U.S.-Japan Cooperative Science: Structure-Function Relationship in Hyperthermostable, Archaeal Rieske- Type Proteins

美日合作科学：超热稳定古菌 Rieske 型蛋白质的结构与功能关系

• 批准号: 9910113
• 负责人: Sergei Dikanov
• 金额: $ 4.88万
• 依托单位: University of Illinois at Urbana-Champaign
• 依托单位国家: 美国
• 项目类别: Standard Grant
• 财政年份: 2000
• 资助国家: 美国
• 起止时间: 2000-07-15 至 2006-06-30
• 项目状态: 已结题
• 来源: https://www.nsf.gov/awardsearch/showAward?AWD_ID=9910113&HistoricalAwards=false
• 关键词: U.S.; Japan; Cooperative; Science; Structure

9910113DikanovThis award supports a three year collaborative research project between Professor Sergei Dikanov of the University of Illinois, Urbana-Champaign and Professor Toshio Iwasaki of the Nippon Medical School in Tokyo, Japan. The researchers will be undertaking a study of the structure-function relationship in hyperthermostable archael Rieske type protein. Iron-sulfur (Fe-S) proteins, widely represented in nature, exhibit reversible oxidation-reduction between different oxidation states of the iron-sulfur cluster. Because iron-sulfur proteins are engaged in electron transport, the redox potentials of the clusters are among the principal characteristics of their biological function. The project is devoted to the study structure-function relationships in two hyperthermostable, archael Rieske-type proteins: a) sulredoxin (SDX) of Sulfolobus sp. Strain 7; and b) archaeal Rieske-type ferredoxin (ARF) from a closely related organism, Sulfolobus solfataricus by advanced magnetic resonance techniques. It is proposed to investigate samples of reduced SDX and ARF as well as their mutants, to compare with the Rieske center in cytochrome bc1 complex, whose X-ray structure is available, and to characterize the cluster environment in detail including coordination of histidine and cysteine ligands, presence of hydrogen bonds and noncoordinated nitrogens, and accessibility of the solvent. The project brings together the efforts of two laboratories that have complementary expertise and research capabilities. Results of the research will provide fundamental information about the structural factors controlling the redox potentials in hyperthermostable, iron-sulfur proteins, and will have far reaching consequences in both basic and applied energy conversion systems involving more complex metallo-enzymes. The research would also have an impact across a wide spectrum of disciplines. This research advances international human resources through the participation of postdocs and graduate students. Through the exchange of ideas and technology, this project will broaden our base of basic knowledge and promote international understanding and cooperation. The researchers plan to publish results of the research in scientific journals and report on the findings at scientific meetings. The results will also be available on the www home page of the Illinois EPR center: http://ierc.scs.uiuc.edu and at the Center for Biophysics at the University of Illinois at: http://www.life.uiuc.edu/crofts/bc_complex_site9910113DikanovThis award supports a three year collaborative research project between Professor Sergei Dikanov of the University of Illinois, Urbana-Champaign and Professor Toshio Iwasaki of the Nippon Medical School in Tokyo, Japan. The researchers will be undertaking a study of the structure-function relationship in hyperthermostable archael Rieske type protein. Iron-sulfur (Fe-S) proteins, widely represented in nature, exhibit reversible oxidation-reduction between different oxidation states of the iron-sulfur cluster. Because iron-sulfur proteins are engaged in electron transport, the redox potentials of the clusters are among the principal characteristics of their biological function. The project is devoted to the study structure-function relationships in two hyperthermostable, archael Rieske-type proteins: a) sulredoxin (SDX) of Sulfolobus sp. Strain 7; and b) archaeal Rieske-type ferredoxin (ARF) from a closely related organism, Sulfolobus solfataricus by advanced magnetic resonance techniques. It is proposed to investigate samples of reduced SDX and ARF as well as their mutants, to compare with the Rieske center in cytochrome bc1 complex, whose X-ray structure is available, and to characterize the cluster environment in detail including coordination of histidine and cysteine ligands, presence of hydrogen bonds and noncoordinated nitrogens, and accessibility of the solvent. The project brings together the efforts of two laboratories that have complementary expertise and research capabilities. Results of the research will provide fundamental information about the structural factors controlling the redox potentials in hyperthermostable, iron-sulfur proteins, and will have far reaching consequences in both basic and applied energy conversion systems involving more complex metallo-enzymes. The research would also have an impact across a wide spectrum of disciplines. This research advances international human resources through the participation of postdocs and graduate students. Through the exchange of ideas and technology, this project will broaden our base of basic knowledge and promote international understanding and cooperation. The researchers plan to publish results of the research in scientific journals and report on the findings at scientific meetings. The results will also be available on the www home page of the Illinois EPR center: http://ierc.scs.uiuc.edu and at the Center for Biophysics at the University of Illinois at: http://www.life.uiuc.edu/crofts/bc_complex_site

