQQ) and thus catalytic site for glucose. By screening specific inhibitors to prevent the reaction of GDH with ubiquinone, we have found several intense inhibitors of capsaicins analogs. Furthermore, we have examined their inhibitory mode for GDH and also the reaction site in the glucose oxidase respiratory chain. The inhibitor spectrum was also compared between GDH and mitochondrial NADH dehydrogenase, suggesting that GDH may have a structure for ubiquinone-binding site rather di … More fferent from NADH dehydrogenase. Now, we have been searching to isolate mutants of GDH insensitive to these inhibitors. Thereafter, we will figure our the amino acid residues and the structure involved in the ubiquinone-binding site by examining DNA sequence and kinetic analysis with mutated GDH.ADH,unlike GDH,is a quinohemoprotein which consists of three different subunits, subunit I containing PQQ and heme c, subunit II having 3 hemes c, and subunit III.By separating and then reconstituting the subunits of ADH,all three subunits have been shown to be required to have ubiquinone reductase activity, and the subunit II to have the ubiquinone-binding site. Furthermore, it has been shown that ADH has ubiquinol oxidase activity as well as ubiquinone reductase activity. By examining the effect of several ubiquinone analogs as the inhibitor and also the substrate, then both sites for ubiquinone oxidation and reduction was shown to have different structure and to be located in regions different from each other within subunit II. Less
本研究项目通过阐明氧化细菌的膜结合醌蛋白、葡萄糖脱氢酶(GDH)和醇脱氢酶(ADH)的泛醌结合位点来进行,所述葡萄糖脱氢酶(GDH)和醇脱氢酶(ADH)分别在大肠杆菌的葡萄糖氧化酶呼吸链和乙酸细菌的醇氧化酶呼吸链中起作用。GDH是一种单肽醌蛋白,由跨膜N端区域和含有脯喹啉醌(PQQ)的大的可溶性区域组成,因此是葡萄糖的催化位点。通过筛选特异性抑制剂来阻止GDH与泛醌的反应,我们已经发现了几种辣椒素类似物的强烈抑制剂。此外,我们还研究了它们对GDH的抑制模式以及葡萄糖氧化酶呼吸链中的反应位点。GDH和线粒体NADH脱氢酶之间的抑制谱也进行了比较,表明GDH可能具有一个泛素结合位点的结构,而不是二聚体。 ...更多信息 与NADH脱氢酶不同。现在,我们一直在寻找分离的GDH突变体对这些抑制剂不敏感。ADH与GDH不同,它是一种醌血红素蛋白,由三个不同的亚基组成,亚基I含有PQQ和血红素c,亚基II含有3个血红素c,亚基III。已经证明,所有三个亚基都需要具有泛醌还原酶活性,并且亚基II需要具有泛醌结合位点。此外,已经表明ADH具有泛醇氧化酶活性以及泛醌还原酶活性。通过研究几种泛醌类似物作为抑制剂和底物的效果,则泛醌氧化和还原的两个位点被证明具有不同的结构,并且位于亚基II内彼此不同的区域。少
项目成果
期刊论文数量(46)
专著数量(0)
科研奖励数量(0)
会议论文数量(0)
专利数量(0)
Kazunobu Matsushita et al.: "Soluble and membrane-bound quinoprotein D-glucose dehydrogenase of the Acinetobacter calcoaceticus ; The binding process of PQQ to the apoenzymes" Biosci. Biotech. Biochem.59. 1548-1555 (1995)
Kazunobu Matsushita 等人:“乙酸钙不动杆菌的可溶性膜结合醌蛋白 D-葡萄糖脱氢酶;PQQ 与脱辅基酶的结合过程”Biosci。
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- 影响因子:0
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K.Sakamoto, H.Miyoshi, K.Matsushita, M.Nakagawa, J.Ikeda, M.Ohshima, O.Adachi, T.Akagi, & H.Iwamura: "Comparison of the structural features of ubiquinone reduction sites between glucose dehydrogenase in Escherichia coli and bovine heart mitochondrial comp
K.Sakamoto、H.Miyoshi、K.Matsushita、M.Nakakawa、J.Ikeda、M.Ohshima、O.Adachi、T.Akagi、
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Kimitoshi Sakamoto et al.: "Comparison of the structural features of ubiquinone reduction sites between glucose dehydrogenase in Escherichia coli and bovine heart mitochondrial complex I" Eur.J.Biochem.(in press). (1996)
Kimitoshi Sakamoto 等人:“大肠杆菌葡萄糖脱氢酶和牛心线粒体复合物 I 之间泛醌还原位点结构特征的比较”Eur.J.Biochem.(出版中)。
