RUI: Infrared Spectroscopy as a Probe of Molecular Mechanismin the Hydrogenases
RUI:红外光谱作为氢化酶分子机制的探针
基本信息
- 批准号:9723828
- 负责人:
- 金额:$ 15万
- 依托单位:
- 依托单位国家:美国
- 项目类别:Standard Grant
- 财政年份:1997
- 资助国家:美国
- 起止时间:1997-08-01 至 2001-07-31
- 项目状态:已结题
- 来源:
- 关键词:
项目摘要
9723828 Bagley Low temperature infrared difference spectroscopy will be used to delineate the molecular mechanism of hydrogen binding and activation in hydrogenases. Previous infrared spectroscopic studies on the NiFe hydrogenases have shown that this class of enzymes display anomalous, intense infrared bands arising from one intrinsic carbon monoxide molecule and two intrinsic cyanide molecules coordinated to the active site Fe ion. These anomalous infrared signatures will be used for further study of the various redox states of the enzyme; for exploration of the nature of the similarities in the active sites of the NiFe and Fe hydrogenases as detected using infrared spectroscopy; determination of the nature of carbon monoxide binding in the NiFe and Fe hydrogenases; and examination of the role amino acids play in the activation of hydrogen. The overall goal of this work is to understand the mechanism underlying the hydrogenases' ability to split molecular hydrogen into protons and electrons. Understanding this process has important consequences for the development of cheap and stable catalysts for use in hydrogen production and fuel cells. In addition, the development of methodologies for handling infrared samples under strictly anaerobic conditions as required in this research should prove of general utility in infrared studies of other oxygen sensitive metallo-proteins. The research will involve participation of undergraduate students. Participation in this project will afford undergraduate chemistry students a unique opportunity to apply skills and knowledge they have learned so far while contributing to a project in modern physical biochemistry. ***
9723828巴格利低温红外差光谱将用于描绘氢化酶中氢结合和活化的分子机制。 以前的红外光谱研究表明,这类酶显示异常,强烈的红外波段所产生的一个内在的一氧化碳分子和两个内在的氰化物分子协调的活性位点铁离子。 这些异常的红外签名将被用于进一步研究的各种氧化还原状态的酶;探索的性质的相似性的活性位点的NiFe和Fe氢化酶检测使用红外光谱;确定的性质的一氧化碳结合的NiFe和Fe氢化酶;和检查的作用氨基酸在氢的活化中发挥。 这项工作的总体目标是了解氢化酶将分子氢分解为质子和电子的能力的机制。 了解这一过程对于开发用于制氢和燃料电池的廉价且稳定的催化剂具有重要意义。 此外,在严格的厌氧条件下处理红外样品的方法,在这项研究中所需的发展应证明其他氧敏感金属蛋白的红外研究的一般效用。 这项研究将涉及本科生的参与。 参与这个项目将为本科化学学生提供一个独特的机会,应用他们迄今为止学到的技能和知识,同时为现代物理生物化学项目做出贡献。 ***
项目成果
期刊论文数量(0)
专著数量(0)
科研奖励数量(0)
会议论文数量(0)
专利数量(0)
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Kimberly Bagley其他文献
Kimberly Bagley的其他文献
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{{ truncateString('Kimberly Bagley', 18)}}的其他基金
Acquisition of a Step-scan Time-resolved FTIR and pulsed Nd-YAG Pump Laser for Studies of Photo-induced Species in Chemical and Biomolecular Systems
获取步进扫描时间分辨 FTIR 和脉冲 Nd-YAG 泵浦激光器,用于研究化学和生物分子系统中的光诱导物质
- 批准号:
0520826 - 财政年份:2005
- 资助金额:
$ 15万 - 项目类别:
Standard Grant
RUI: Infrared Spectroscopy as a Probe of Active Site Structure and Molecular Mechanism in the Hydrogenases
RUI:红外光谱作为氢化酶活性位点结构和分子机制的探针
- 批准号:
0130905 - 财政年份:2002
- 资助金额:
$ 15万 - 项目类别:
Continuing Grant
Elucidating the Molecular Mechanism of a Ni Hydrogenase: An Infrared Spectroscopic Approach
阐明镍氢化酶的分子机制:红外光谱方法
- 批准号:
9509064 - 财政年份:1995
- 资助金额:
$ 15万 - 项目类别:
Standard Grant
PostDoctoral Research Fellowships in Plant Biology
植物生物学博士后研究奖学金
- 批准号:
8710654 - 财政年份:1987
- 资助金额:
$ 15万 - 项目类别:
Fellowship Award
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- 批准号:
0213356 - 财政年份:2002
- 资助金额:
$ 15万 - 项目类别:
Continuing Grant
RUI: Infrared Spectroscopy as a Probe of Active Site Structure and Molecular Mechanism in the Hydrogenases
RUI:红外光谱作为氢化酶活性位点结构和分子机制的探针
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0130905 - 财政年份:2002
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Continuing Grant
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