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

该奖项支持伊利诺伊大学香槟分校的Sergei Dikanov教授和日本东京医学院的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性古Rieske型蛋白的结构-功能关系进行研究。铁硫（Fe-S）蛋白在自然界中广泛存在，在铁硫簇的不同氧化态之间表现出可逆的氧化还原。因为铁硫蛋白参与电子传递，簇的氧化还原电位是其生物功能的主要特征之一。本项目主要研究两种高温稳定的古生源rieske型蛋白的结构-功能关系：a) Sulfolobus sp.菌株7的sulredoxin (SDX)；b)利用先进的磁共振技术，从一个近缘的生物，solfataricus中分离出rieske型铁氧还蛋白（ARF）。我们拟对SDX和ARF的还原样品及其突变体进行研究，并与细胞色素bc1配合物中的Rieske中心进行比较，后者的x射线结构是可用的，并详细表征团簇环境，包括组氨酸和半胱氨酸配体的配位，氢键和非配位氮的存在，以及溶剂的可及性。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。该研究结果将为控制超热稳定铁硫蛋白氧化还原电位的结构因素提供基础信息，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的影响。这项研究还将在广泛的学科领域产生影响。本研究通过博士后和研究生的参与促进了国际人力资源的发展。通过思想和技术的交流，该项目将扩大我们的基础知识基础，促进国际了解与合作。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。研究结果也可在伊利诺斯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_site9910113DikanovThis上获得。该奖项支持伊利诺斯大学厄巴纳-香槟分校的Sergei Dikanov教授和日本东京医学院的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性古Rieske型蛋白的结构-功能关系进行研究。铁硫（Fe-S）蛋白在自然界中广泛存在，在铁硫簇的不同氧化态之间表现出可逆的氧化还原。因为铁硫蛋白参与电子传递，簇的氧化还原电位是其生物功能的主要特征之一。本项目主要研究两种高温稳定的古生源rieske型蛋白的结构-功能关系：a) Sulfolobus sp.菌株7的sulredoxin (SDX)；b)利用先进的磁共振技术，从一个近缘的生物，solfataricus中分离出rieske型铁氧还蛋白（ARF）。我们拟对SDX和ARF的还原样品及其突变体进行研究，并与细胞色素bc1配合物中的Rieske中心进行比较，后者的x射线结构是可用的，并详细表征团簇环境，包括组氨酸和半胱氨酸配体的配位，氢键和非配位氮的存在，以及溶剂的可及性。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。该研究结果将为控制超热稳定铁硫蛋白氧化还原电位的结构因素提供基础信息，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的影响。这项研究还将在广泛的学科领域产生影响。本研究通过博士后和研究生的参与促进了国际人力资源的发展。通过思想和技术的交流，该项目将扩大我们的基础知识基础，促进国际了解与合作。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。研究结果也可以在伊利诺斯州EPR中心的www主页上找到：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

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