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- 影响因子:0
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Kazunobu Matsushita et al.: "Function of multiple heme c moieties in intramolecular electron transport and ubiquinone reduction in the quinohemoprotein alcohol dehydrogenase-cytochromec complex of Gluconobocter suborydans" J. Biol. Chem.271 (in press). No
Kazunobu Matsushita 等人:“Gluconobacter suborydans 的醌血红蛋白醇脱氢酶-细胞色素复合物中多个血红素 c 部分在分子内电子传递和泛醌还原中的功能”J. Biol。
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- 影响因子:0
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Hiroshi Takemura et al.: "Prosthetic Group of Aldehyde Dehydrogenase in Acetic Acid Bacteria Not Pyrroloquinoline Quinone" Bioscience Biotechnology and Biochemistry. 58. 2082-2083 (1994)
Hiroshi Takemura 等人:“乙酸细菌中醛脱氢酶的辅基不是吡咯喹啉醌”生物科学生物技术和生物化学。
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MATSUSHITA Kazunobu其他文献
MATSUSHITA Kazunobu的其他文献
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{{ truncateString('MATSUSHITA Kazunobu', 18)}}的其他基金
Basic Analysis of Oxidative Fermentation of Acetic Acid Bacteriaand Development of Novel Fermentation System
醋酸菌氧化发酵的基础分析及新型发酵体系的开发
- 批准号:
22380054 - 财政年份:2010
- 资助金额:
$ 1.34万 - 项目类别:
Grant-in-Aid for Scientific Research (B)
Quinoprotein Glycerol Dehydrogenase of Acetic Acid Bacteria and 5-Ketogluconate Production
乙酸菌的奎宁蛋白甘油脱氢酶和 5-酮葡萄糖酸生产
- 批准号:
16580061 - 财政年份:2004
- 资助金额:
$ 1.34万 - 项目类别:
Grant-in-Aid for Scientific Research (C)
Molecular Mechanism and Structural Basis of Ubiquinone-Redox Reaction in Bacterial Respiratory Chains
细菌呼吸链中泛醌氧化还原反应的分子机制和结构基础
- 批准号:
12460045 - 财政年份:2000
- 资助金额:
$ 1.34万 - 项目类别:
Grant-in-Aid for Scientific Research (B)
Comparative and Biochemical Studies on Periplasmic Alcohol Oxidase Systems in Pseudomonads and Acetic Acid Bacteria
假单胞菌和乙酸菌周质醇氧化酶系统的比较和生化研究
- 批准号:
10660091 - 财政年份:1998
- 资助金额:
$ 1.34万 - 项目类别:
Grant-in-Aid for Scientific Research (C)
Structure and Function of Quinoprotein Dehydrogenase
醌蛋白脱氢酶的结构和功能
- 批准号:
09044228 - 财政年份:1997
- 资助金额:
$ 1.34万 - 项目类别:
Grant-in-Aid for Scientific Research (B).
Mechanism for Generation and the Physiology of Inactive Form of Alcohol Dehydrogenase in Acetic Acid Bacteria
乙酸菌中乙醇脱氢酶失活形式的产生机制和生理学
- 批准号:
08660114 - 财政年份:1996
- 资助金额:
$ 1.34万 - 项目类别:
Grant-in-Aid for Scientific Research (C)
Functionnal Characters of Alcohol and Methanol Dehydrogenases in the Respiratory Chain of Acetic Acid Bacteria
乙酸菌呼吸链中醇和甲醇脱氢酶的功能特征
- 批准号:
02660122 - 财政年份:1990
- 资助金额:
$ 1.34万 - 项目类别:
Grant-in-Aid for General Scientific Research (C)
Biochemical Study on Terminal Oxidase of Bacterial Respiratory Chain
细菌呼吸链末端氧化酶的生化研究
- 批准号:
62560086 - 财政年份:1987
- 资助金额:
$ 1.34万 - 项目类别:
Grant-in-Aid for General Scientific Research (C)
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Research Grants
Crystallographic Study of a Quinoprotein Electron Transfer System: Methylamine Dehydrogenase
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Crystallographic Study of a Quinoprotein Electron Transfer System: Methylamine Dehydrogenase
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Electrochemical Biosensors Based on Quinoprotein Enzymes
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