9910113 Dikanov该奖项支持伊利诺伊大学厄巴纳-香槟分校的Sergei Dikanov教授和日本东京日本医学院的Toshio Iwasaki教授之间为期三年的合作研究项目。 研究人员将对超热稳定archael Rieske型蛋白质的结构-功能关系进行研究。 铁硫蛋白是自然界中广泛存在的一类蛋白质，其不同氧化态的铁硫簇之间存在可逆的氧化还原反应。 由于铁硫蛋白参与电子传递，簇的氧化还原电位是其生物学功能的主要特征之一。 该项目致力于通过先进的磁共振技术研究两种超热稳定的古细菌Rieske型蛋白质的结构-功能关系：a）硫化叶菌菌株7的硫氧还蛋白（SDX）;和B）来自密切相关的生物体硫磺硫化叶菌的古细菌Rieske型铁氧还蛋白（ARF）。 建议调查样品的减少SDX和ARF以及它们的突变体，比较与Rieske中心的细胞色素bc 1复合物，其X-射线结构是可用的，并详细表征集群环境，包括组氨酸和半胱氨酸配体的协调，存在的氢键和非协调氮，和溶剂的可及性。该项目汇集了两个具有互补专业知识和研究能力的实验室的努力。研究结果将提供有关控制超耐热铁硫蛋白氧化还原电位的结构因素的基本信息，并将在涉及更复杂金属酶的基础和应用能量转换系统中产生深远影响。 这项研究还将对广泛的学科产生影响。 本研究通过博士后和研究生的参与促进国际人力资源。 通过交流思想和技术，该项目将扩大我们的基础知识，促进国际理解与合作。 研究人员计划在科学期刊上发表研究结果，并在科学会议上报告研究结果。 研究结果也将在伊利诺斯州EPR中心的www主页上公布：http://ierc.scs.uiuc.edu和伊利诺斯大学生物物理学中心http://www.life.uiuc.edu/crofts/bc_complex_site9910113DikanovThis奖项支持伊利诺伊大学厄巴纳-香槟分校的Sergei Dikanov教授和日本东京日本医学院的Toshio Iwasaki教授之间为期三年的合作研究项目。 研究人员将对超热稳定archael Rieske型蛋白质的结构-功能关系进行研究。 铁硫蛋白是自然界中广泛存在的一类蛋白质，其不同氧化态的铁硫簇之间存在可逆的氧化还原反应。 由于铁硫蛋白参与电子传递，簇的氧化还原电位是其生物学功能的主要特征之一。 该项目致力于通过先进的磁共振技术研究两种超热稳定的古细菌Rieske型蛋白质的结构-功能关系：a）硫化叶菌菌株7的硫氧还蛋白（SDX）;和B）来自密切相关的生物体硫磺硫化叶菌的古细菌Rieske型铁氧还蛋白（ARF）。 建议调查样品的减少SDX和ARF以及它们的突变体，比较与Rieske中心的细胞色素bc 1复合物，其X-射线结构是可用的，并详细表征集群环境，包括组氨酸和半胱氨酸配体的协调，存在的氢键和非协调氮，和溶剂的可及性。该项目汇集了两个具有互补专业知识和研究能力的实验室的努力。研究结果将提供有关控制超耐热铁硫蛋白氧化还原电位的结构因素的基本信息，并将在涉及更复杂金属酶的基础和应用能量转换系统中产生深远影响。 这项研究还将对广泛的学科产生影响。 本研究通过博士后和研究生的参与促进国际人力资源。 通过交流思想和技术，该项目将扩大我们的基础知识，促进国际理解与合作。 研究人员计划在科学期刊上发表研究结果，并在科学会议上报告研究结果。 结果也将在伊利诺斯州EPR中心的www主页：http://ierc.scs.uiuc.edu和伊利诺斯大学生物物理中心：http://www.life.uiuc.edu/crofts/bc_complex_site上提供。